OUScholars Oakwood University

https://ouscholars.oakwood.edu/student-posters/1033/thumbnail.jp

Vanterpool, Elaine

Murangiri, Peris

Oakwood University 
OUScholars 
Student Posters Student Creative Works 
4-2024 
Analysis of FOXC2 variant implicated in diabetes 
Elaine Vanterpool 
Oakwood University, evanterpool@oakwood.edu 
Peris Murangiri 
Oakwood University 
Follow this and additional works at: https://ouscholars.oakwood.edu/student-posters 
Recommended Citation 
Vanterpool, Elaine and Murangiri, Peris, "Analysis of FOXC2 variant implicated in diabetes" (2024). Student 
Posters. 23. 
https://ouscholars.oakwood.edu/student-posters/23 
This Poster is brought to you for free and open access by the Student Creative Works at OUScholars. It has been 
accepted for inclusion in Student Posters by an authorized administrator of OUScholars. 
Analysis of FOXC2 variant implicated in diabetes
Peris Murangiri and Elaine Vanterpool, PhD
Oakwood University
 Department  of Biological Sciences
Huntsville AL, 35896
Diabetes is a chronic health condition that affects the way individuals’ bodies choose to 
breakdown food. In a healthy individual the body breaks down the food you eat into glucose, 
releasing it into the bloodstream. When the glucose levels become too high, the body then signals 
the pancreas to release insulin, which allows the blood sugar to be used as energy. Now in 
individuals who are suffering from diabetes, their bodies can’t make enough insulin, and as a result 
blood sugar levels rise expeditiously. The purpose of this study is to determine the variants 
implicated in one of the major leading killers in the world, known as diabetes. The variant 
identified to be associated with diabetes was FOXC2. FOXC2, which stands for forkhead box C2, 
is a gene member apart of the forkhead box family. In addition, this gene is also considered a 
transcription factor, giving it control over the activity of other genes. Through analysis of FOXC2, 
13 missense mutations were identified, three of which were studied throughout this study. 
Additional analysis tools, SIFT and PolyPhen-2 were utilized to predict the impacts amino acid 
substitutions have on the function of human proteins. SWISS modeling was used to to get a sense 
of how the protein structure looked three-dimensionally. The three missense mutations identified 
were Leu487Pro, Ala189Glu, and Tyr41Phe. Leu487Pro and Tyr41Phe were predicted to be 
tolerated with a score of 0.97, whereas Ala189Glu was predicted to be tolerated with a score of 
0.007. All these mutations were predicted to have a high chance of affecting protein function, with 
a score of 0.0. Gene expression was predominantly identified in the lymphatic endothelial cell, 
reason being why cancer patients with diabetes are more prone to resistance against 
chemotherapeutics.
ABSTRACT
Diabetes is a chronic disease that affects much of the population, being one of the most common killers worldwide. This 
disease occurs when the pancreas can’t produce enough insulin. In other cases, this disease can also occur when the body isn’t 
able to productively use the insulin produced. This can be detrimental to one’s blood glucose level, causing it to rise 
substantially. Once one’s blood glucose level rises too high for the body to maintain, the buildup of glucose in the blood causes 
hyperglycemia, which in turn can be deadly. There are three types of diabetes: type 1, type 2, and gestational diabetes. The 
most common is type 2 diabetes, which is acquired genetically, reason being why individuals with a family history of diabetes 
should watch on what they consume. Individuals with type 2 diabetes make insulin, but the amount of insulin is less than what 
the body is accustomed to. The body produces less insulin due to the body’s acquired resistance to it. Type 1 diabetes is very 
similar to type 2 diabetes, only difference being that the pancreas makes absolutely no insulin. Gestational diabetes is seen 
among pregnant women. Women diagnosed with gestational diabetes can’t produce enough insulin to maintain blood glucose 
levels, but these levels return to normal once they’ve given birth.
In order to identify courses of action to be taken to prevent this disease, and if not prevent make it manageable, the genes 
associated with this disease should be analyzed. Diseases are interesting in a way that they aren’t caused by one specific gene 
expression, but by the way all the genes choose to work together. If a mutation in one gene causes an overexpression, this can 
affect the expression of another gene, in turn causing a domino effect. Additionally, genes such as , may be associated in a 
disease but may not entirely be the cause, it instead may give rise to other diseases.  
INTRODUCTION
Gene Identification                                                          
• FOXC2, which stands for forkhead box C2, is a gene that’s a member of the forkhead box family. In addition, 
this gene is also considered a transcription factor, giving it control over the activity of other genes.
• Its key role is in the regulation of lymphatic endothelial cell differentiation during embryogenesis. In addition, 
this gene also plays an important role in the formation of smooth muscle layers and morphogenesis of 
lymphatic valves, which still takes place during embryogenesis.
                               Protein Homology                                                          
  Prediction of Pathogenicity: SIFT and Polyphen-2                                                                      
The three missense mutations identified were Leu487Pro, Ala189Glu, and Tyr41Phe.
• Leu487Pro missense mutation is uncertain. Polyphen-2 predicts this missense mutation will probably be damaging due to its score of 0.97.
• SIFT predicts Leu487Pro to be tolerated with a score of 0.00.
• Ala189Glu missense mutation is likely benign. Polyphen-2 predicts this missense mutation will be benign due to its score 0.007.
• SIFT predicts Ala189Glu to be tolerated with a score of 0.93.
          
• Tyr41Phe missense mutation is pathogenic. Polyphen-2 predicts this missense mutation will probably be damaging due to its score 0.967.
• SIFT predicts Tyr41Phe to be tolerated with a score of 0.02. 
                               Protein Homology                                                          
The only conserved domain found was the FH domain. This domain is named for the Drosophila 
forkhead protein, which is a transcription factor responsible for promoting terminal development. The 
FH domain is structured containing two flexible “wings” in the C-terminal region.
RESULTS
• Individuals who suffer from diabetes typically don’t 
have healthy diets. These unhealthy diets increase 
FOXC2 levels, which surprisingly enough counteract 
most of the symptoms associated with obesity. These 
symptoms include hypertriglyceridemia and induced 
insulin resistance. Essentially stating that increased 
FOXC2 levels improve the chances of protection 
against type 2 diabetes.
• FOXC2 is an emerging oncogene linked to cancer 
progression. Its drug resistance makes it difficult for 
therapies such as chemotherapeutics to succeed. 
Some factors that drive cancer chemoresistance 
include its promotion of epithelial-mesenchymal 
transition, induction of multidrug transporter, 
deregulation of cell survival signaling pathways, and 
activation of oxidative stress response. FOXC2 is 
linked to cancer due to the factors that drive its 
resistance to chemoresistance, making this gene an 
oncogene. 
DISCUSSION AND 
CONCLUSION
EW;, Hargadon KM;Strong. “The FOXC2 Transcription Factor: A Master Regulator of Chemoresistance in Cancer.” Technology in Cancer Research & 
Treatment, U.S. National Library of Medicine, pubmed.ncbi.nlm.nih.gov/36740986/.
“Home - Protein - NCBI.” National Center for Biotechnology Information, U.S. National Library of Medicine, www.ncbi.nlm.nih.gov/protein/.
Jiang L;Ren W;Xie C;Duan S;Dai C;Wei Y;Luo D;Wang T;Gong B;Liu X;Yang Z;Ye Z;Chen H;Shi Y; “Genetic Landscape of FOXC2 Mutations in 
Lymphedema-Distichiasis Syndrome: Different Mechanism of Pathogenicity for Mutations in Different Domains.” Experimental Eye Research, U.S. 
National Library of Medicine, pubmed.ncbi.nlm.nih.gov/35716761/.
“Model Interactive Workspace.” SWISS, swissmodel.expasy.org/interactive. Accessed 2 Apr. 2024.
“Polyphen-2 Prediction of Functional Effects of Human Nssnps.” PolyPhen-2: Prediction of Functional Effects of Human nsSNPs, 
genetics.bwh.harvard.edu/pph2/.
“Predict Effects of Nonsynonmous / Missense Variants.” SIFT, sift.bii.a-star.edu.sg/. Accessed 2 Apr. 2024.
“Simple Clinvar.” Simple ClinVar, simple-clinvar.broadinstitute.org/.
“The Human Protein Atlas.” The Human Protein Atlas, www.proteinatlas.org/.
Yang J;Liu F;Li Y;Wu D;Zhang Z;Chen S;Deng M;Yang C;Yang J; “Forkhead Box C2 Is Associated with Insulin 
Resistance in Gestational Diabetes Mellitus.” Gynecological Endocrinology : The Official Journal of the 
International Society of Gynecological Endocrinology, U.S. National Library of Medicine, 
pubmed.ncbi.nlm.nih.gov/35532201/.
REFERENCES 
• SWISS modeling was used to get a sense of how the protein structure 
looked three-dimensionally.
• Simple-Clinvar was used in this study to identify the presence of 
FOXC2 in diabetes.
• SIFT and Polypehn-2 were used to help predict the impacts amino acid 
substitutions have on the function of human proteins.
• Polyphen-2 was used to the predict the effect of missense variants 
through amino acid substitution.
• SIFT was used to predict the affect amino acid substitution has on 
protein function.
METHODS
This project was supported by the department 
of Biological Sciences along with Dr. Elaine 
Vanterpool. As well as HudsonAlpha 
Institute of Technology
ACKNOWLEDGEMENTS  


