44 research outputs found
Complementary feed for the control of pruritus in atopic dermatitis in dogs
No full textPruritus is a common manifestation in dogs with allergic skin diseases and itching can significantly affect the
quality of life of both affected animals and their owners, with even severe repercussions [1]. Pharmacological treatments and complementary feeds that are able to control itching quickly and in the long run are in great demand
and attract the attention of many researchers and companies. The aim of this study was to assess the effectiveness
of a complementary feed containing flavonoids, stilbenes, and cannabinoids (obtained from vegetable/botanical by- products/vegetable/botanical source) in the control of itching in dogs suffering from atopic dermatitis. Such complementary feed has been shown to be able to reduce the gene expression of ccl2, ccl17, il31ra and tslp in an experimental in vitro model of atopic dermatitis [3]. The primary efficacy endpoint was the reduction of CADESI-04
and pruritus visual analogue scale (pVas) scores. The study protocol was successfully submitted to the Animal Welfare Body of the University of Camerino (protocol code 10/2021). Ten dogs affected by atopic dermatitis, diagnosed according to current guidelines [1, 2], received a hypoallergenic food for the duration of the study. Once enrolled, in the first 6 weeks dogs received the administration of oclacitinib (Apoquel®, Zoetis) twice daily for two weeks and then once daily for 4 weeks. Starting from the fifth week, the administration of complementary feed began, according to the following dosage: twice daily for two weeks and then once daily for 8 weeks. Administration
of oclacitinib was discontinued at week 6 in all dogs enrolled in the study, who received the complementary feed up to week 12. In all dogs there was a marked reduction in both CADESI-04 and owner-reported pVas for pruritus in
the first four weeks of oclacitinib administration. In the fifth and sixth week of the study (oclacitinib + complementary feed) the trend of CADESI-04 and pVas was the same, as well as from the seventh week onwards for all dogs enrolled in the study. Although data collected are only preliminary, it is possible to highlight that the
complementary feed effectively control itching in supplemented dogs, which did not show any adverse event. This study further confirm the ability of selected complementary feed to control dermatological disease manifestation in dogs [4].
COMPLEMENTARY FEED FOR THE CONTROL OF PRURITUS IN ATOPIC DERMATITIS IN DOGS
Andrea Marchegiani (1), Alessandro Fruganti (1), Elena Dalle Vedove (2), Benedetta Bachetti (2), Marcella Massimini (2), Cataldo Ribecco (2), Matteo Cerquetella (1), AndreaSpaterna (1)
(1) Università degli Studi di Camerino, Scuola di Bioscienze e Medicina Veterinaria. (2) Research and Development Unit (NIL), C.I.A.M. srl.
Corresponding author: A. Marchegiani ([email protected])
[1] Favrot C et al. A prospective study on the clinical features of chronic canine atopic dermatitis and its diagnosis. Vet Dermatol, 21:23–31, 2010.
[2] Hensel P et al. Canine atopic dermatitis: detailed guidelines for diagnosis and allergen identification. BMC Vet Res, 11(1):196, 2015.
[3] Massimini M et al. Polyphenols and Cannabidiol Modulate Transcriptional Regulation of Th1/Th 2 Inflammatory Genes Related to Canine Atopic Dermatitis. Front Vet Sci, 8:1–14, 2021.
[ 4] M arc hegi ani A et al . Im pac t o f N utri ti o na l Supplementation on Canine Dermatological Disorders. Vet Sci MDPI, 38:1–13, 2020
Crystal structure of the deglycating enzyme Amadoriase I in its free form and substrate-bound complex
No full textAmadoriases, also known as fructosyl amine oxidases (FAOX), are enzymes that catalyze the de-glycosylation of fructosyl amino acids. As such, they are excellent candidates for the development of enzyme-based diagnostic and therapeutic tools against age-and diabetes-induced protein glycation. However, mostly because of the lack of a complete structural characterization of the different members of the family, the molecular bases of their substrate specificity have yet to be fully understood. The high resolution crystal structures of the free and the substrate-bound form of Amadoriase I shown herein allow for the identification of key structural features that account for the diverse substrate specificity shown by this class of enzymes. This is of particular importance in the context of the rather limited and partially incomplete structural information that has so far been available in the literature on the members of the FAOX family. Moreover, using molecular dynamics simulations, we describe the tunnel conformation and the free energy profile experienced by the ligand in going from bulk water to the catalytic cavity, showing the presence of four gating helices/loops, followed by an "L-shaped" narrow cavity. In summary, the tridimensional architecture of Amadoriase I presented herein provides a reference structural framework for the design of novel enzymes for diabetes monitoring and protein deglycation. (C) 2016 Wiley Periodicals, Inc
Collagen glycation and deglycation. Candidate locations of collagen non-enzymatic glycation and characterization of an Amadoriase enzyme for its prevention.
