{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["94(6)"],"submitter":["Colige A"],"pubmed_abstract":["Procollagen N-proteinase (EC 3.4.24.14) cleaves the amino-propeptides in the processing of type I and type II procollagens to collagens. Deficiencies of the enzyme cause dermatosparaxis in cattle and sheep, and they cause type VIIC Ehlers-Danlos syndrome in humans, heritable disorders characterized by accumulation of pNcollagen and severe skin fragility. Amino acid sequences for the N-proteinase were used to obtain cDNAs from bovine skin. Three overlapping cDNAs had an ORF coding for a protein of 1205 residues. Mammalian cells stably transfected with a complete cDNA secreted an active recombinant enzyme that specifically cleaved type I procollagen. The protein contained zinc-binding sequences of the clan MB of metallopeptidases that includes procollagen C-proteinase/BMP-1. The protein also"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pagination":["2374-9"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC20095"],"repository":["biostudies-literature"],"pubmed_title":["cDNA cloning and expression of bovine procollagen I N-proteinase: a new member of the superfamily of zinc-metalloproteinases with binding sites for cells and other matrix components."],"pmcid":["PMC20095"],"pubmed_authors":["Li SW","Nusgens BV","Lapiere CM","Colige A","Sieron AL","Prockop DJ"],"additional_accession":[]},"is_claimable":false,"name":"cDNA cloning and expression of bovine procollagen I N-proteinase: a new member of the superfamily of zinc-metalloproteinases with binding sites for cells and other matrix components.","description":"Procollagen N-proteinase (EC 3.4.24.14) cleaves the amino-propeptides in the processing of type I and type II procollagens to collagens. Deficiencies of the enzyme cause dermatosparaxis in cattle and sheep, and they cause type VIIC Ehlers-Danlos syndrome in humans, heritable disorders characterized by accumulation of pNcollagen and severe skin fragility. Amino acid sequences for the N-proteinase were used to obtain cDNAs from bovine skin. Three overlapping cDNAs had an ORF coding for a protein of 1205 residues. Mammalian cells stably transfected with a complete cDNA secreted an active recombinant enzyme that specifically cleaved type I procollagen. The protein contained zinc-binding sequences of the clan MB of metallopeptidases that includes procollagen C-proteinase/BMP-1. The protein also","dates":{"release":"1997-01-01T00:00:00Z","publication":"1997 Mar","modification":"2025-04-04T09:42:54.636Z","creation":"2019-03-26T22:29:07Z"},"accession":"S-EPMC20095","cross_references":{"pubmed":["9122202"],"doi":["10.1073/pnas.94.6.2374"]}}