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PCOLCE

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{{Short description|Protein-coding gene in humans}}

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Procollagen C-endopeptidase enhancer 1 is an enzyme that in humans is encoded by the PCOLCE gene.{{cite journal | vauthors = Takahara K, Osborne L, Elliott RW, Tsui LC, Scherer SW, Greenspan DS | title = Fine mapping of the human and mouse genes for the type I procollagen COOH-terminal proteinase enhancer protein | journal = Genomics | volume = 31 | issue = 2 | pages = 253–256 |date=Mar 1997 | pmid = 8824813 | doi = 10.1006/geno.1996.0043 }}{{cite journal | vauthors = Glockner G, Scherer S, Schattevoy R, Boright A, Weber J, Tsui LC, Rosenthal A | title = Large-scale sequencing of two regions in human chromosome 7q22: analysis of 650 kb of genomic sequence around the EPO and CUTL1 loci reveals 17 genes | journal = Genome Res | volume = 8 | issue = 10 | pages = 1060–1073 |date=Dec 1998 | pmid = 9799793 | pmc = 310788 | doi = 10.1101/gr.8.10.1060}}{{cite web | title = Entrez Gene: PCOLCE procollagen C-endopeptidase enhancer| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5118}}

Fibrillar collagen types I-III are synthesized as precursor molecules known as procollagens. These precursors contain amino- and carboxyl-terminal peptide extensions known as N- and C-propeptides, respectively, which are cleaved, upon secretion of procollagen from the cell, to yield the mature triple helical, highly structured fibrils. This gene encodes a glycoprotein which binds and drives the enzymatic cleavage of type I procollagen and heightens activity.

References

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Further reading

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  • {{cite journal |vauthors=Takahara K, Kessler E, Biniaminov L, etal |title=Type I procollagen COOH-terminal proteinase enhancer protein: identification, primary structure, and chromosomal localization of the cognate human gene (PCOLCE) |journal=J. Biol. Chem. |volume=269 |issue= 42 |pages= 26280–26285 |year= 1994 |doi=10.1016/S0021-9258(18)47191-8 |pmid= 7523404 |doi-access=free }}
  • {{cite journal |vauthors=Scott IC, Clark TG, Takahara K, etal |title=Structural organization and expression patterns of the human and mouse genes for the type I procollagen COOH-terminal proteinase enhancer protein |journal=Genomics |volume=55 |issue= 2 |pages= 229–234 |year= 1999 |pmid= 9933570 |doi= 10.1006/geno.1998.5663 }}
  • {{cite journal |vauthors=Mott JD, Thomas CL, Rosenbach MT, etal |title=Post-translational proteolytic processing of procollagen C-terminal proteinase enhancer releases a metalloproteinase inhibitor |journal=J. Biol. Chem. |volume=275 |issue= 2 |pages= 1384–1390 |year= 2000 |pmid= 10625689 |doi=10.1074/jbc.275.2.1384 |doi-access=free }}
  • {{cite journal |vauthors=Ricard-Blum S, Bernocco S, Font B, etal |title=Interaction properties of the procollagen C-proteinase enhancer protein shed light on the mechanism of stimulation of BMP-1 |journal=J. Biol. Chem. |volume=277 |issue= 37 |pages= 33864–33869 |year= 2002 |pmid= 12105202 |doi= 10.1074/jbc.M205018200 |doi-access= free }}
  • {{cite journal |vauthors=Ligon AH, Scott IC, Takahara K, etal |title=PCOLCE deletion and expression analyses in uterine leiomyomata |journal=Cancer Genet. Cytogenet. |volume=137 |issue= 2 |pages= 133–137 |year= 2002 |pmid= 12393284 |doi=10.1016/S0165-4608(02)00547-2 }}
  • {{cite journal | vauthors=Steiglitz BM, Keene DR, Greenspan DS |title=PCOLCE2 encodes a functional procollagen C-proteinase enhancer (PCPE2) that is a collagen-binding protein differing in distribution of expression and post-translational modification from the previously described PCPE1 |journal=J. Biol. Chem. |volume=277 |issue= 51 |pages= 49820–49830 |year= 2003 |pmid= 12393877 |doi= 10.1074/jbc.M209891200 |doi-access= free }}
  • {{cite journal |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–16903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 |bibcode=2002PNAS...9916899M |doi-access=free }}
  • {{cite journal |vauthors=Bernocco S, Steiglitz BM, Svergun DI, etal |title=Low resolution structure determination shows procollagen C-proteinase enhancer to be an elongated multidomain glycoprotein |journal=J. Biol. Chem. |volume=278 |issue= 9 |pages= 7199–7205 |year= 2003 |pmid= 12486138 |doi= 10.1074/jbc.M210857200 |doi-access= free }}
  • {{cite journal |vauthors=Liepinsh E, Banyai L, Pintacuda G, etal |title=NMR structure of the netrin-like domain (NTR) of human type I procollagen C-proteinase enhancer defines structural consensus of NTR domains and assesses potential proteinase inhibitory activity and ligand binding |journal=J. Biol. Chem. |volume=278 |issue= 28 |pages= 25982–25989 |year= 2003 |pmid= 12670942 |doi= 10.1074/jbc.M302734200 |doi-access= free }}
  • {{cite journal |vauthors=Gerhard DS, Wagner L, Feingold EA, etal |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC) |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–2127 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504 | pmc=528928 }}
  • {{cite journal | vauthors=Petropoulou V, Garrigue-Antar L, Kadler KE |title=Identification of the minimal domain structure of bone morphogenetic protein-1 (BMP-1) for chordinase activity: chordinase activity is not enhanced by procollagen C-proteinase enhancer-1 (PCPE-1) |journal=J. Biol. Chem. |volume=280 |issue= 24 |pages= 22616–22623 |year= 2005 |pmid= 15817489 |doi= 10.1074/jbc.M413468200 |doi-access= free }}
  • {{cite journal | vauthors=Ge G, Zhang Y, Steiglitz BM, Greenspan DS |title=Mammalian tolloid-like 1 binds procollagen C-proteinase enhancer protein 1 and differs from bone morphogenetic protein 1 in the functional roles of homologous protein domains |journal=J. Biol. Chem. |volume=281 |issue= 16 |pages= 10786–10798 |year= 2006 |pmid= 16507574 |doi= 10.1074/jbc.M511111200 |doi-access= free }}
  • {{cite journal |vauthors=Blanc G, Font B, Eichenberger D, etal |title=Insights into how CUB domains can exert specific functions while sharing a common fold: conserved and specific features of the CUB1 domain contribute to the molecular basis of procollagen C-proteinase enhancer-1 activity |journal=J. Biol. Chem. |volume=282 |issue= 23 |pages= 16924–16933 |year= 2007 |pmid= 17446170 |doi= 10.1074/jbc.M701610200 |doi-access= free|url=https://www.jbc.org/action/showPdf?pii=S0021-9258%2819%2957638-4|archive-url=https://web.archive.org/web/20180723232756/http://www.jbc.org/content/282/23/16924.full.pdf|archive-date=2018-07-23|url-access=subscription }}

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