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J. Biol. Chem., Vol. 269, Issue 42, 26280-26285, Oct, 1994
K Takahara, E Kessler, L Biniaminov, M Brusel, RL Eddy, S Jani-Sait, TB Shows and DS Greenspan
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.
Type I procollagen COOH-terminal proteinase enhancer protein: identification, primary structure, and chromosomal localization of the cognate human gene (PCOLCE)
Department of Pathology and Laboratory Medicine, University of Wisconsin, Madison 53706.
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