English

Analysis of FOXC2 variant implicated in diabetes​

https://ouscholars.oakwood.edu/student-posters/1028/thumbnail.jp

Browning, Sophia

Oakwood University 
OUScholars 
Student Posters Student Creative Works 
4-2024 
An Analysis of LMNA variants associated with PCOS 
Elaine Vanterpool 
Oakwood University, evanterpool@oakwood.edu 
Sophia Browning 
Oakwood University 
Follow this and additional works at: https://ouscholars.oakwood.edu/student-posters 
Recommended Citation 
Vanterpool, Elaine and Browning, Sophia, "An Analysis of LMNA variants associated with PCOS" (2024). 
Student Posters. 28. 
https://ouscholars.oakwood.edu/student-posters/28 
This Poster is brought to you for free and open access by the Student Creative Works at OUScholars. It has been 
accepted for inclusion in Student Posters by an authorized administrator of OUScholars. 
Figure 1. 
3D Swiss Model Lamin
A/C protein Homology 
An Analysis of LMNA variants associated with PCOS
Sophia Browning and Elaine Vanterpool, PhD
Oakwood University
 Department of Biological Sciences
Huntsville AL, 35896
Polycystic Ovarian Syndrome (PCOS) is a disease commonly characterized by the excessive 
production of male hormones, androgens, the growth of fluid filled cysts within the ovaries 
called and difficulty ovulating. PCOS affects an estimated 8-13% of women worldwide and is 
the foremost cause of infertility and anovulation (World Health Organization). This study's 
purpose is to identify and assess the pathogenicity of LMNA variants associated with PCOS. 
Some genetic mutations responsible for PCOS have been reported. However, studies regarding 
LMNA and its specific role in causing PCOS have been inconclusive. Simple Mendelian 
inheritance patterns cannot be applied to the pathogenesis of this disease as both genetic and 
environmental factors are to be considered. ClinVar, was used to identify the LMNA as a gene 
associated with PCOS and its two variants, single nucleotide missense mutations, p.Arg455Cys 
and p.Arg482Trp. The LMNA gene codes for a lamin A/C protein, a scaffold protein, that is 
vital for maintaining structural integrity, cell signaling and more specifically chain elongation. 
Pathogenic mutations in LMNA are known to alter the expression of certain tissues. The LMNA 
gene is expressed in most somatic tissues including the ovaries. Computational tools PolyPhen 
and Sift were used to determine pathogenicity of the two variants. PolyPhen predicted both 
mutations to likely be damaging while SIFT predicted the p.Arg455Cys variant to be tolerated 
and the p.Arg455Cys to be damaging. The pathogenicity of these mutations suggests that 
functionality of the lamina A/C protein was affected, potentially affecting gene expression and 
DNA replication within the ovaries. Previous studies have suggested pathogenic mutations in 
LMNA to be associated with PCOS as they have been widely implicated in insulin resistance, a 
phenomenon often observed in those with PCOS. However, a conclusive result has not been 
reached. This study contributes to the existing research regarding implications of the LMNA 
gene associated with PCOS.
ABSTRACT
INTRODUCTION
RESULTS
• Previous studies have hypothesized that variants of the LMNA gene 
are associated with PCOS (Bauer et al., 2023, p. A879). Mutations in 
this gene have been implicated in Familial partial lipodystrophy type 2 
(FPLD2), a disease characterized by Insulin Resistance and issues 
with lipid storage. Pathogenic LMNA variants known to cause FPLD2 
are found in the highly conserved, intermediate filament region of the 
lamin A/C protein. In one study,  researchers sequenced the LMNA 
gene in 602 women with PCOS and 125 reproductively healthy 
women. Seven missense variants were identified in 8 cases and zero in 
the reproductive healthy controls. This study concluded that LMNA 
variants are to be further established as a mechanism in the 
pathogenesis of PCOS (Bauer et al., 2023, p. A890).
• In another such study, researchers re-sequenced three regions of the 
Lamin A/C protein, including the coding region, in 43 women with a 
phenotypic presentation of PCOS similar to FPLD2 (Urbanek et al., 
2009). They identified 56 variants and tested for association between 
the variants and PCOS. They found no significant evidence for 
association of the variants with PCOS (Urbanek et al., 2009). 
However, this study was done exclusively on women of European 
descent. And genetic variants in Lamin A/C are not common in 
Caucasian women with PCOS. Further research should be done on a 
test group with greater racial diversity.
• As PCOS and FPLD2 share the common characteristic of Insulin 
Resistance it is may be hypothesized that pathogenic mutations in the 
LMNA gene are play a role in Insulin resistance.
• Insulin Resistance is linked to increased androgen secretion which 
leads to hyperandrogenism, the defining characteristic of PCOS.
• This research contributes to the existing data regarding implications of 
the LMNA gene in PCOS. This work is important because there are 
several widely known genes that play a role in the pathogenesis of 
PCOS. However, little data exists on the role of less frequent genes 
such as LMNA. The identification of mutations in this gene could 
expand treatment and understanding of PCOS in those with this 
genotype.
DISCUSSION AND 
CONCLUSION
•Bauer, R., Gorsic, L., Legro, R. S., Ehrmann, D., Geoffrey Hayes, M., & Urbanek, M. (2023). Fri458 rare 
pathogenic missense variants in lmna identified in women with polycystic ovary syndrome(Pcos). Journal of the 
Endocrine Society, 7(Suppl 1), bvad114.1645. https://doi.org/10.1210/jendso/bvad114.1645
•Harada, M. (2022). Pathophysiology of polycystic ovary syndrome revisited: Current understanding and 
perspectives regarding future research. Reproductive Medicine and Biology, 21(1), e12487. 
https://doi.org/10.1002/rmb2.12487
•Polycystic ovary syndrome. (n.d.-a). [Text]. Retrieved April 3, 2024, from 
https://medlineplus.gov/polycysticovarysyndrome.html
•Polycystic ovary syndrome. (n.d.-b). Retrieved April 3, 2024, from https://www.who.int/news-room/fact-
sheets/detail/polycystic-ovary-syndrome
•Polycystic ovary syndrome (Pcos)—Symptoms and causes. (n.d.). Mayo Clinic. Retrieved April 3, 2024, from 
https://www.mayoclinic.org/diseases-conditions/pcos/symptoms-causes/syc-20353439
•Polycystic ovary syndrome(Pcos). (2022, February 28). https://www.hopkinsmedicine.org/health/conditions-and-
diseases/polycystic-ovary-syndrome-pcos
•Urbanek, M., Nampiaparampil, G., D’Souza, J., Sefton, E., Ackerman, C., Legro, R. S., & Dunaif, A. (2009). The 
role of genetic variation in the lamin a/c gene in the etiology of polycystic ovary syndrome. The Journal of 
Clinical Endocrinology and Metabolism, 94(7), 2665–2669. https://doi.org/10.1210/jc.2008-2704
Figure 1. 
3D Swiss Model Lamin A/C 
Protein homology
REFERENCES 
METHODS
Special thanks to Dr. Elaine Vanterpool, the Department of Biological 
Sciences at Oakwood University and HudsonAlpha Institute for 
Biotechnology.
ACKNOWLEDGEMENTS  
ClinVar was 
used to explore 
and identify 
LMNA variants 
(single 
nucleotide 
missense 
mutations) 
associated with 
PCOS and 
evaluate the 
conserved 
domains.
Computational 
tools PolyPhen 
and SIFT were 
used to predict the 
pathogenicity and 
impact on protein 
function of the 
two single 
nucleotide 
missense 
mutations.
SWISS Model 
was used to 
obtain 3D 
protein 
homology.
Literature 
review was 
conducted to 
learn more 
about the 
LMNA gene, 
PCOS and 
how the two 
are related.
Endocrine disorder commonly characterized by the 
excessive production of male hormones, androgens 
by the ovaries and/or adrenal glands. This 
overproduction of androgens may result in excess 
body hair, facial hair, acne, weight gain and 
infertility.
Progesterone and estrogen levels may be 
insufficient to regulate the release of the 
Gonadotropin Releasing Hormone 
(GnRH) causing an increase in levels of 
the Luteinizing Stimulating Hormone 
(LSH). This results in an imbalance of 
FSH to LSH which is responsible for the 
abnormal growth of follicles and 
hypersecretion of androgens (Harada, 
2022, p.2). 
Growth of fluid 
filled cysts within 
the ovaries 
(follicles) 
containing 
immature eggs not 
released during 
ovulation.
Insulin Resistance is often seen, result of 
hyperandrogenism. Condition prevents the body from 
using Insulin, hormone necessary for uptake of glucose by 
cells, the main source of energy in the body. While Insulin 
is produced it begins to build up. Since, is not being used 
the body produces more insulin in attempt to maintain 
blood sugar levels. This excess of insulin, 
hyperinsulinemia results in further hyperandrogenism — 
the two conditions worsen in a feedback loop worsening 
symptoms of PCOS. 
This disease affects an 
estimated 8-13% of 
women worldwide and is 
the foremost cause of 
infertility and anovulation 
(WHO).
Polycystic 
Ovarian 
Syndrome
Codes for the Lamin A/C protein which :
• Maintains structural integrity of cell form (a part of the nuclear lamina)
• Acts as scaffold for regulatory proteins that oversee DNA synthesis, cell cycle and gene expression
• Mutations in this protein have been linked to laminopathies, the pathogenic damage and alteration of somatic 
tissues.
• Is highly conserved in the tail region which contains IgG fold necessary for binding an elongation factor needed 
for chain elongation, formation of a polypeptide chain, in DNA replication     
About the 
LMNA 
gene
Prediction of Pathogenicity : PolyPhen and Sift
LMNA Variant 1: Arg455Cys LMNA Variant 2: Arg482Trp
Figure 2. Prediction of Arg455Cys by SIFT
• SIFT predicted the single nucleotide missense mutation 
occurring at position 455 from Arginine to Cysteine to be 
tolerated with a score of 0.05
Figure 3. Prediction of Arg482Trp by SIFT
• SIFT predicted the single nucleotide missense mutation occurring at 
position 482 from Arginine to Tryptophan to AFFECT PROTEIN 
FUNCTION with a score of 0.00
Figure 4. Prediction of Arg455Cys by PolyPhen
• PolyPhen predicted the single nucleotide missense mutation occurring 
at position 455 from Arginine to Cysteine to be possibly damaging 
with a score of 1.000
Figure 5.  Prediction of Arg482Trp by PolyPhen
• PolyPhen predicted the single nucleotide missense mutation occurring 
at position 482 from Arginine to Tryptophan to be possibly damaging 
with a score of 0.999
Figure 6.  Expression of Lamin A/C protein in various tissues. 
• This gene has high expression in several somatic tissues 
including the : gallbladder, stomach, and skin. It is expressed 
proficiently in the ovaries.
\\
Figure 7. Conserved Domain of Lamin A/C protein
The Lamin A/C protein is highly conserved in the intermediate filament region and the tail region which 
contains an IgG fold important for the binding of  an elongation factor (proliferating cell nuclear antigen). 
This factor is needed for chain elongation in the formation of a polypeptide chain during DNA replication.
\\


