Identification of unique α4 chain structure and conserved antiangiogenic activity of α3NC1 type IV collagen in zebrafish

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dc.citation.firstpage1046en_US
dc.citation.issueNumber7en_US
dc.citation.journalTitleDevelopmental Dynamicsen_US
dc.citation.lastpage1060en_US
dc.citation.volumeNumber252en_US
dc.contributor.authorLeBleu, Valerie S.en_US
dc.contributor.authorDai, Jianlien_US
dc.contributor.authorTsutakawa, Susanen_US
dc.contributor.authorMacDonald, Brian A.en_US
dc.contributor.authorAlge, Joseph L.en_US
dc.contributor.authorSund, Malinen_US
dc.contributor.authorXie, Liangen_US
dc.contributor.authorSugimoto, Hikaruen_US
dc.contributor.authorTainer, Johnen_US
dc.contributor.authorZon, Leonard I.en_US
dc.contributor.authorKalluri, Raghuen_US
dc.date.accessioned2023-08-01T17:29:40Zen_US
dc.date.available2023-08-01T17:29:40Zen_US
dc.date.issued2023en_US
dc.description.abstractBackground Type IV collagen is an abundant component of basement membranes in all multicellular species and is essential for the extracellular scaffold supporting tissue architecture and function. Lower organisms typically have two type IV collagen genes, encoding α1 and α2 chains, in contrast with the six genes in humans, encoding α1–α6 chains. The α chains assemble into trimeric protomers, the building blocks of the type IV collagen network. The detailed evolutionary conservation of type IV collagen network remains to be studied. Results We report on the molecular evolution of type IV collagen genes. The zebrafish α4 non-collagenous (NC1) domain, in contrast with its human ortholog, contains an additional cysteine residue and lacks the M93 and K211 residues involved in sulfilimine bond formation between adjacent protomers. This may alter α4 chain interactions with other α chains, as supported by temporal and anatomic expression patterns of collagen IV chains during the zebrafish development. Despite the divergence between zebrafish and human α3 NC1 domain (endogenous angiogenesis inhibitor, Tumstatin), the zebrafish α3 NC1 domain exhibits conserved antiangiogenic activity in human endothelial cells. Conclusions Our work supports type IV collagen is largely conserved between zebrafish and humans, with a possible difference involving the α4 chain.en_US
dc.identifier.citationLeBleu, Valerie S., Dai, Jianli, Tsutakawa, Susan, et al.. "Identification of unique α4 chain structure and conserved antiangiogenic activity of α3NC1 type IV collagen in zebrafish." <i>Developmental Dynamics,</i> 252, no. 7 (2023) Wiley: 1046-1060. https://doi.org/10.1002/dvdy.590.en_US
dc.identifier.digital2023-LeBleuen_US
dc.identifier.doihttps://doi.org/10.1002/dvdy.590en_US
dc.identifier.urihttps://hdl.handle.net/1911/115036en_US
dc.language.isoengen_US
dc.publisherWileyen_US
dc.rightsExcept where otherwise noted, this work is licensed under a Creative Commons Attribution-NoDerivatives (CC BY-ND) license.  Permission to reuse, publish, or reproduce the work beyond the terms of the license or beyond the bounds of Fair Use or other exemptions to copyright law must be obtained from the copyright holder.en_US
dc.rights.urihttps://creativecommons.org/licenses/by-nc-nd/4.0/en_US
dc.titleIdentification of unique α4 chain structure and conserved antiangiogenic activity of α3NC1 type IV collagen in zebrafishen_US
dc.typeJournal articleen_US
dc.type.dcmiTexten_US
dc.type.publicationpublisher versionen_US
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