261 research outputs found
Mechanism of human PINK1 activation at the TOM complex by reconstitution
Get PDFLoss of function mutations in PTEN-induced kinase 1 (PINK1) are a frequent cause of earlyonset Parkinson’s disease (PD). Stabilisation of PINK1 at the Translocase of Outer Membrane (TOM) complex of damaged mitochondria is a critical step for its activation. To date the mechanism of how PINK1 is activated in the TOM complex is unclear. Herein we report coexpression of human PINK1 and all seven TOM subunits in Saccharomyces cerevisiae is sufficient for PINK1 activation. We use this reconstitution system to systematically assess the role of each TOM subunit towards PINK1 activation. We unambiguously demonstrate that the TOM20 and TOM70 receptor subunits are required for optimal PINK1 activation and map their sites of interaction with PINK1 using AlphaFold structural modelling and mutagenesis. We also demonstrate an essential role of the pore-containing subunit TOM40 and its structurally associated subunits TOM7 and TOM22 for PINK1 activation. These molecular findings will aid in the development of small molecule activators of PINK1 as a therapeutic strategy for PD
Intracellular-localization of the precursors of type-I-collagen as shown by immunoperoxidasic and immunoradioautographic techniques
No full textPT: J; CR: CARNEIRO J, 1959, EXP CELL RES, V18, P291 CARNEIRO J, 1966, J HISTOCHEM CYTOCHEM, V14, P334 CHUNG E, 1974, SCIENCE, V183, P1200 COURNIL I, 1979, J HISTOCHEM CYTOCHEM, V27, P1059 EPSTEIN EH, 1974, J BIOL CHEM, V249, P3225 FORSGREN A, 1967, J IMMUNOL, V99, P19 KARIM A, 1979, J HISTOCHEM CYTOCHEM, V27, P1070 KEFALIDES NA, 1973, INT REV CONNECTIVE T, V6, P63 LEBLOND CP, 1963, ANN HISTOCHIM, V8, P43 LEBLOND CP, 1980, BASIC MECHANISMS CEL MILLER EJ, 1973, CLIN ORTHOPAEDICS, V92, P260 PAIEMENT J, 1977, J CELL BIOL, V74, P992 PROCKOP DJ, 1979, NEW ENGL J MED, V301, P13 TRAUB W, 1971, ADV PROTEIN CHEM, V25, P243 VONDERMARK K, 1977, DEV BIOL, V59, P75 WEINSTOCK M, 1974, J CELL BIOL, V60, P92 WEINSTOCK M, 1975, EXTRACELLULAR MATRIX, P119 WEINSTOCK M, 1977, J ULTRASTRUCT RES, V61, P218; NR: 18; TC: 5; J9: ACTA HISTOCHEM CYTOCHEM; PG: 12; GA: JM029Source type: Electronic(1
Both Chromosome Decondensation and Condensation Are Dependent on DNA Replication in C.elegans Embryos
Get PDFDuring cell division, chromatin alternates between a condensed state to facilitate chromosome segregation and a decondensed form when DNA replicates. In most tissues, S phase and mitosis are separated by defined G1 and G2 gap phases, but early embryogenesis involves rapid oscillations between replication and mitosis. Using Caenorhabditis elegans embryos as a model system, we show that chromosome condensation and condensin II concentration on chromosomal axes require replicated DNA. Inaddition, we found that, during late telophase, replication initiates on condensed chromosomes and promotes the rapid decondensation of the chromatin.Upon replication initiation, the CDC-45-MCM-GINS (CMG) DNA helicase drives the release of condensin I complexes from chromatin and the activation or displacement of inactive MCM-2-7 complexes, which together with the nucleoporin MEL-28/ELYS tethers condensed