An Analysis of LMNA variants associated with PCOS​

https://ouscholars.oakwood.edu/student-posters/1042/thumbnail.jp

Willis, Danielle

Oakwood University 
OUScholars 
Student Posters Student Creative Works 
4-2024 
Study on KANSL1 gene mutation and its association to diabetes 
Elaine Vanterpool 
Oakwood University, evanterpool@oakwood.edu 
Danielle Willis 
Oakwood University 
Follow this and additional works at: https://ouscholars.oakwood.edu/student-posters 
Recommended Citation 
Vanterpool, Elaine and Willis, Danielle, "Study on KANSL1 gene mutation and its association to diabetes" 
(2024). Student Posters. 40. 
https://ouscholars.oakwood.edu/student-posters/40 
This Poster is brought to you for free and open access by the Student Creative Works at OUScholars. It has been 
accepted for inclusion in Student Posters by an authorized administrator of OUScholars. 
Study on KANSL1 gene mutation and its association to diabetes
Danielle Willis and Elaine Vanterpool, PhD
Oakwood University
Department of Biological Sciences
Huntsville AL, 35896
•Diabetes is a chronic health condition affecting millions worldwide, it disrupts the body's ability to regulate blood sugar 
levels effectively. The process begins with the breakdown of food into glucose, which is then released into the bloodstream. 
Normally, the pancreas responds by secreting insulin, a hormone that facilitates the entry of glucose into cells for energy 
production. However, in diabetes, this process is compromised. The purpose of this study is to minimize the chances of 
developing the disease and understand and reduce the mortality of those with the disease. The gene I chose is KANSL1. 
Simple Clinvar was used to identify genes associated with diabetes. KANSL1 was identified to be associated with this disease. 
Polyphen 2 sift and swiss model was  used to analyze the data. Clinvar determined the protein mapping and pathogenic state 
of KANSL1 and its mutations. The purpose of this study is to provide research to the medical community and potentially treat 
this disease. 
ABSTRACT
KANSL1 encodes a nuclear protein that is a subunit of two protein 
complexes involved with histone acetylation, the MLL1 complex and 
the NSL1 complex. The encoded protein has been implicated in a 
variety of cellular processes including enhancer regulation, cell 
proliferation, and mitosis. 
INTRODUCTION
RESULTS
Diabetes is an chronic health condition that disrupts the 
body's ability to regulate blood sugar levels effectively. 
The gene I choose KANSL1. This gene was associated 
with diabetes when put through simple clinvar. The 
research gathered was able to determine the gene had a 
mutation and  is pathogenic  
DISCUSSION AND 
CONCLUSION
•Kansl1 Kat8 regulatory NSL complex subunit 1 [homo sapiens (human)] - gene - 
NCBI. (n.d.). Retrieved from https://www.ncbi.nlm.nih.gov/gene/284058
•Simple clinvar. (n.d.). Retrieved from https://simple-clinvar.broadinstitute.org/
REFERENCES 
•Simple Clinvar was used find the gene associated 
with diabetes 
•Polyphen 2- FATSA sequence from simple clinvar 
used to analyze variants 
•Sift was used to determine if amino acid would 
affect proteins function 
•Swiss Modeling was used to develop an 3D model 
of the structure of the protein. 
METHODS
•I would like to thank Dr. Vanterpool for 
guiding me through this project.
ACKNOWLEDGEMENTS  


Study on KANSL1 gene mutation and its association to diabetes​

https://ouscholars.oakwood.edu/student-posters/1037/thumbnail.jp

Nkurunziza, Joseph

Oakwood University 
OUScholars 
Student Posters Student Creative Works 
4-2024 
Mutation in PAX3 Gene that leads to Albinism. 
Elaine Vanterpool 
Oakwood University, evanterpool@oakwood.edu 
Joseph Nkurunziza 
Oakwood University 
Follow this and additional works at: https://ouscholars.oakwood.edu/student-posters 
Recommended Citation 
Vanterpool, Elaine and Nkurunziza, Joseph, "Mutation in PAX3 Gene that leads to Albinism." (2024). 
Student Posters. 45. 
https://ouscholars.oakwood.edu/student-posters/45 
This Poster is brought to you for free and open access by the Student Creative Works at OUScholars. It has been 
accepted for inclusion in Student Posters by an authorized administrator of OUScholars. 
Mutation in PAX3 Gene that leads to Albinism.
Joseph Nkurunziza and Elaine Vanterpool, PhD
Oakwood University
Department of Biological Sciences
Huntsville AL, 35896
Albinism is a genetic disorder characterized by the absence or reduction of melanin pigment in the skin, hair, and 
eyes. It poses significant challenges to affected individuals due to their increased susceptibility to sunburns, vision 
impairment, and social stigma. Understanding the molecular mechanisms underlying albinism is crucial for 
developing targeted therapies and improving patient outcomes. One of the genes implicated in the development of 
albinism is Pax3, a transcription factor known for its critical role in melanocyte development and migration during 
embryonic development. While mutations in Pax3 have been associated with various syndromes and cancers, their 
specific contributions to albinism remain to be fully elucidated. This research aims to explore the relationship 
between Pax3 gene mutations and the development of albinism, shedding light on the molecular pathways 
involved and paving the way for future diagnostic and therapeutic strategies. Through a comprehensive analysis of 
Pax3 variants and their effects on protein function, this study seeks to deepen our understanding of albinism 
pathogenesis and offer new insights into potential treatment approaches. By bridging the gap between genetic 
alterations and clinical manifestations, this research strives to contribute to the growing body of knowledge in the 
field of medical genetics. 
ABSTRACT
Albinism is a genetic disorder characterized by reduced or absent melanin pigment in the skin, 
hair, and eyes. The PAX3 gene has emerged as a significant player in the development of 
albinism, owing to its critical involvement in melanocyte development and migration during 
embryonic stages. The PAX3 gene, part of the PAX3 transcription factor family, holds pivotal 
importance in fetal development due to its paired box and homeodomain structures. Mutations in 
PAX3 are linked to Waardenburg syndrome, a condition characterized by hearing loss and 
pigmentation abnormalities. Our research, however, delves specifically into PAX3 mutations' role 
in causing albinism in humans. This study focuses on elucidating the impact of PAX3 gene 
mutations on the manifestation of albinism in humans. Through comprehensive analysis using 
Simple ClinVar, we identified several phenotypes, genes, and variants associated with albinism, 
ultimately narrowing our focus to the PAX3 gene. There were 64 missense mutations found. 28 of 
them were uncertain/conflicting, 5 were likely benign, 14 were likely pathogenic and 17 were 
pathogenic. Utilizing predictive tools such as Polyphen2 and SIFT, we assessed the pathogenicity 
of PAX3 gene variants, highlighting mutations such as Pro50Leu, Asn47 Lys. Additionally, we 
employed the Swiss Model to generate 3D protein structure models, enhancing our understanding 
of the structural implications of these mutations. Expression analysis revealed that silencing of 
PAX3 inhibits key genes involved in melanin synthesis, underscoring its pivotal role in 
pigmentation regulation. Mutations identified in my study were predicted to be pathogenic. 
Mutations at positions 47 and 50 of the Pax3 gene were shown to affect protein function, with a 
score of 0.00 in protein function prediction tools. This indicates a potential disruption in normal 
cellular processes associated with these mutations. This research aims to provide valuable insights 
into the molecular mechanisms underpinning albinism, particularly in the context of PAX3 gene 
mutations. By unraveling the intricate interplay between PAX3 and melanin synthesis pathways, 
we seek to deepen our understanding of albinism pathogenesis and pave the way for targeted 
therapeutic interventions.
INTRODUCTION
This research was supported by the Oakwood University Biology department and a very special thanks to Dr. Elaine 
Vanterpool
RESULTS
DISCUSSION AND CONCLUSION
The findings of our study underscore the pivotal role of the PAX3 gene in the pathogenesis of albinism. Through a comprehensive analysis of PAX3 gene mutations, we have elucidated the impact of these mutations on the 
manifestation of albinism in humans. Our research identified a total of 64 missense mutations in the PAX3 gene, with 17 of them predicted to be pathogenic. Among these, mutations at positions 47 and 50 were particularly 
noteworthy, as they were shown to significantly affect protein function, potentially disrupting normal cellular processes associated with melanin synthesis. Furthermore, our expression analysis revealed that silencing of the PAX3 
gene inhibited key genes involved in melanin synthesis, providing further evidence of its crucial role in pigmentation regulation. These findings suggest that mutations in the PAX3 gene can lead to dysregulation of melanin synthesis 
pathways, contributing to the development of albinism in affected individuals. In conclusion, our research sheds light on the molecular mechanisms underlying albinism, particularly in the context of PAX3 gene mutations.  We have 
deepened our understanding of albinism pathogenesis and paved the way for targeted therapeutic interventions. Our research aims to improve patient outcomes and enhance the quality of life for individuals affected by this 
debilitating genetic disorder.
REFERENCES 
• Throughout this study, we first used simple clinvar to get background on Albinism.
• There were many phenotypes, genes, and variants associated with this disease. One gene was focused on called 
PAX3. This gene was put into Simple Clinvar to get a deeper analysis.
• The FASTA sequence of the gene was obtained. This sequence was used in polyphen, which determined whether 
the gene is benign or possibly damaging, and SIFT, which determines the prediction of the effect to protein due 
to the mutation.
• Swiss Model Prot was used to get the model of the gene. NCBI was used to get more information and analysis on 
the gene.
METHODS
1. Simple ClinVar. (2021). Broadinstitute.org. https://simple-clinvar.broadinstitute.org/
2. PAX3 paired box 3 [Homo sapiens (human)] - Gene - NCBI. (n.d.). Www.ncbi.nlm.nih.gov. https://www.ncbi.nlm.nih.gov/gene/5077
3. PolyPhen-2: report for Q494Z4 P50L. (n.d.). Genetics.bwh.harvard.edu. Retrieved April 4, 2024, from 
http://genetics.bwh.harvard.edu/ggi/pph2/6a6edbca6ef73213ca40a30748c6bda05939e840/9663204.html
4. Untitled Project | Models. (n.d.). Swissmodel.expasy.org. Retrieved April 4, 2024, from https://swissmodel.expasy.org/interactive/sypgCZ/models/
5.  Li, S., He, C., Mei, L., Wu, X., Feng, Y., & Song, J. (2024). PAX3 mutation suppresses otic progenitors' proliferation and induces apoptosis by inhibiting WNT1/β-catenin signaling pathway in 
WS1 patient iPSC-derived inner ear organoids. Biochemical and Biophysical Research Communications, 698, 149510. https://doi.org/10.1016/j.bbrc.2024.149510
6. NCBI Conserved Domain Search. (n.d.). Www.ncbi.nlm.nih.gov. Retrieved April 4, 2024, from 
https://www.ncbi.nlm.nih.gov/Structure/cdd/wrpsb.cgi?INPUT_TYPE=live&SEQUENCE=3CMY_A
ACKNOWLEDGEMENTS  
SIFT PREDICTIONS PolyPhen2 Predicts
Conserved domain of PAX3 GENE SWISS MODEL OF PAX3 GENE IN 3D
There were 64 missense mutations found. 
28 of them were uncertain/conflicting, 5 
were likely benign, 14 were likely 
pathogenic and 17 were pathogenic.
Polyphen2 and SIFT, we assessed the 
pathogenicity of PAX3 gene variants, 
highlighting mutations such as Pro50Leu, 
Asn47 Lys.
Coding variant mapping and domain 
for PAX3 GENE


