title: Type I procollagen COOH-terminal proteinase enhancer protein: identification, primary structure, and chromosomal localization of the cognate human gene (PCOLCE).
abstract: Type I procollagen COOH-terminal proteinase (C-proteinase) enhancer, a glycoprotein that binds to the COOH-terminal propeptide of type I procollagen and enhances procollagen C-proteinase activity, was purified from mouse fibroblast culture media. Partial amino acid sequences obtained from proteolytic fragments were found to have identity with the deduced amino acid sequence of a cDNA clone of unknown function, previously isolated from a mouse astrocyte library. Sequences of mouse enhancer cDNA, obtained in the present study, predict a approximately 50-kDa, 468-amino acid protein that differs from the 43-kDa, 402-amino acid protein predicted by the previously reported astrocyte-derived clone. Human cDNAs encode an enhancer of 449 amino acids. Previous biochemical studies have found the mouse enhancer as a 55-kDa form, which is readily processed to 36- and 34-kDa forms, retaining full C-proteinase enhancing activity and the ability to bind the COOH-terminal propeptide. Data presented here show the 36-kDa form to correspond to the amino-terminal portion of the 55-kDa protein. This is the most conserved region between mouse and human enhancers, comprising two domains with homology to domains found in a number of proteases and proteins with developmental functions. Such domains are thought to mediate interactions between proteins. Mouse enhancer RNA is shown to be at highest levels in collagen-rich tissues, especially tendon. The human enhancer gene, PCOLCE, is localized to 7q21.3-->q22, the same chromosomal region containing the type I collagen alpha 2 chain gene, COL1A2.
authors.affiliation: Department of Pathology and Laboratory Medicine, University of Wisconsin, Madison 53706.
authors.forename: K
authors.initials: K
authors.lastname: Takahara
authors.forename: E
authors.initials: E
authors.lastname: Kessler
authors.forename: L
authors.initials: L
authors.lastname: Biniaminov
authors.forename: M
authors.initials: M
authors.lastname: Brusel
authors.forename: R L
authors.initials: RL
authors.lastname: Eddy
authors.forename: S
authors.initials: S
authors.lastname: Jani-Sait
authors.forename: T B
authors.initials: TB
authors.lastname: Shows
authors.forename: D S
authors.initials: DS
authors.lastname: Greenspan
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D055395:Bone Morphogenetic Protein 1; D019485:Bone Morphogenetic Proteins; D002874:Chromosome Mapping; D018076:DNA, Complementary / Q000302:isolation & purification; D010450:Endopeptidases / Q000235:genetics*; D004742:Enhancer Elements, Genetic; D006801:Humans; D008666:Metalloendopeptidases; D051379:Mice; D008969:Molecular Sequence Data; D012313:RNA / Q000032:analysis; D017386:Sequence Homology, Amino Acid
chemical_list: D019485:Bone Morphogenetic Proteins; D018076:DNA, Complementary; D012313:RNA; D010450:Endopeptidases; D008666:Metalloendopeptidases; C525705:BMP1 protein, human; C525707:Bmp1 protein, mouse; D055395:Bone Morphogenetic Protein 1