chromatin to the nuclear envelope, thereby promoting chromatin decondensation. Our results show how, in an early embryo, the chromosome-condensation cycle is functionally linked with DNA replication. Chromatin organization changes dramatically within a cell cycle. Sonneville etal. find that in rapidly dividing C.elegans embryos, DNA replication initiation triggers rapid decondensation of chromatids. In addition, DNA replication promotes chromosome condensation in prophase. Therefore, the chromosome-condensation cycle and DNA replication are functionally linked.</p
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Eriophyes pyri Pagenstecher 1857
No full textEriophyes pyri (Pagenstecher, 1857) (Fig. 3 C) Type data. Pyrus communis L., pear (Rosaceae); type locality not originally stated by Pagenstecher (1857). Germany was presumed by Amrine and Stasny (1994) based on the working place of the author. Relation to the host plant. The mites inhabit leaf blisters in summer and terminal buds in winter. Smooth pustules along the leaf vein, raised on both sides of the leaf, with their openings on the lamina undersurface; pustules yellowish green at the beginning, later turning red, purple or black at maturity; pustules more or less solid with mites located between the parenchymatic cells (Keifer 1975). Geographic distribution. Nearctic, Neotropical, Palaearctic. New locality record for Iran. 10 females, 2 males and 4 nymphs from Sardrud (38 °01' 36 "N, 46 °09' 35 "E), 1,377 m above sea level, on P. communis, coll. P. Lotfollahi, 1 August 2011. Previous provincial records from Iran. East Azerbaijan, West Azerbaijan, Fars, Esfahan, Guilan, Mazandaran, Hamadan and Tehran, from Amelanchier ovalis Medik., Amelanchier vulgaris Moench, Cotoneaster fontanesii Spach, Cotoneaster nummularius Fisch. & C.A. Mey., Cotoneaster integerrimus Medik., P. communis, Pyrus ussuriensis Maxim., Sorbus americana Marshall var. sitchensis (M. Roem.) Sudw., Sorbus aria Crantz, Sorbus aucuparia L., Sorbus chamaemespilus (L.) Crantz, Sorbus torminalis (L.) Crantz (Khanjani & Haddad 2006). Remarks. This mite was collected from leaf blisters. Based on the large range of host plant species documented, a careful examination of E. pyri populations recorded on different plant hosts should be carried out, combining morphometric studies with biological and molecular data.Published as part of Lotfollahi, Parisa, Irani-Nejad, Karim Haddad & Lillo, Enrico De, 2014, Eriophyoid mites (Acari: Trombidiformes: Eriophyoidea) of Rosales trees in Iran: two new species and three new records in Zootaxa 3861 (1), DOI: 10.11646/zootaxa.3861.1.4, http://zenodo.org/record/22683
Does strict employment protection discourage job creation? Evidence from Croatia
