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J. Biol. Chem., Vol. 277, Issue 51, 49820-49830, December 20, 2002
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From the The procollagen COOH-terminal proteinase enhancer
(PCPE) is a glycoprotein that binds the COOH-terminal propeptide of
type I procollagen and potentiates its cleavage by procollagen
C-proteinases, such as bone morphogenetic protein-1 (BMP-1). Recently,
sequencing of a human expressed sequence tag, which maps near the
primary open angle glaucoma region on chromosome 3q21, showed it to
encode a novel protein with only 43% identity with PCPE but with a
similar domain structure. Here we show this novel protein to be a
functional procollagen COOH-terminal proteinase enhancer with activity
comparable with that of PCPE and thus propose the designations PCPE2
and PCPE1, respectively. PCPE2 is shown to have a much more limited distribution of expression than does PCPE1, with strong expression primarily in nonossified cartilage in developing tissues and at high
levels in the adult heart. PCPE2 is shown to be a glycoprotein that
differs markedly in the nature of its glycosylation from that of PCPE1.
PCPE2 is also shown to have markedly stronger affinity for heparin than
PCPE1, which may account for higher affinities for cell layers.
Unexpectedly, both PCPE1 and PCPE2 were found to be collagen-binding
proteins, capable of binding at multiple sites on the triple helical
portions of fibrillar collagens and also capable of competing for such
binding with procollagen C-proteinases. The latter observations may
provide insights into the ways PCPEs affect the kinetics of the
C-proteinase reaction and into the physical interactions that occur
between procollagen C-proteinases and their substrates.
The nucleotide sequence(s) reported in this paper has been
submitted to GenBankTM/EBI Data Bank with accession
number(s) AF352788.
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*
§,
**
Departments of Biomolecular Chemistry and
Pathology and Laboratory Medicine, University of Wisconsin
Medical School, Madison, Wisconsin 53706 and ¶ Shriners Hospital
for Children, Portland, Oregon 97201
*
This work was supported by National Institutes of Health
Grants AR47746 and GM63471 (to D. S. G.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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