No full textEnzymatic deglycation of proteins: crystal structure and computational characterization of Amadoriase I
No full textThe crystal structure of the deglycating enzyme Amadoriase I provides nover insights for the development of therapeutic tools against ages and diabetes-induced protein glycation
No full textThe X-ray structure of human P-cadherin EC1-EC2 in a closed conformation provides insight into the type I cadherin dimerization pathway
No full textCadherins are a large family of calcium-dependent proteins that mediate cellular adherens junction formation and tissue morphogenesis. To date, the most studied cadherins are those classified as classical, which are further divided into type I or type II depending on selected sequence features. Unlike other members of the classical cadherin family, a detailed structural characterization of P-cadherin has not yet been fully obtained. Here, the high-resolution crystal structure determination of the closed form of human P-cadherin EC1-EC2 is reported. The structure shows a novel, monomeric packing arrangement that provides a further snapshot in the yet-to-be-achieved complete description of the highly dynamic cadherin dimerization pathway. Moreover, this is the first multidomain cadherin fragment to be crystallized and structurally characterized in its closed conformation that does not carry any extra N-terminal residues before the naturally occurring aspartic acid at position 1. Finally, two clear alternate conformations are observed for the critical Trp2 residue, suggestive of a transient, metastable state. The P-cadherin structure and packing arrangement shown here provide new and valuable information towards the complete structural characterization of the still largely elusive cadherin dimerization pathway
Crystal structure and computational characterization of Amadoriase I, a strategy for protein deglycation
No full textBiochemical and cellular mechanism of protein kinase CK2 inhibition by deceptive curcumin
No full textProtein kinase CK2 is an antiapoptotic cancer-sustaining protein. Cur-cumin, reported previously as a CK2 inhibitor, is too bulky to be accom-modated in the CK2 active site and rapidly degrades in solution generatingvarious ATP-mimetic inhibitors; with a detailed comparative analysis, bymeans of both protein crystallography and enzymatic inhibition, ferulicacid was identified as the principal curcumin degradation product responsi-ble for CK2 inhibition. The other curcumin derivatives vanillin, feruloyl-methane and coniferyl aldehyde are weaker CK2 inhibitors. The highinstability of curcumin in standard buffered solutions flags this compound,which is included in many commercial libraries, as a possible source of mis-leading interpretations, as was the case for CK2. Ferulic acid does notshow any cytotoxicity and any inhibition of cellular CK2, due to its poorcellular permeability. However, curcumin acts as a prodrug in the cellularcontext, by generating its degradation products inside the treated cells, thusrescuing CK2 inhibition and consequently inducing cell death. Through theintracellular release of its degradation products, curcumin is expected toaffect various target families; here, we identify the first bromodomain ofBRD4 as a new target for those compounds
Impact of Nutritional Supplementation on Canine Dermatological Disorders
No full textNutritional supplements, also known as complementary feeds, are products administered with the aim of furnishing health benefits, regardless of nutritional needs. They have been used since ancient times in veterinary dermatology, and a number of studies have focused on investigating the health benefits of some ingredients found in commercially available complementary feed for dogs. The aim of this paper is to review the literature available on the use of nutritional supplementation for the management of canine skin diseases, critically appraising the clinical efficacy of such interventions and summarizing the current state of knowledge. This review highlights how these feeds can be considered useful in the management of dermatological disorders and outlines their beneficial effects in the prevention of dietary deficiencies and treatment of diseases, alone, or in addition to conventional pharmacological therapy. In recent years, nutritional supplements have found increasing potential application in veterinary medicine, and the scientific proofs of their beneficial effects are described in this review
