Biosynthesis and assembly of the Collagen IV-like protein Pericardin in Drosophila melanogaster

DC FieldValueLanguage
dc.contributor.authorWilmes, Ariane C.
dc.contributor.authorKlinke, Nora
dc.contributor.authorRotstein, Barbara
dc.contributor.authorMeyer, Heiko
dc.contributor.authorPaululat, Achim
dc.date.accessioned2021-12-23T15:59:57Z-
dc.date.available2021-12-23T15:59:57Z-
dc.date.issued2018
dc.identifier.issn20466390
dc.identifier.urihttps://osnascholar.ub.uni-osnabrueck.de/handle/unios/4248-
dc.description.abstractIn Drosophila, formation of the cardiac extracellular matrix (ECM) starts during embryogenesis. Assembly and incorporation of structural proteins such as Collagen IV, Pericardin, and Laminin A, B1, and B2 into the cardiac ECM is critical to the maintenance of heart integrity and functionality and, therefore, to longevity of the animal. The cardiac ECM connects the heart tube with the alary muscles; thus, the ECM contributes to a flexible positioning of the heart within the animal's body. Moreover, the cardiac ECM holds the larval pericardial nephrocytes in close proximity to the heart tube and the inflow tract, which is assumed to be critical to efficient haemolymph clearance. Mutations in either structural ECM constituents or ECM receptors cause breakdown of the ECM network upon ageing, with disconnection of the heart tube from alary muscles becoming apparent at larval stages. Finally, the heart becomes non-functional. Here, we characterised existing and new pericardin mutants and investigated biosynthesis, secretion, and assembly of Pericardin in matrices. We identified two new pericardin alleles, which turned out to be a null (pericardin(3-548)) and a hypomorphic allele (pericardin(3-21)). Both mutants could be rescued with a genomic duplication of a fosmid coding for the pericardin locus. Biochemical analysis revealed that Pericardin is highly glycosylated and forms redox-dependent multimers. Multimer formation is remarkably reduced in animals deficient for the prolyl-4 hydroxylase cluster at 75D3-4.
dc.description.sponsorshipDeutsche ForschungsgemeinschaftGerman Research Foundation (DFG) [DFG PA 13-1, SFB 944 TP7, SFB 944 Z-Project]; Deutscher Akademischer Austauschdienst (ProCope program), the State of Lower-SaxonyDeutscher Akademischer Austausch Dienst (DAAD) [ZN2832]; Osnabruck University; This work was supported by grants from Deutsche Forschungsgemeinschaft to A.P. (DFG PA 13-1, SFB 944 TP7, SFB 944 Z-Project), Deutscher Akademischer Austauschdienst (ProCope program), the State of Lower-Saxony (ZN2832) and Osnabruck University (Open Access Publishing Fund).
dc.language.isoen
dc.publisherCOMPANY BIOLOGISTS LTD
dc.relation.ispartofBIOLOGY OPEN
dc.subjectBiology
dc.subjectCardiac matrix
dc.subjectCardiogenesis
dc.subjectCELLS
dc.subjectCellular biology
dc.subjectDevelopmental biology
dc.subjectDorsal vessel
dc.subjectENZYMES
dc.subjectEXPRESSION
dc.subjectExtracellular matrix
dc.subjectGENE DISRUPTION PROJECT
dc.subjectHeart
dc.subjectLife Sciences & Biomedicine - Other Topics
dc.subjectMORPHOGENESIS
dc.subjectMUTATIONS
dc.subjectPericardin
dc.subjectPROCOLLAGEN
dc.subjectPROLYL 4-HYDROXYLASE
dc.subjectROLES
dc.subjectSECRETION
dc.titleBiosynthesis and assembly of the Collagen IV-like protein Pericardin in Drosophila melanogaster
dc.typejournal article
dc.identifier.doi10.1242/bio.030361
dc.identifier.isiISI:000434211800004
dc.description.volume7
dc.description.issue4
dc.contributor.orcid0000-0002-8845-6859
dc.publisher.placeBIDDER BUILDING, STATION RD, HISTON, CAMBRIDGE CB24 9LF, ENGLAND
dcterms.isPartOf.abbreviationBiol. Open
dcterms.oaStatusGreen Published, gold
crisitem.author.deptFB 05 - Biologie/Chemie-
crisitem.author.deptidfb05-
crisitem.author.orcid0000-0002-8845-6859-
crisitem.author.parentorgUniversität Osnabrück-
crisitem.author.netidPaAc947-
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