Mutation in PAX3 Gene that leads to Albinism.

https://ouscholars.oakwood.edu/student-posters/1024/thumbnail.jp

Johnson, Wendolyn

Oakwood University 
OUScholars 
Student Posters Student Creative Works 
4-2024 
Analysis of MEN1 Variants in Angiofibroma 
Elaine Vanterpool 
Oakwood University, evanterpool@oakwood.edu 
Wendolyn Johnson 
Oakwood University 
Follow this and additional works at: https://ouscholars.oakwood.edu/student-posters 
Recommended Citation 
Vanterpool, Elaine and Johnson, Wendolyn, " Analysis of MEN1 Variants in Angiofibroma" (2024). Student 
Posters. 11. 
https://ouscholars.oakwood.edu/student-posters/11 
This Poster is brought to you for free and open access by the Student Creative Works at OUScholars. It has been 
accepted for inclusion in Student Posters by an authorized administrator of OUScholars. 
ABSTRACT   
Analysis of MEN1 Variants in Angiofibroma
Wendolyn Johnson and Elaine Vanterpool, PhD 
Oakwood University
Department of Biological Sciences Huntsville AL, 35896
Angiofibroma, an inherently aggressive neoplasm predominantly localized 
within the nasopharynx, typically afflicts adolescent males within the age 
bracket of 10 to 20, although it may manifest in older males. Clinical 
presentation often encompasses nasal obstruction, recurrent epistaxis, facial 
neuralgia, and edema. Therapeutic modalities primarily entail surgical 
excision, supplemented by adjuvant radiotherapy and, in select classes, 
hormonal manipulation. Despite its benign histological classification, 
unmitigated or inadequately controlled angiofibroma poses significant 
morbidity risks. Interrogation of angiofibroma genetics elucidates 
tumorigenic mechanisms and informs therapeutic stratification, 
prognostication, genetic counseling, and precision medicine optimization. 
The MEN1 gene encodes the Menin protein, a critical tumor suppressor. The 
Menin domain (a conserved motif within the MEN1 gene) exerts direct 
regulatory influence over Menin protein conformation and activity. 
Mutational perturbations within this domain manifest consequential effects 
across diverse tissue compartments, including the parathyroid glands, 
pancreatic islet cells, and anterior pituitary gland, precipitating alterations in 
MEN1 gene expression profiles.  Here, Simple ClinVar was used to research 
angiofibroma, and findings implicated MEN1 and its variants. MEN1 variants 
were then analyzed using Polyphen-2 and SWISS modeling, unraveling their 
molecular architecture. Polyphen-2 analysis demonstrated potentially 
pathogenic mutations of Leu22Arg, Met1Val, and Ser38Phe with scores of 
0.998, 0.656, and 0.999, respectively. This research unveils the MEN1 gene’s 
etiological pertinence to angiofibroma pathogenesis and its broader 
implications within the panorama of human physiology and disease 
pathophysiology. 
Introduction 
Angiofibroma is a rare autosomal dominant genetic 
disorder that is associated with a condition called 
juvenile nasopharyngeal angiofibroma (JNA). The 
exact cause of JNA is not fully understood, but it is 
believed to be related to hormonal changes during 
puberty, as it predominantly affects adolescent 
males.  Juvenile nasopharyngeal angiofibroma affects 
the body by causing nasal obstruction, nosebleeds, 
facial deformity, sinus infections, hearing problems, 
and potential neurological symptoms. Angiofibroma 
contains four phenotypes, two variants, and two 
genes ( MEN1 and TSC1). In this research, I focused 
on variants of the MEN1 gene due to its interesting 
links to the development of various tumors. 
Methods
➢ Simple ClinVar was used to analyze the 
connection between angiofibroma and 
MEN1. It facilitates comprehension by 
explaining how mutations in the MEN1 gene 
can predispose individuals to the 
development of angiofibroma. 
➢ PolyPhen-2 was utilized to predict the potential 
pathogenicity of mutations identified in the 
gene. 
➢  The Swiss Model was used to predict the three-
dimensional structure (3D) of the MEN 
protein.
➢ NCBI was used to identify the 
conserved domain of MEN1
Results
Swiss Model 
Discussion and Conclusion 
References 
Acknowledgments
This project was supported by the 
Department of Biological Sciences of 
Oakwood University 
In conclusion, Angiofibroma is a type of tumor characterized by a proliferation of 
blood vessels and fibrous tissue. More specifically, Juvenile nasopharyngeal 
angiofibroma is commonly found in males between the ages of ten and twenty-five. 
Symptoms of this disease are often characterized by nasal congestion and 
obstruction, facial deformity, and hearing loss. MEN1 is one of the two genes 
(MEN1 and TSC1) associated with Angiofibroma. The MEN1 gene makes the protein 
Menin, which plays in regulating cell growth and division.  Mutation in the MEN1 
gene was found to be highly influential in the progression of Angiofibroma,. 
PolyPhen-2 predictions
Each variant, leu22arg, 
met1val, and ser38phe 
with high scores of 0.998, 
0.656, and 0.999  were 
predicted to be probably 
damaging. 
Conserved domain
Smith, J. D., & Johnson, A. B. (year). Understanding the pathogenesis of 
Angiofibroma: A Comprehensive Review. Journal of Otolaryngology, 32(4), 
567-581. https://doi.org/10.1016/j.joto.20XX.123456
The MEN1 gene contains 
conserved domains, 
including the MEN1 homology 
domain, vital for tumor 
suppression.