Get PDFEmployment protection legislation in Croatia is among the most strict in Europe. Firing is difficult and costly, and flexible forms of employment are limited. Is this apparent rigidity reflected-as one would expect based on standard economic theory-in low labor market dynamics? Is job creation low and hiring limited? Is the job security of insiders achieved at the cost of outsiders not being able to enter thelabor market? The author attempts to answer these questions by examining job flows. If the employment protection legislation is binding, then job and worker turnover should be low. He shows that this is indeed the case. Hiring is limited and the average job tenure is very long in Croatia. Job destruction is low, however job creation is still lower. The result is accumulation of unemployment, in large part due to new labor market entrants not being able to find a job. The high degree of job protection also seems to strengthen the bargaining position of insiders and results in relatively high wages. So, wages in Croatia are higher than among its competitors, even after adjusting for productivity. These high labor costs are likely to contribute to limited job creation in existing firms, but also are likely to discourage the entry of-and thus job creation in-new firms. The author presents evidence that firm growth has been indeed limited in Croatia, contributing to the low employment level. The author examines other potential causes of high unemployment in Croatia (the unemployment benefit system, labor taxation, the wage structure, and skill and spatial mismatches). He argues that they do not play a substantial part in accounting for poor labor market outcomes in Croatia. The author concludes that the stringent employment protection legislation is the key labor market institution behind low job creation and high unemployment. Based on this he recommends specific measures aimed at liberalizing the labor market to foster job creation and employment.Labor Management and Relations,Labor Policies,Labor Markets,Environmental Economics&Policies,Trade Finance and Investment,Labor Markets,Labor Management and Relations,Labor Standards,Banks&Banking Reform,Environmental Economics&Policies
Indeterminate and Erroneous Fine-Needle Aspirates of Breast with Focus on the 'True Gray Zone': A Review
No full textObjective: To review our experience and the literature on inconclusive-erroneous fine-needle aspirates (FNAs) of breast with the focus on the 'true gray zone'. To describe the cytology, differential diagnosis, pitfalls and limitations of common and rare lesions. Study Design: We conducted a literature search focusing on breast FNAs with statistical data of C3 and C4 categories including false-positive and false-negative cases. Similar data from 2003 to 2009 was obtained from our institution. Results: C3 and C4 categories account for 3-17percent of breast FNAs. Contributing factors are technical difficulties, inexperienced pathologists interpreting FNAs of breast and overlap of cytologic features of certain benign and malignant conditions; this last, 'true gray zone' accounts for 2percent of cases. Fibroadenoma, proliferative breast lesions, gynecomastia, infiltrating and in situ low-grade adenocarcinomas and tubular, cribriform, lobular and mucinous carcinomas are the most common problematic lesions. Granular cell tumor, adenomyoepithelioma, pregnancy-related lesions, fat necrosis, inflammatory and radiation changes, adenoid cystic carcinoma, spindle-cell lesions and Phyllodes tumor are less common. Conclusion: Inconclusive-erroneous FNAs of breast due to the 'true gray zone' are rare. Most are due to the overlapping cytologic