3.4.24.19	Enhancer glycoprotein	bound to the carboxyl propeptide of type I procollagen	31034	
3.4.24.19	Enhancer glycoprotein	characterization	31043	
3.4.24.19	Enhancer glycoprotein	enhancer may play a regulatory role in procollagen processing	31043	
3.4.24.19	Enhancer glycoprotein	enhances activity of C-proteinase	31034, 31036	
3.4.24.19	Enhancer glycoprotein	stimulates activity	668838	
3.4.24.19	Frizzled-related protein	secreted Frizzled-related protein sFRP2 serves as a direct enhancer of procollagen C proteinase activity of tolloid-like metalloproteinases. The level of fibrosis, in which procollagen processing by tolloid-like proteinases has a rate-limiting role, is markedly reduced in Sfrp2-null mice subjected to myocardial infarction. This reduced level of fibrosis is accompanied by significantly improved cardiac function	700348	
3.4.24.19	heparin	stimulation of BMP-1 activity by procollagen C-proteinase enhancer-1 is further increased by the presence of 0.05 mg/ml heparin	712425	
3.4.24.19	heparin sulfate	in the presence of both procollagen C-proteinase enhancer-1 and heparin or heparan sulfate, the activity of BMP-1 is further stimulated	712425	
3.4.24.19	additional information	both PCPE1 and PCPE2 are located in the extracellular matrix, where they facilitate bone morphogenetic protein 1 (BMP1) cleavage of C-terminal procollagen propeptides. PCPE2 and PCPE1 have different tissue distributions and heparin-binding affinities, suggesting a functional divergence. PCPE2 is heavily expressed in heart tissue in contrast to PCPE1. Both PCPE1 and PCPE2 have two CUB (Complement C1r/C1s, Uegf, Bmp1) domains separated by a short linker region, with each domain consisting of about 110 residues containing a beta-sandwich fold that mediates a variety of protein-protein interactions. Phenotype of PCPE2-/- mice, overview	754110	
3.4.24.19	PCPE-1	enhances degredation of procollagen type I 5 fold, enhances C-terminal processing of procollagen type III when this substrate is in its native, disulfide-bonded conformation, has no effect on the in vitro BMP-1 processing of procollagen VII, procollagen V N-propeptide, laminin 5 gamma2 chain, osteoglycin, prolysyl oxidase or chordin	669352