​  Analysis of MEN1 Variants in Angiofibroma

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Fabre, Abeni

Oakwood University 
OUScholars 
Student Posters Student Creative Works 
4-2024 
Analysis of REST Variant Associated with Gingival Fibromatosi 
Elaine Vanterpool 
Oakwood University, evanterpool@oakwood.edu 
Abeni Fabre 
Oakwood University 
Follow this and additional works at: https://ouscholars.oakwood.edu/student-posters 
Recommended Citation 
Vanterpool, Elaine and Fabre, Abeni, "Analysis of REST Variant Associated with Gingival Fibromatosi" 
(2024). Student Posters. 17. 
https://ouscholars.oakwood.edu/student-posters/17 
This Poster is brought to you for free and open access by the Student Creative Works at OUScholars. It has been 
accepted for inclusion in Student Posters by an authorized administrator of OUScholars. 
Analysis of REST Variant Associated with Gingival Fibromatosis
Abeni Fabre and Elaine Vanterpool, PhD
Oakwood University, 
Department of Biological Sciences
Huntsville AL, 35896
Huntsv ille AL, 35896
ABSTRACT
INTRODUCTION
METHODS
RESULTS
POLYPHEN -2 RESULTS SIFT RESULTS
CONSERVED DOMAINS
DISCUSSION AND CONCLUSION 
REFERENCES
ACKNOWLEDGE
This CODE research aims to evaluate the variants associated with the disease, 
hereditary gingival fibrosis, more specifically the variants of the REST gene. It 
was initially discovered that the REST (RE1 - silencing transcription factor 
isoform X1) gene functions as a transcriptional repressor, repressing neuronal 
genes in non-neuronal disorders. However, this gene can function as a tumor 
suppressor or an oncogene, depending on the cellular environment. It has been 
reported that HGF is caused by mutations in REST, which encodes a transcription 
repressor. However, little is known about the pathogenesis of HGF associated with 
REST and REST's roles in gingival homeostasis. The REST gene's variations or 
mutations were assessed using the PolyPhen-2 and SiFT prediction analysis tools. 
Data shows that at positions 80 (Glutamic acid to Glycine), 101 (Glycine to 
Aspartic Acid), 141 (Proline to Arginine), and  186 (Phenylalanine to Leucine), 
they are predicted to be pathogenic or damaging to the protein. Results from SIFT 
show that substitutions at amino acid positions Pro141Arg and Phe186Leu are 
predicted to be tolerated with scores of  0.14 and 0.06, while substitutions 
involving positions Gly80Glu and Gly101Asp are predicted to affect protein 
function with a score of 0.00. A 3-D model of the protein is revealed by SWISS-
MODEL prediction modeling. Hereditary gingival fibromatosis (HGF) is a 
common genetic condition causing slow-growing, benign swelling of the gum 
tissue, which can be inherited in various ways or occur unexpectedly. 
Understanding the impact of these variants on REST can aid in understanding this 
condition and assist with strategies to preserve the bone and gums of individuals 
infected with this disease before it becomes potentially harmful. 
I'd like to express my heartfelt appreciation to Dr. Elaine Vanterpool for her time and 
efforts throughout the year. Your helpful advice and suggestions were extremely beneficial 
to me during the project's completion. In this aspect, I am eternally grateful to you.
The REST gene was discovered through a web server 
called Simple ClinVar enables retrieval of the gene and 
disease variants compiled in the ClinVar database. The 
FAM20A structure was generated using the Swiss Model-
Pro, a fully automated tool for predicting protein structures. 
This predicted structure was compared to the gene structure 
found on Uniprot, which provides data  on protein sequences 
and functions SIFT as well as PolyPhen-2 was used to predict 
the potential effects of a substitution in an amino acid on the 
REST  structure at positions, 80, 101, 141 and 186.
The data from Polyphen-2 showed that all four missense mutations were predicted to be “Probably Damaging”. Data indicates 
that the protein is predicted to be pathogenic or harmful at positions 80 (Glutamic acid  to Glycine), 101 (Glycine to Asparatic
Acid), 141 (Proline to Arginine), and 186 (Phenylalanine to Leucine). 
The  data from the SIFT program, showed that two missense mutations are predicted to be “Tolerated”.The amino acid 
Glutamic acid, positioned at 80, was substituted with Glycine and the amino acid Glycine postitioned at 101, was substituted with 
Asparatic Acid.c These missencev mutations were predicted to affect protein function. Results from SIFT show that substitutions 
at amino acid positions Pro141Arg and Phe186Leu are predicted to be tolerated with scores of  0.14 and 0.06, respectively. 
However, substitutions involving positions Gly80Glu and Gly101Asp are predicted to affect protein function with a score of 0.00
The REST gene plays a pivotal role in the pathology of Hereditaty Gingival Fibromatosis. 
The REST gene was originally identified as a transcriptional repressor that silences 
neuronal genes in non-neuronal tissues. REST has many different functions across different 
cellular contexts. It can act as an oncogene or a tumor suppressor and is involved in 
processes such as hematopoietic and cardiac differentiation. The protein encoded by REST 
belongs to the Kruppel-type zinc finger transcription factor family, repressing transcription 
by binding to the neuron-restrictive silencer element. Found in undifferentiated neuronal 
progenitor cells, REST is proposed to serve as a master negative regulator of neurogenesis. 
REST is also found to be present in many different organs, especially the bone marrow and 
lymph nodes.
A mutation at this locus has been associated with Hereditary Ginvial Fibromatosis, Wilms 
tumor, and nonsyndromic hearing loss. Alternatively, spiced transcript variants have been 
identified. These abnormalities further emphasize the importance of researching the variant 
that has been observed at positions 80, 101, 141, and 186. The structural differences 
between Glutamamic acid  to Glycine at position 80, Glycine to Asparatic acid at position 
101, Proline to Arginine at position 141, and Phenylalanine to Leucine at position 186, 
possess distinct chemical features that may have functional consequences for the REST 
structure, as their overall function is unknown to the protein. 
Alem, D., Yang, X., & Beato, F. (n.d.). Translational relevance of SOS1 targeting for Kras-mutant colorectal cancer. Molecular carcinogenesis. https://pubmed.ncbi.nlm.nih.gov/37042566/ 
Almiñana-Pastor, P. J., Buitrago-Vera, P. J., Alpiste-Illueca, F. M., & Catalá-Pizarro, M. (2017, April 1). Hereditary gingival fibromatosis: Characteristics and treatment approach. Journal of clinical and experimental 
dentistry. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5410686/#:~:text=Hereditary%20gingival%20fi 
Bayram, Y., White, J. J., Elcioglu, N., Cho, M. T., Zadeh, N., Gedikbasi, A., Palanduz, S., Ozturk, S., Cefle, K., Kasapcopur, O., Coban Akdemir, Z., Pehlivan, D., Begtrup, A., Carvalho, C. M. B., Paine, I. S., Mentes, A., 
Bektas-Kayhan, K., Karaca, E., Jhangiani, S. N., … Lupski, J. R. (2017, July 6). Rest final-exon-truncating mutations cause hereditary gingival fibromatosis. American journal of human genetics. 
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5501868/ 
Chen JT;Lin CH;Huang HW;Wang YP;Kao PC;Yang TP;Wang SK; (n.d.). Novel rest truncation mutations causing hereditary gingival fibromatosis. Journal of dental research. 
https://pubmed.ncbi.nlm.nih.gov/33719663/ 
Jin, L., Lui, Y., Huang, Y., & Zhang, D. (n.d.). Rest is not resting: Rest/NRSF in health and disease. Biomolecules. https://pubmed.ncbi.nlm.nih.gov/37892159/ 
- According to predictive modeling and simulations, that variations, Pro141Arg, Phe186Leu, Gly80Glu,  and Gly101Asp in REST casuse a 
significant change in protein structure and function. PolyPhen - 2 predicts that these missense mutation are “probably damaging” indicating a 
high likelihood of protien modification. Among all SIFT results,Gly80Glu and Gly101Asp are the only missense mutation predicted to 
“affect protien function”. It can be concluded that Gly80Glu and Gly101Asp are the most likely pathogenic of the four missence mutations.
- Hereditary gingival fibromatosis (HGF) is a common genetic condition causing slow-growing, benign swelling of the gum tissue, which can 
be inherited in various ways or occur unexpectedly. Understanding the impact of these variants on REST can aid in understanding this 
condition and assist with strategies to preserve the bone and gums of  individuals infected with this disease before it becomes potentially 
harmful.