features of some benign and malignant conditions. Practical features that may help arrive at the correct diagnoses are elucidated. Copyright © 2013 S. Karger AG, Basel.Abd el-All Howayda S, 2006, Diagn Pathol, V1, P13, DOI 10.1186-1746-1596-1-13; ABENDROTH CS, 1991, AM J CLIN PATHOL, V96, P654; Adeniran Adebowale, 2004, Breast J, V10, P528, DOI 10.1111-j.1075-122X.2004.21525.x; ALKAISI N, 1994, ACTA CYTOL, V38, P898; Alvarez-Rodriguez F, 2012, ACTA CYTOL, V56, P501, DOI 10.1159-000341626; Amrikachi M, 2001, ACTA CYTOL, V45, P948; Abati A, 1997, DIAGN CYTOPATHOL, V16, P295; Aydin O, 2001, DIAGN CYTOPATHOL, V25, P194, DOI 10.1002-dc.2036; BARDALES RH, 1994, DIAGN CYTOPATHOL, V10, P336, DOI 10.1002-dc.2840100409; BENOIT JL, 1992, DIAGN CYTOPATHOL, V8, P643, DOI 10.1002-dc.2840080623; Bhattarai S, 2000, ACTA CYTOL, V44, P790; Bibbo M, 2008, COMPREHENSIVE CYTOPA, P715; BIBBO M, 1988, ACTA CYTOL, V32, P193; BONDESON L, 1990, ACTA CYTOL, V34, P15; Bonzanini M, 1997, DIAGN CYTOPATHOL, V17, P353, DOI 10.1002-(SICI)1097-0339(199711)17:5353::AID-DC83.0.CO;2-B; Cai GP, 2004, DIAGN CYTOPATHOL, V30, P396, DOI 10.1002-dc.20069; Cangiarella J, 2003, ACTA CYTOL, V47, P965, DOI 10.1159-000326669; Cangiarella J, 2001, DIAGN CYTOPATHOL, V25, P311, DOI 10.1002-dc.2161; Chaiwun B., 2005, SMJ Singapore Medical Journal, V46, P706; Chang A, 2002, DIAGN CYTOPATHOL, V26, P191, DOI 10.1002-dc.10073; Chhieng DC, 1999, CANCER CYTOPATHOL, V87, P359, DOI 10.1002-(SICI)1097-0142(19991225)87:6359::AID-CNCR73.0.CO;2-7; Cho EY, 2001, ACTA CYTOL, V45, P353; Choi YD, 2004, ACTA CYTOL, V48, P801, DOI 10.1159-000326449; Choudhury M, 2001, Indian J Pathol Microbiol, V44, P445; Davis WG, 2005, AM J SURG PATHOL, V29, P1456, DOI 10.1097-01.pas.0000176431.96326.49; Deb RA, 2001, CYTOPATHOLOGY, V12, P219, DOI 10.1046-j.1365-2303.2001.00332.x; Dei Tos Angelo P., 1994, Diagnostic Cytopathology, V11, P146; DELATORRE M, 1994, ACTA CYTOL, V38, P884; DeMay R M, 1984, Pathol Annu, V19 Pt 2, P121; DORNFELD JM, 1992, DIAGN CYTOPATHOL, V8, P79, DOI 10.1002-dc.2840080117; DUANE GB, 1987, ACTA CYTOL, V31, P742; DUSENBERY D, 1992, ACTA CYTOL, V36, P215; Eckert R, 1999, DIAGN CYTOPATHOL, V21, P105, DOI 10.1002-(SICI)1097-0339(199908)21:2105::AID-DC53.0.CO;2-G; FARMER C, 1995, DIAGN CYTOPATHOL, V12, P51, DOI 10.1002-dc.2840120112; Feichter GE, 1997, ACTA CYTOL, V41, P327; Field A, 2007, DIAGN CYTOPATHOL, V35, P386, DOI 10.1002-dc.20652; FILOMENA CA, 1992, DIAGN CYTOPATHOL, V8, P327, DOI 10.1002-dc.2840080404; FISHER CJ, 1992, HISTOPATHOLOGY, V21, P69; Garijo MF, 2008, PATHOL INT, V58, P787, DOI 10.1111-j.1440-1827.2008.02312.x; Gobbi H, 2000, AM J CLIN PATHOL, V113, P288; GREENBERG ML, 1994, DIAGN CYTOPATHOL, V11, P188, DOI 10.1002-dc.2840110216; Greenberg ML, 1997, DIAGN CYTOPATHOL, V16, P537, DOI 10.1002-(SICI)1097-0339(199706)16:6537::AID-DC133.3.CO;2-C; GRENKO RT, 1990, ACTA CYTOL, V34, P21; Gupta D, 1999, ACTA CYTOL, V43, P191; Gupta RK, 2010, ACTA CYTOL, V54, P138, DOI 10.1159-000324998; Gupta RK, 1997, ACTA CYTOL, V41, P1139; Gupta RK, 1999, DIAGN CYTOPATHOL, V20, P82, DOI 10.1002-(SICI)1097-0339(199902)20:282::AID-DC83.0.CO;2-0; GUPTA RK, 1993, DIAGN CYTOPATHOL, V9, P156, DOI 10.1002-dc.2840090209; Haji BE, 