Procollagen C-endopeptidase enhancer 1 is an enzyme that in humans is encoded by the PCOLCEgene.[1][2][3]
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 C-proteinase activity.[3]
References
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Takahara K, Kessler E, Biniaminov L, et al. (1994). "Type I procollagen COOH-terminal proteinase enhancer protein: identification, primary structure, and chromosomal localization of the cognate human gene (PCOLCE)". J. Biol. Chem. 269 (42): 26280–5. PMID7523404.
Scott IC, Clark TG, Takahara K, et al. (1999). "Structural organization and expression patterns of the human and mouse genes for the type I procollagen COOH-terminal proteinase enhancer protein". Genomics. 55 (2): 229–34. doi:10.1006/geno.1998.5663. PMID9933570.
Mott JD, Thomas CL, Rosenbach MT, et al. (2000). "Post-translational proteolytic processing of procollagen C-terminal proteinase enhancer releases a metalloproteinase inhibitor". J. Biol. Chem. 275 (2): 1384–90. doi:10.1074/jbc.275.2.1384. PMID10625689.
Ricard-Blum S, Bernocco S, Font B, et al. (2002). "Interaction properties of the procollagen C-proteinase enhancer protein shed light on the mechanism of stimulation of BMP-1". J. Biol. Chem. 277 (37): 33864–9. doi:10.1074/jbc.M205018200. PMID12105202.
Ligon AH, Scott IC, Takahara K, et al. (2002). "PCOLCE deletion and expression analyses in uterine leiomyomata". Cancer Genet. Cytogenet. 137 (2): 133–7. doi:10.1016/S0165-4608(02)00547-2. PMID12393284.
Steiglitz BM, Keene DR, Greenspan DS (2003). "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". J. Biol. Chem. 277 (51): 49820–30. doi:10.1074/jbc.M209891200. PMID12393877.
Bernocco S, Steiglitz BM, Svergun DI, et al. (2003). "Low resolution structure determination shows procollagen C-proteinase enhancer to be an elongated multidomain glycoprotein". J. Biol. Chem. 278 (9): 7199–205. doi:10.1074/jbc.M210857200. PMID12486138.
Liepinsh E, Banyai L, Pintacuda G, et al. (2003). "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". J. Biol. Chem. 278 (28): 25982–9. doi:10.1074/jbc.M302734200. PMID12670942.
Petropoulou V, Garrigue-Antar L, Kadler KE (2005). "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)". J. Biol. Chem. 280 (24): 22616–23. doi:10.1074/jbc.M413468200. PMID15817489.
Ge G, Zhang Y, Steiglitz BM, Greenspan DS (2006). "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". J. Biol. Chem. 281 (16): 10786–98. doi:10.1074/jbc.M511111200. PMID16507574.
Blanc G, Font B, Eichenberger D, et al. (2007). "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". J. Biol. Chem. 282 (23): 16924–33. doi:10.1074/jbc.M701610200. PMID17446170.