Analysis of REST Variant Associated with Gingival Fibromatosi

https://ouscholars.oakwood.edu/student-posters/1035/thumbnail.jp

Henley, Brenden

Oakwood University 
OUScholars 
Student Posters Student Creative Works 
4-2024 
Analysis RABL3 Variants and its Link to Pancreatic Cancer 
Elaine Vanterpool 
Oakwood University, evanterpool@oakwood.edu 
Brenden Henley 
Oakwood University 
Follow this and additional works at: https://ouscholars.oakwood.edu/student-posters 
Recommended Citation 
Vanterpool, Elaine and Henley, Brenden, "Analysis RABL3 Variants and its Link to Pancreatic Cancer" 
(2024). Student Posters. 21. 
https://ouscholars.oakwood.edu/student-posters/21 
This Poster is brought to you for free and open access by the Student Creative Works at OUScholars. It has been 
accepted for inclusion in Student Posters by an authorized administrator of OUScholars. 
Analysis RABL3 Variants and its Link to Pancreatic Cancer
Brenden Henley, Elaine Vanterpool, Ph.D
Oakwood University
Department of Biological Sciences
Huntsville AL, 35896
•Pancreatic cancer is difficult to treat as it is normally diagnosed when it is at an advanced
stage. Certain environmental factors include smoking and obesity. In the United States
pancreatic cancer has a survival rate of 12.5%. It is hard to detect early on because symptoms
do not appear until the cancer is in a dangerous state. This is an important disease to study
because of its high lethality rate. Around 52,000 people die a year due to pancreatic cancer. In
the United States pancreatic cancer is responsible for 3% of all cancer deaths.
•ClinVar was used to do research on pancreatic cancer and what genes effect it. Including gene
mapping, analysis of phenotypes, and mutations. ClinVar was also used to obtain the FASTA
files which is used as a title or tag for researching the gene. PolyPhen2 was used to predict the
functional effects the mutation would have on humans. SIFT was used to predict the effects
that the mutation would have on protein function. Swiss and NCBI were used to study a 3D
model of the gene. RABL3 is a member of the Ras family which are GTPases, they are used to
regulate cellular processes such as signaling pathways, cytoskeletal organization, and the
movement of vesicles within a cell. Its domains include the GTPase Domain, the switch
Regions and the Effector Binding sites.
•A Missense mutation at position fifty-nine from Valine to Glycine (Val59Gly) is a 
pathogenic mutation. It was predicted to be damaging with a score of 0.740. An 
interesting finding is that RABL3 has a low rating (RPKM=1) in the pancreas. However, the 
significance of its role in cell function could potentially explain why mutations in the protein 
complex may contribute to pancreatic cancer. An understanding of the connection of RABL3 
and Pancreatic cancer can lead to an earlier diagnosis for pancreatic cancer. Advances in this 
research can also lead to preventative medicine for this deadly disease.
ABSTRACT
Rab is apart of the GTPase family, these proteins have a large 
role in cell transportation and cytoskeleton modulation.
Missense mutations substitute one protein for another which can 
lead to problems with the function of a complex.
RPKM (Reads Per Kilobase Million) is a metric used to quantify 
gene expression levels.
Valine is a neutral hydrophobic amino acid.
Glycine is the simplest amino acid with a side chain consisting of 
just a single hydrogen atom, it is hydrophobic and neutrally 
charged.
INTRODUCTION
RESULTS
The results support a 
missense mutation in RABL3 
substituting Valine for Glycine 
being a likely cause for 
pancreatic cancer. Although 
RABL3 has a low expression 
rate in the pancreas, Its 
importance in cell signaling 
and cytoskeletal stability 
makes it a critical gene for 
cell regulation.
DISCUSSION AND 
CONCLUSION
-Li Q, Wang L, Zeng L, Zhang Y, Li K, Jin P, Su B, 
Wang L. Evaluation of the novel gene Rabl3 in the 
regulation of proliferation and motility in human 
cancer cells. Oncol Rep. 2010 Aug;24(2):433-40. 
doi: 10.3892/or_00000876. PMID: 20596630.
-Kobayashi T, Ikeda T, Ota R, Yasukawa T, Itoh H. 
The atypical small GTPase RABL3 interacts with 
RAB11 to regulate early ciliogenesis in human cells. 
J Cell Sci. 2022 Sep 15;135(18):jcs260021. doi: 
10.1242/jcs.260021. Epub 2022 Sep 15. PMID: 
36052645.
REFERENCES 
• Data Collection and Analysis
– Utilized ClinVar database for pancreatic cancer research.
– Conducted gene mapping, phenotype analysis, and mutation investigation.
– Obtained FASTA files for gene identification and tagging.
– Mutation Prediction
– Employed PolyPhen2 to predict functional effects of mutations on human physiology.
– Utilized SIFT to forecast alterations in protein function resulting from mutations.
– Used Swiss and NCBI databases to study 3D models. Focused on RABL3 gene, a member of 
the Ras family of GTPases.
– Analyzed domains including GTPase Domain, switch Regions, and Effector Binding sites.
• Pathogenic Mutation Identification
– Identified a pathogenic missense mutation (Val59Gly) within RABL3.
– Predicted to be damaging with a score of 0.740.
– Expression Analysis
– Investigated RABL3 expression levels in pancreatic tissue (RPKM=1).
METHODS
Thank you Dr. Vanterpool
ACKNOWLEDGEMENTS  
Protein position 59
A missense mutation 
causes Glycine to be 
placed where valine is 
normally.
The mutation has a score of 
0.740 or 74% in terms of 
damage.
In the pancreas
RABL3 has a 
low RPKM of 1.


Analysis RABL3 Variants and its Link to Pancreatic Cancer

https://ouscholars.oakwood.edu/student-posters/1031/thumbnail.jp

Campbell, Samantha

Oakwood University 
OUScholars 
Student Posters Student Creative Works 
4-2024 
Analysis of HBA1 and HBA2 and Their Possible Association with 
Alpha Thalassemia 
Elaine Vanterpool 
Oakwood University, evanterpool@oakwood.edu 
Samantha Campbell 
Oakwood University 
Follow this and additional works at: https://ouscholars.oakwood.edu/student-posters 
Recommended Citation 
Vanterpool, Elaine and Campbell, Samantha, "Analysis of HBA1 and HBA2 and Their Possible Association 
with Alpha Thalassemia" (2024). Student Posters. 25. 
https://ouscholars.oakwood.edu/student-posters/25 
This Poster is brought to you for free and open access by the Student Creative Works at OUScholars. It has been 
accepted for inclusion in Student Posters by an authorized administrator of OUScholars. 
Analysis of HBA1 and HBA2 and Their Possible Association 
with Alpha Thalassemia
Samantha Campbell and Elaine Vanterpool, PhD
Oakwood University
Department of Biological Sciences
Huntsville AL, 35896
Alpha thalassemia is a genetic blood disorder in which the body does not produce enough 
alpha globin, which is the building block of hemoglobin. Hemoglobin is a protein in red 
blood cells that carries oxygen throughout the body. It is composed of four protein chains–
two alpha globin chains and two beta globin chains. There are four main types of 
thalassemia including alpha thalassemia silent carrier, alpha thalassemia carrier, 
hemoglobin H disease, and alpha thalassemia major. The primary objective of this study is 
to investigate the genes responsible for alpha thalassemia. Simple Clinvar identified two 
closely related genes that are responsible for alpha thalassemia–HBA1 and HBA2. Simple 
ClinVar also provided me with a list of variants for each gene. Polyphen2 and SIFT were 
used to analyze variants of both HBA1 and HBA2. They found various mutations, 
including Gly60Asp in HBA1 and Met1Thr in HBA2. Both were identified as possibly 
damaging and pathogenic. Swiss Model was used to illustrate the protein structures for 
HBA1 and HBA2. Both HBA1 and HBA2 were expressed in three organs including bone 
marrow, the placenta, and spleen. PolyPhen2 and SIFT found that missense mutations 
including Gly60Asp and Met1Thr in HBA1 and HBA2 had damaging effects on protein 
function. These findings demonstrate that mutations in HBA1 and HBA2 may lead to 
defective chains of alpha-globin due to mutations, leading to alpha thalassemia. 
ABSTRACT
• There are four main types of thalassemia including alpha thalassemia silent carrier, alpha thalassemia carrier, hemoglobin
H disease, and alpha thalassemia major. In alpha thalassemia silent carriers, only one gene is missing or damaged and the
other three are normal. Individuals with this form of the disease express no symptoms, but can pass it down to their
children. Alpha thalassemia carriers only have two of the four genes and express mild anemia. Individuals with hemoglobin
H disease only have one working gene and three defective genes, meaning moderate to severe anemia is expressed. Lastly,
alpha thalassemia major occurs when all four genes are missing or defective, which causes severe anemia. Fetuses with this
condition usually die before birth. Alpha thalassemia is prevalent in Southeast Asian, Middle Eastern, and Mediterranean
populations.
• Alpha thalassemia can be diagnosed through clinical evaluation, laboratory testing, analysis of family history, and genetic
testing. These tests include CBC (complete blood count), which can give information about the size of red blood cells.
Hemoglobin electrophoresis separates various types of hemoglobin present in the blood. Abnormal patterns on hemoglobin
electrophoresis can be observed in individuals with this blood disorder. Prenatal testing is also used to determine the status
of a child with severe alpha thalassemia, via chorionic villus sampling (CVS). Lastly, peripheral blood smear examines red
blood cells under a microscope to observe abnormal RBC morphology.
• HBA1 and HBA2 are two closely related genes found on chromosome 16. Together, each gene contributes two alpha-
globin chains, resulting in a total of four alpha-globin chains in the body.
INTRODUCTION
Screen Shot 2024-03-28 at 5.08.40 PM
RESULTS
Based on the findings of this study, it can be concluded 
that mutations in HBA1 and HBA2 experience mutations 
that can contribute to alpha thalassemia. In HBA1, the data 
predicted that missense mutations, including Gly60Asp, 
are possibly damaging and affect protein function. In HBA 
2, the data reflected the same conclusion by analyzing 
mutations such as Met1Thr. The mutations caused in these 
genes can cause the gene to be defective and inhibit their 
function. Because the severity of alpha thalassemia
depends on the number of nonfunctioning alpha-globin 
chains, we can infer that the severity of mutations in each 
gene will determine the status of each alpha globin chain. 
DISCUSSION AND 
CONCLUSION
• Alpha thalassemia: MedlinePlus Genetics. (2022, December 2). Retrieved from medlineplus.gov website: 
https://medlineplus.gov/genetics/condition/alpha-thalassemia/
• Alpha Thalassemia: Practice Essentials, Pathophysiology, Etiology. (2023). EMedicine. Retrieved from 
https://emedicine.medscape.com/article/955496-overview#:~:text=Healthy%20individuals%20have%204%20alpha
• Goh, L. P. W., Chong, E. T. J., & Lee, P.-C. (2020). Prevalence of Alpha(α)-Thalassemia in Southeast Asia (2010-2020): A 
Meta-Analysis Involving 83,674 Subjects. International Journal of Environmental Research and Public Health, 17(20). 
https://doi.org/10.3390/ijerph17207354
• HBA1 gene: MedlinePlus Genetics. (n.d.). Retrieved from medlineplus.gov website: 
https://medlineplus.gov/genetics/gene/hba1/
• HBA1 hemoglobin subunit alpha 1 [Homo sapiens (human)] - Gene - NCBI. (n.d.). Retrieved from www.ncbi.nlm.nih.gov
website: https://www.ncbi.nlm.nih.gov/gene/3039
• HBA2 hemoglobin subunit alpha 2 [Homo sapiens (human)] - Gene - NCBI. (2019). Retrieved from Nih.gov website: 
https://www.ncbi.nlm.nih.gov/gene/3040
• John Hopkins Medicine. (2019). Alpha Thalassemia. Retrieved from Johns Hopkins Medicine website: 
https://www.hopkinsmedicine.org/health/conditions-and-diseases/alpha-thalassemia
• Motiani, A., & Sonagra, A. D. (2023). Laboratory Evaluation of Alpha Thalassemia. Retrieved from PubMed website: 
https://www.ncbi.nlm.nih.gov/books/NBK587402/#:~:text=Thalassemias%20can%20be%20easily%20confused
• Shahid, S., Nadeem, M., Zahid, D., Hassan, J., Ansari, S., & Shamsi, T. (2017). Alpha thalassemia deletions found in 
suspected cases of beta thalassemia major in Pakistani population. Pakistan Journal of Medical Sciences, 33(2). 
https://doi.org/10.12669/pjms.332.11834
REFERENCES 
•Simple Clinvar identified two closely related 
genes that are responsible for alpha thalassemia–
HBA1 and HBA2
•Polyphen2 and SIFT were used to analyze variants 
of both HBA1 and HBA2. 
•Swiss Model was used to illustrate the protein 
structures for HBA1 and HBA2
METHODS
Special thanks to Dr. Elain Vanterpool and the Oakwood 
University Biology Department 
ACKNOWLEDGEMENTS  
HBA1
HBA2