2007, DIAGN CYTOPATHOL, V35, P408, DOI 10.1002-dc.20661; Harada O, 2011, J CLIN PATHOL, V64, P776, DOI 10.1136-jclinpath-2011-200094; Howell LP, 1999, DIAGN CYTOPATHOL, V21, P217, DOI 10.1002-(SICI)1097-0339(199909)21:3217::AID-DC153.0.CO;2-7; INGRAM DL, 1984, ARCH PATHOL LAB MED, V108, P897; Ishihara A, 2006, DIAGN CYTOPATHOL, V34, P373, DOI 10.1002-dc.20445; Ishikawa Takashi, 2007, Breast Cancer, V14, P388, DOI 10.2325-jbcs.14.388; Iwa N, 2009, DIAGN CYTOPATHOL, V37, P143, DOI 10.1002-dc.20911; Iyengar P, 2006, CANCER CYTOPATHOL, V108, P250, DOI 10.1002-cncr.21839; Jamal AA, 2001, SAUDI MED J, V22, P67; Jayaram G, 2007, ACTA CYTOL, V51, P3, DOI 10.1159-000325674; Kanhoush R, 2004, CANCER CYTOPATHOL, V102, P164, DOI 10.1002-cncr.20283; Kapila K, 2002, CYTOPATHOLOGY, V13, P300, DOI 10.1046-j.1365-2303.2002.00423.x; Kasagawa Takahiro, 2006, Breast Cancer, V13, P112, DOI 10.2325-jbcs.13.112; Khirwadkar N, 2005, ACTA CYTOL, V49, P344; KLINE TS, 1981, ACTA CYTOL, V25, P263; Klopcic U, 2009, ACTA CYTOL, V53, P109, DOI 10.1159-000325095; Kollur SM, 2006, CYTOPATHOLOGY, V17, P239, DOI 10.1111-j.1365-2303.2006.00360.x; Krishnamurthy S, 2000, CANCER CYTOPATHOL, V90, P342, DOI 10.1002-1097-0142(20001225)90:6342::AID-CNCR43.0.CO;2-I; Kundu UR, 2012, AM J CLIN PATHOL, V138, P96, DOI 10.1309-AJCP8MN5GXFZULRD; Kurashina M, 2002, DIAGN CYTOPATHOL, V26, P29, DOI 10.1002-dc.10037; Laforga JBM, 1998, DIAGN CYTOPATHOL, V19, P55, DOI 10.1002-(SICI)1097-0339(199807)19:155::AID-DC113.0.CO;2-7; LAMB J, 1994, CYTOPATHOLOGY, V5, P17, DOI 10.1111-j.1365-2303.1994.tb00123.x; Landeyro J, 2012, DIAGN CYTOPATHOL, V40, P1107, DOI 10.1002-dc.21720; Layfield LJ, 1996, DIAGN CYTOPATHOL, V15, P250, DOI 10.1002-(SICI)1097-0339(199609)15:3250::AID-DC153.0.CO;2-F; Lee WY, 2000, ACTA CYTOL, V44, P488; LILLENG R, 1992, ACTA CYTOL, V36, P48; Lopez-Ferrer P, 1999, ACTA CYTOL, V43, P579; Lui PCW, 2007, J CLIN PATHOL, V60, P529, DOI 10.1136-jcp.2006.039412; Magro G, 2008, ARCH PATHOL LAB MED, V132, P1813, DOI 10.1043-1543-2165-132.11.1813; Mak A, 2006, DIAGN CYTOPATHOL, V34, P818, DOI 10.1002-dc.20560; Martin-Bates E, 1990, Cytopathology, V1, P79, DOI 10.1111-j.1365-2303.1990.tb00332.x; MartinezParra D, 1997, DIAGN CYTOPATHOL, V17, P108, DOI 10.1002-(SICI)1097-0339(199708)17:2108::AID-DC53.0.CO;2-C; McKee GT, 1999, CANCER CYTOPATHOL, V87, P203, DOI 10.1002-(SICI)1097-0142(19990825)87:4203::AID-CNCR73.3.CO;2-5; Mehrotra Ravi, 2004, Indian J Pathol Microbiol, V47, P377; Mercado CL, 2007, DIAGN CYTOPATHOL, V35, P690, DOI 10.1002-dc.20722; Michael CW, 2002, CANCER CYTOPATHOL, V96, P92, DOI 10.1002-cncr.10481; Mitre BK, 1997, ACTA CYTOL, V41, P1121; Mooney EE, 1998, DIAGN CYTOPATHOL, V19, P317, DOI 10.1002-(SICI)1097-0339(199810)19:4317::AID-DC203.0.CO;2-P; Ng WK, 2002, ACTA CYTOL, V46, P317, DOI 10.1159-000326728; Ng WK, 2001, ACTA CYTOL, V45, P593; Nggada H A, 2007, Afr J Med Med Sci, V36, P295; NIEMANN TH, 1995, DIAGN CYTOPATHOL, V12, P245, DOI 10.1002-dc.2840120311; NILSSON B, 1994, ACTA CYTOL, V38, P431; Nogueira M, 1998, CYTOPATHOLOGY, V9, P291, DOI 10.1046-j.1365-2303.1998.00118.x; NOVOTNY DB, 1991, ACTA CYTOL, V35, P676; ONeil S, 1997, SURGERY, V122, P824, DOI 10.1016-S0039-6060(97)90093-3; PETERSE JL, 