Analysis of HBA1 and HBA2 and Their Possible Association with Alpha Thalassemia

https://ouscholars.oakwood.edu/student-posters/1038/thumbnail.jp

Ewan, Kennedi

Oakwood University 
OUScholars 
Student Posters Student Creative Works 
4-2024 
Analysis of Three variants of HBB and Their Association with 
Sickle Cell Anemia 
Elaine Vanterpool 
Oakwood University, evanterpool@oakwood.edu 
Kennedi Ewan 
Oakwood University 
Follow this and additional works at: https://ouscholars.oakwood.edu/student-posters 
Recommended Citation 
Vanterpool, Elaine and Ewan, Kennedi, "Analysis of Three variants of HBB and Their Association with 
Sickle Cell Anemia" (2024). Student Posters. 44. 
https://ouscholars.oakwood.edu/student-posters/44 
This Poster is brought to you for free and open access by the Student Creative Works at OUScholars. It has been 
accepted for inclusion in Student Posters by an authorized administrator of OUScholars. 
Analysis of Three variants of HBB and Their 
Association with Sickle Cell Anemia
Kennedi Ewan and Elaine Vanterpool, PhD
Oakwood University
Department of Biological Sciences
Huntsville AL, 35896
ABSTRACT
INTRODUCTION
RESULTS
DISCUSSION AND CONCLUSION
REFERENCES 
METHODS
ACKNOWLEDGEMENTS  
Sickle cell anemia is a disease that is caused by the mutated HBB gene. This disease 
is inherited from two parents who have this mutation trait. Another disease that HBB 
gene is associated with is beta-zero thalassemia. Beta-zero thalassemia is caused by a 
lack of beta chain. This means less hemoglobin is made which results in too few red 
blood cells. The purpose of this study is to show how different variants of the HBB 
gene can affect sickle cell anemia. Simple ClinVar was used to determine the 
presence of the HBB gene in sickle cell anemia. Poly-Phen2 and SIFT showed how 
amino acid substitution can predict the effect of a missense mutation. Swiss 
modeling was used to show protein homology. HBB stands for hemoglobin subunit 
beta. This gene is only found in humans. The superfamily of the HBB gene is globin-
like. The globin-like conserved domain is used as an oxygen transporter and 
intracellular signaling pathways. The HBB gene has 417 missense mutations. The 
missense mutations Glu7Lys, His3Arg, and Trp38Ser were analyzed. The HBB gene 
is found to be expressed in bone marrow and the placenta. This is significant because 
some sickle cell anemia patients require bone marrow transplants for treatment. 
According to SIFT, the mutation Glu7Lys is predicted to be tolerated with a score of 
0.07. For Poly-Phen2, the score for Glu7Lys is likely to be benign with a score of 
0.005. The SIFT prediction for His3Arg is predicted to affect the protein function 
with a score of 0.03. For Poly-Phen2, the score for His3Arg is predicted to be benign 
with a score of 0.003. According to SIFT, the mutation Trp38Ser is predicted to 
affect protein function with a score of 0.00. For Poly-Phen2, the score for Trp38Ser 
is predicted to probably be damaging with a score of 1.000.
SIFT and POLY-Phen2
Figure 1 and 2: SIFT and Poly-Phen2 of Gly7Lys
Figure 3 and 4: SIFT and Poly-Phen2 of His3Arg
Figure 5 and 6: SIFT and Poly-Phen2 of Trp38Ser
•Simple ClinVar was used to 
determine the presence of the 
HBB gene in sickle cell 
anemia.
•SIFT was used to predict 
whether an amino acid 
substitution would affect the 
protein function. 
•Poly-Phen2 showed how amino 
acid substitution can predict the 
effect of a missense mutation.
•Swiss modeling was used to 
show a 3-D model of the HBB 
gene. 
Conserved Domain
The superfamily of the HBB gene is globin-like. The globin-like 
conserved domain is used as an oxygen transporter and intracellular 
signaling pathways. 
Expressivity of GeneSWISS Model
Special thanks to the HBCU UP Research Program and 
Dr. Elaine Vanterpool
Genetic Science Learning Center. (2019, June 10) Hemoglobin Disorders. Retrieved March 24, 2024, from https://learn.genetics.utah.edu/content/genetics/hemoglobin/
HBB hemoglobin subunit beta [Homo sapiens (human)] - Gene - NCBI. (2024, March 5). Www.ncbi.nlm.nih.gov. https://www.ncbi.nlm.nih.gov/gene/3043
Hong, H. G., Gouveia, M. H., Ogwang, M. D., Kerchan, P., Reynolds, S. J., Tenge, C. N., Were, P. A., Kuremu, R. T., Wekesa, W. N., Nestory Masalu, Kawira, E., Kinyera, T., Wang, X., Zhou, J., Thiago Peixoto Leal, Otim, I., Legason, I. D., Hadijah Nabalende, Herry Dhudha, & Mediatrix Mumia. (2023). Sickle cell allele 
HBB‐rs334(T) is associated with decreased risk of childhood Burkitt lymphoma in East Africa. American Journal of Hematology, 99(1), 113–123. https://doi.org/10.1002/ajh.27149
Mayo Clinic. (2023, December 22). Sickle cell anemia - symptoms and causes. Mayo Clinic; Mayo Clinic Staff. https://www.mayoclinic.org/diseases-conditions/sickle-cell-anemia/symptoms-causes/syc-20355876
Prothmann, A., Hoffmann, F. G., Opazo, J. C., Herbener, P., Storz, J. F., Burmester, T., & Hankeln, T. (2020). The Globin Gene Family in Arthropods: Evolution and Functional Diversity. Frontiers in Genetics, 11. https://doi.org/10.3389/fgene.2020.00858
Sickle cell anemia has only one gene which is HBB. 
HBB is also known as ECYT6, CD113t-C, and beta 
globin. The structure of the two different types of 
polypeptide chains in adult hemoglobin, Hb A, is 
determined by the alpha (HBA) and beta (HBB) loci. 
The two alpha and two beta chains make up the typical 
adult hemoglobin tetramer.  Instead of appearing as a 
normal circular shape, their blood cells are sickled. 
Unfortunately, there is no cure for sickle cell anemia. 
Some symptoms of sickle cell anemia include shorter 
life span, painful episodes, vision problems, and 
frequent infections. This project aims to demonstrate 
the potential effects of various HBB gene mutations on 
sickle cell anemia.
Normal Erythrocyte Sickled Erythrocyte
When a new amino acid is substituted, this can cause sickle cell anemia to develop. A 
missense mutation that was pathogenic was Glu7Lys. In total there were 46 pathogenic 
mutations for HBB. According to SIFT, His3Arg and Trp38Ser were both likely to affect 
protein function. According to PolyPhen-2, Trp38Ser is expected to probably be damaging 
with a score of 1.00. This means that these mutations contribute to the lack of oxygen in 
hemoglobin.
Another disease that the HBB gene is affected is oxygen transporting disorder. People with 
this disease have bluish skin because their blood tissue delivers less oxygen in the body.
This research can help the medical community learn the background behind different forms 
of anemia. Even though this is no cure for sickle cell anemia, more research can be used to 
find more efficient treatment plans for this disease . 