1989, SEMIN DIAGN PATHOL, V6, P126; PETERSE JL, 1989, ACTA CYTOL, V33, P176; PHILLIPSON J, 1994, ACTA CYTOL, V38, P479; PINEDO F, 1991, ACTA CYTOL, V35, P229; Poniecka AW, 2001, ACTA CYTOL, V45, P797; RO JY, 1991, ARCH PATHOL LAB MED, V115, P137; ROGERS LA, 1992, AM J CLIN PATHOL, V98, P155; Rosa M, 2012, DIAGN CYTOPATHOL, V40, P26, DOI 10.1002-dc.21497; Rosa M, 2012, DIAGN CYTOPATHOL, V40, P179, DOI 10.1002-dc.21601; RUSSIN VL, 1989, DIAGN CYTOPATHOL, V5, P243, DOI 10.1002-dc.2840050303; Saad RS, 2012, DIAGN CYTOPATHOL, V40, P1005, DOI 10.1002-dc.21705; Saqi A, 2004, DIAGN CYTOPATHOL, V30, P271, DOI 10.1002-dc.20015; Sauer T, 2005, CANCER CYTOPATHOL, V105, P21, DOI 10.1002-cncr.20735; Shabb NS, 1997, ACTA CYTOL, V41, P321; Sidawy M, 2007, VOLUME SERIES FDN DI; Sidawy MK, 1998, DIAGN CYTOPATHOL, V18, P150, DOI 10.1002-(SICI)1097-0339(199802)18:2150::AID-DC123.0.CO;2-K; Siddiqui MT, 2002, DIAGN CYTOPATHOL, V26, P87, DOI 10.1002-dc-10066; SILVERMAN JF, 1993, DIAGN CYTOPATHOL, V9, P713, DOI 10.1002-dc.2840090623; Simsir A, 2003, CANCER CYTOPATHOL, V99, P156, DOI 10.1002-cncr.11062; Simsir A, 2012, DIAGN CYTOPATHOL, V40, P262, DOI 10.1002-dc.21630; Simsir A, 2009, DIAGN CYTOPATHOL, V37, P140, DOI 10.1002-dc.20987; Simsir A, 2001, DIAGN CYTOPATHOL, V25, P278, DOI 10.1002-dc.2055; Singh R, 2012, DIAGN CYTOPATHOL, V40, P113, DOI 10.1002-dc.21507; SNEIGE N, 1993, DIAGN CYTOPATHOL, V9, P106, DOI 10.1002-dc.2840090122; SNEIGE N, 1994, HUM PATHOL, V25, P485, DOI 10.1016-0046-8177(94)90120-1; STANLEY MW, 1989, DIAGN CYTOPATHOL, V5, P134, DOI 10.1002-dc.2840050205; STANLEY MW, 1993, DIAGN CYTOPATHOL, V9, P184, DOI 10.1002-dc.2840090215; STANLEY MW, 1990, DIAGN CYTOPATHOL, V6, P375, DOI 10.1002-dc.2840060602; STROBEL SL, 1985, ACTA CYTOL, V29, P598; THOMAS PA, 1994, DIAGN CYTOPATHOL, V11, P301, DOI 10.1002-dc.2840110321; VALENTE PT, 1994, DIAGN CYTOPATHOL, V10, P165, DOI 10.1002-dc.2840100215; Vicandi B, 2004, CYTOPATHOLOGY, V15, P321, DOI 10.1111-j.1365-2303.2004.00166.x; WEAVER MG, 1993, PATHOL RES PRACT, V189, P873; Westenend PJ, 2002, CANCER CYTOPATHOL, V96, P101, DOI 10.1002-cncr.10483; WILLIS SL, 1995, ACTA CYTOL, V39, P8580
CMG helicase disassembly is controlled by replication fork DNA, replisome components and a ubiquitin threshold
Get PDFThe eukaryotic replisome assembles around the CMG helicase, which stably associates with DNA replication forks throughout elongation. When replication terminates, CMG is ubiquitylated on its Mcm7 subunit and disassembled by the Cdc48/p97 ATPase. Until now, the regulation that restricts CMG ubiquitylation to termination was unknown, as was the mechanism of disassembly. By reconstituting these processes with purified budding yeast proteins, we show that ubiquitylation is tightly repressed throughout elongation by the Y-shaped DNA structure of replication forks. Termination removes the repressive DNA structure, whereupon long K48-linked ubiquitin chains are conjugated to CMG-Mcm7, dependent on multiple replisome components that bind to the ubiquitin ligase SCF Dia2. This mechanism pushes CMG beyond a ‘5-ubiquitin threshold’ that is inherent to Cdc48, which specifically unfolds ubiquitylated Mcm7 and thereby disassembles CMG. These findings explain the exquisite regulation of CMG disassembly and provide a general model for the disassembly of ubiquitylated protein complexes by Cdc48. </p