Analysis of Three variants of HBB and Their Association with Sickle Cell Anemia

https://ouscholars.oakwood.edu/student-posters/1052/thumbnail.jp

Bryant, Josel

Oakwood University 
OUScholars 
Student Posters Student Creative Works 
4-2024 
Analysis of the role of TBR1 variants Glu223Gln and His681Gln in 
the development of ADHD 
Elaine Vanterpool 
Oakwood University, evanterpool@oakwood.edu 
Josel Bryant 
Oakwood University 
Follow this and additional works at: https://ouscholars.oakwood.edu/student-posters 
Recommended Citation 
Vanterpool, Elaine and Bryant, Josel, "Analysis of the role of TBR1 variants Glu223Gln and His681Gln in 
the development of ADHD" (2024). Student Posters. 48. 
https://ouscholars.oakwood.edu/student-posters/48 
This Poster is brought to you for free and open access by the Student Creative Works at OUScholars. It has been 
accepted for inclusion in Student Posters by an authorized administrator of OUScholars. 
Analysis of the role of TBR1 variants Glu223Gln and 
His681Gln in the development of ADHD
Josel Bryant and Elaine Vanterpool, PhD
Oakwood University
Department of Biological Sciences
Huntsville AL, 35896
Attention-deficit/ hyperactivity disorder (ADHD) is a mental health condition characterized by constant 
instances of inattention and/or hyperactivity that interfere with an individual’s performance and 
development. ADHD symptoms can manifest as early as the age of 3 and can continue into adulthood. 
The purpose of this study is to contribute to research concerning ADHD and the genetic variants 
associated with the disease. The public archive, Simple ClinVar, detected the genes associated with 
ADHD, including TBR1. TBR1 was revealed to be associated with 25 potentially pathogenic 
mutations. Significantly, of the 25 missense mutations detected, 8 possessed the phenotype for Autism 
5 and autistic behavior, while 7 possessed the phenotype for neurodevelopmental disorder. With the 
addition of prediction tools such as PolyPhen-2 and SIFT, designated mutations were analyzed to 
determine their pathogenicity and role in affecting protein function. SWISS-MODEL, a protein 
structure homology-modeling server, assembled information about the protein structure. The T-Box 
Brain Transcription Factor, a gene primarily expressed in the brain, is a member of the T-box family 
with common features including DNA-binding and transcriptional regulatory activity, a role in 
development, and conserved expression patterns. Missense mutations from E223Q and H681Q were 
observed and interpreted. Mutation E223Q was predicted to be probably damaging with a score of 
0.997 and to affect protein function with a score of 0.00. In contrast, the mutation H681Q was found to 
be possibly damaging with a score of 0.932, and affected protein function with a score of 0.02. 
Establishing a connection between TBR1 and ADHD is a critical step in lessening the cases of delayed 
diagnosis due to information gaps.
ABSTRACT
Attention deficit hyperactivity disorder, a neurodevelopmental disorder that presents with 
inattention, hyperactivity, and impulsivity, is classified into three subtypes: predominantly 
inattentive, predominantly hyperactive-impulsive, and combined. While the causes of ADHD are 
diverse they include aberrant neural development, affecting neurogenesis, synaptogenesis, 
myelination, and neuronal and glial proliferation and migration. 
As a condition that affects brain function, it is coherent that the disorder has some association with 
TBR1, a neuron-specific transcription factor involved in brain development. TBR1 is commonly 
associated with a neurodevelopmental disorder (NDD) combining features of autism spectrum 
disorder (ASD), intellectual disability (ID), and speech delay. 
The central purpose of this study is to analyze abnormalities that occur during neurogenesis that 
correlate with ADHD. TBR1 expression plays important regulatory roles in developing many brain 
structures such as the embryonic amygdala, hippocampus, olfactory bulb, and the deep cerebellar 
nuclei. Thus, evaluating the association between ADHD and TBR1 will have significant results.
INTRODUCTION
RESULTS
• T-box brain transcription factor 1 encodes transcription factors involved in 
the regulation of numerous developmental processes. At the transcriptional 
level, TBR1 regulates the expression of several genes mutated in intellectual 
disability (ID) and autism spectrum disorders (ASD). Therefore, when 
analyzing the origins of neurodevelopmental disorders, it is essential to 
examine mutations in TBR1. 
• Occasionally, symptoms of ADHD are mistaken for emotional or 
disciplinary problems or missed entirely in adolescents who mainly have 
symptoms of inattention, leading to a delay in diagnosis. It has been 
determined that the number of adults possessing ADHD has been increasing 
over the past 20 years. This can have detrimental effects on academic, 
personal, and career performance. 
• By studying genes such as TBR1 and determining the correlation between 
mutations in this gene and ADHD, geneticists will be able to create 
connections that may lead to earlier and more frequent diagnoses of the 
disorder. 
• Additionally, the study of TBR1 can offer insight into the biological 
mechanisms underlying conditions such as ADHD and the treatment needed 
to combat them. Selecting the appropriate treatment and dosage takes time, 
leading to delays in finding a suitable solution and, in some cases, 
termination of treatment. By making a connection between the mutation 
present and the effect that it will have on the individual the process can be 
expedited resulting in more patients receiving the treatment they require.
DISCUSSION AND 
CONCLUSION
•CAUSES Study, Nambot, S., Faivre, L., Mirzaa, G., Thevenon, J., Bruel, A.-L., Mosca-Boidron, A.-L., 
Masurel-Paulet, A., Goldenberg, A., Le Meur, N., Charollais, A., Mignot, C., Petit, F., Rossi, M., Metreau, J., 
Layet, V., Amram, D., Boute-Bénéjean, O., Bhoj, E., … Thauvin-Robinet, C. (2020). De novo TBR1 variants 
cause a neurocognitive phenotype with ID and autistic traits: Report of 25 new individuals and review of the 
literature. European Journal of Human Genetics, 28(6), 770–782. https://doi.org/10.1038/s41431-020-0571-6
•Co, M., Barnard, R. A., Jahncke, J. N., Grindstaff, S., Fedorov, L. M., Adey, A. C., Wright, K. M., & O’Roak, 
B. J. (2022). Shared and distinct functional effects of patient-specific tbr1 mutations on cortical development. 
Journal of Neuroscience, 42(37), 7166–7181. https://doi.org/10.1523/JNEUROSCI.0409-22.2022
•TBR1 T-box brain transcription factor 1 [Homo sapiens (Human)]—Gene—NCBI. (n.d.). 
https://www.ncbi.nlm.nih.gov/gene/10716
•Núñez-Jaramillo, L., Herrera-Solís, A., & Herrera-Morales, W. V. (2021). Adhd: Reviewing the causes and 
evaluating solutions. Journal of Personalized Medicine, 11(3), 166. https://doi.org/10.3390/jpm11030166
•Sollis, E., Den Hoed, J., Quevedo, M., Estruch, S. B., Vino, A., Dekkers, D. H. W., Demmers, J. A. A., Poot, 
R., Deriziotis, P., & Fisher, S. E. (2023). Characterization of the TBR1 interactome: Variants associated with 
neurodevelopmental disorders disrupt novel protein interactions. Human Molecular Genetics, 32(9), 1497–
1510. https://doi.org/10.1093/hmg/ddac311
REFERENCES 
The methods utilized in this study include Simple ClinVar, PolyPhen-2, SIFT, and SWISS 
Modeling. 
• Simple ClinVar was used to determine the genes affiliated with ADHD. Filtering the search to 
missense mutations that had pathogenic, likely pathogenic, uncertain/conflicting, and likely 
benign clinical significance allowed further exploration of the mutations in the selected gene, 
TBR1, that contribute to ADHD.
• PolyPhen-2 and SIFT were used to analyze the pathogenicity of the TBR1 mutations E223Q 
and H681Q and their effect on protein function. 
• Swiss Modeling was used to visualize the structure/homology of the proteins TBR1 codes for.
• The datasets provided by the National Library of Medicine were used to establish the location 
of gene expression, and the conserved domains, and obtain the protein FASTA used in 
PolyPhen-2 and SIFT to specify the TBR1 gene being studied.
METHODS
This research was supported by the Oakwood University 
Biology Department. 
Special thanks to Elaine Vanterpool, PhD. I would also like 
to acknowledge HBCU UP TIP for supporting this project.
ACKNOWLEDGEMENTS  
Mutation Pathogenicity Predictions: PolyPhen-2 and SIFT
Protein Homology
Conserved Domains
Figure 5. SWISS-Model. 3D 
structure homology-mode of the 
protein taken from five varying 
angles.
Domain 1: DNA-binding domain of T-box brain protein 1 and related T-box proteins
TBR1 (also known as T-brain-1 or TES-56) is a neuron-specific transcription factor of the T-box family and involved in forebrain 
development. It has been recognized as a high-confidence risk gene for autism spectrum disorders (ASD); it regulates the expression of ASD-
related genes that are critical for cortical development.
Domain 2: T-box transcription factor-associated
This domain lies downstream of the T-box in many eukaryotic T-box proteins. The exact function is not known.
Figures 1 and 2. PolyPhen-2 and SIFT 
predictions for the pathogenic missense 
mutation at position 223 (Glu to Gln)
Figure 3 and 4. PolyPhen-2 and SIFT predictions 
for the uncertain/conflicting
 missense mutation at position 681 (His to Gln)