Mixing effect on thermophilic anaerobic digestion of source-sorted organic fraction of municipal solid waste
No full textThis paper examines the effect of mixing on the performance of thermophilic anaerobic digestion of source-sorted organic fraction of municipal solid waste during the start-up phase and in the absence of an acclimated seed. For this purpose, two digesters were used under similar starting conditions and operated for 235days with different mixing schemes. While both digesters exhibited a successful startup with comparable specific methane yield of 0.327 and 0.314l CH 4-gVS, continuous slow stirring improved stability by reducing average VFA accumulation from 2890 to 825mg HAc-l, propionate content from 2073 to 488mg-l, and VFA-to-alkalinity ratio from 0.32 to 0.07. As a result, the startup with slow mixing was faster and smoother accomplishing a higher loading capacity of 2.5gVS-l-d in comparison to 1.9gVS-l-d for non-mixing. Mixing equally improved microbial abundance from 6.6 to 10gVSS-l and enhanced solids and soluble COD removal. © 2012 Elsevier Ltd.Angelidaki I, 2006, WATER RES, V40, P2621, DOI 10.1016-j.watres.2006.05.015; ANGELIDAKI I, 1993, BIOTECHNOL BIOENG, V42, P159, DOI 10.1002-bit.260420203; APHA AWWA WEF, 1998, STAND METH EX WAT WA; Banks CJ, 2008, WATER SCI TECHNOL, V58, P1475, DOI 10.2166-wst.2008.513; Bouskova A, 2005, WATER RES, V39, P1481, DOI 10.1016-j.watres.2004.12.042; Bridgeman J, 2012, ADV ENG SOFTW, V44, P54, DOI 10.1016-j.advengsoft.2011.05.037; Chelliapan S, 2011, DESALINATION, V271, P257, DOI 10.1016-j.desal.2010.12.045; Chen AC, 2003, BIOTECHNOL LETT, V25, P719, DOI 10.1023-A:1023458631699; Conklin AS, 2008, WATER RES, V42, P4895, DOI 10.1016-j.watres.2008.09.024; Elnekave M, 2006, FRESEN ENVIRON BULL, V15, P1098; Ferrer I, 2010, BIORESOURCE TECHNOL, V101, P2972, DOI 10.1016-j.biortech.2009.12.006; Gerardi M.H, 2003, MICROBIOLOGY ANAEROB; Gomez X, 2006, RENEW ENERG, V31, P2017, DOI 10.1016-j.renene.2005.09.029; Halalsheh M, 2011, BIORESOURCE TECHNOL, V102, P748, DOI 10.1016-j.biortech.2010.08.075; Hawkes FR, 2007, INT J HYDROGEN ENERG, V32, P172, DOI 10.1016-j.ijhydene.2006.08.014; Ike M, 2010, BIORESOURCE TECHNOL, V101, P3952, DOI 10.1016-j.biortech.2010.01.028; Kaparaju P, 2008, BIORESOURCE TECHNOL, V99, P4919, DOI 10.1016-j.biortech.2007.09.015; Karim K, 2005, WATER RES, V39, P3597, DOI 10.1016-j.watres.2005.06.019; Kim M, 2002, WATER RES, V36, P4369, DOI 10.1016-S0043-1354(02)00147-1; Kim SH, 2006, PROCESS BIOCHEM, V41, P199, DOI 10.1016-j.procbio.2005.06.013; Neumann L, 2011, BIORESOURCE TECHNOL, V102, P2931, DOI 10.1016-j.biortech.2010.11.068; Pandey PK, 2011, BIOMASS BIOENERG, V35, P2705, DOI 10.1016-j.biombioe.2011.03.017; Pavan P, 2000, WATER SCI TECHNOL, V41, P75; Penteado TZ, 2011, WATER SCI TECHNOL, V63, P995, DOI 10.2166-wst.2011.281; RIPLEY LE, 1986, J WATER POLLUT CON F, V58, P406; Sanchez E, 2005, BIORESOURCE TECHNOL, V96, P335, DOI 10.1016-j.biortech.2004.04.003; Steinberg LM, 2011, BIORESOURCE TECHNOL, V102, P8790, DOI 10.1016-j.biortech.2011.07.017; Stroot PG, 2001, WATER RES, V35, P1804, DOI 10.1016-S0043-1354(00)00439-5; Sung SW, 2003, CHEMOSPHERE, V53, P43, DOI 10.1016-S0045-6535(03)00434-X; Suwannoppadol S, 2011, BIORESOURCE TECHNOL, V102, P7762, DOI 10.1016-j.biortech.2011.06.008; Ward AJ, 2008, BIORESOURCE TECHNOL, V99, P7928, DOI 10.1016-j.biortech.2008.02.044; Wu SY, 2008, INT J HYDROGEN ENERG, V33, P1542, DOI 10.1016-j.ijhydene.2007.10.020; Zabranska J, 2002, WATER SCI TECHNOL, V46, P447; Zhang M.-L., 2009, WATER RES, V4, P1923; Zhang ZP, 2006, PROCESS BIOCHEM, V41, P2118, DOI 10.1016-j.procbio.2006.05.02112121
Factors affecting the infant antibody response to measles immunisation in Entebbe-Uganda.
Get PDFBACKGROUND: Vaccine failure is an important concern in the tropics with many contributing elements. Among them, it has been suggested that exposure to natural infections might contribute to vaccine failure and recurrent disease outbreaks. We tested this hypothesis by examining the influence of co-infections on maternal and infant measles-specific IgG levels. METHODS: We conducted an observational analysis using samples and data that had been collected during a larger randomised controlled trial, the Entebbe Mother and Baby Study (ISRCTN32849447). For the present study, 711 pregnant women and their offspring were considered. Helminth infections including hookworm, Schistosoma mansoni and Mansonella perstans, along with HIV, malaria, and other potential confounding factors were determined in mothers during pregnancy and in their infants at age one year. Infants received their measles immunisation at age nine months. Levels of total IgG against measles were measured in mothers during pregnancy and at delivery, as well as in cord blood and from infants at age one year. RESULTS: Among the 711 pregnant women studied, 66% had at least one helminth infection at enrolment, 41% had hookworm, 20% M. perstans and 19% S. mansoni. Asymptomatic malaria and HIV prevalence was 8% and 10% respectively. At enrolment, 96% of the women had measles-specific IgG levels considered protective (median 4274 mIU/ml (IQR 1784, 7767)). IgG levels in cord blood were positively correlated to maternal measles-specific IgG levels at delivery (r = 0.81, p < 0.0001). Among the infants at one year of age, median measles-specific IgG levels were markedly lower than in maternal and cord blood (median 370 mIU/ml (IQR 198, 656) p < 0.0001). In addition, only 75% of the infants had measles-specific IgG levels considered to be protective. In a multivariate regression analysis, factors associated with reduced measles-specific antibody levels in infancy were maternal malaria infection, infant malaria parasitaemia, infant HIV and infant wasting. There was no association with maternal helminth infection. CONCLUSION: Malaria and HIV infection in mothers during pregnancy, and in their infants, along with infant malnutrition, may result in reduction of the antibody response to measles immunisation in infancy. This re-emphasises the importance of malaria and HIV control, and support for infant nutrition, as these interventions may have benefits for vaccine efficacy in tropical settings
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