PCPE-1 (procollagen C-proteinase enhancer-1) is an extracellular matrix glycoprotein that can stimulate procollagen processing by procollagen C-proteinases such as BMP-1 (bone morphogenetic protein 1). PCPE-1 interacts with several proteins in addition to procollagens and BMP-1, suggesting that it could be involved in biological processes other than collagen maturation. We thus searched for additional partners of PCPE-1 in the extracellular matrix, which could provide new insights into its biological roles. We identified 17 new partners of PCPE-1 by SPR (surface plasmon resonance) imaging. PCPE-1 forms a transient complex with the β-amyloid peptide, whereas it forms high or very high affinity complexes with laminin-111 (KD=58.8 pM), collagen VI (KD=9.5 nM), TSP-1 (thrombospondin-1) (KD1=19.9 pM, KD2=14.5 nM), collagen IV (KD=49.4 nM) and endostatin, a fragment of collagen XVIII (KD1=0.30 nM, KD2=1.1 nM). Endostatin binds to the NTR (netrin-like) domain of PCPE-1 and decreases the degree of superstimulation of PCPE-1 enhancing activity by heparin. The analysis of the PCPE-1 interaction network based on Gene Ontology terms suggests that, besides its role in collagen deposition, PCPE-1 might be involved in tumour growth, neurodegenerative diseases and angiogenesis. In vitro assays have indeed shown that the CUB1CUB2 (where CUB is complement protein subcomponents C1r/C1s, urchin embryonic growth factor and BMP-1) fragment of PCPE-1 inhibits angiogenesis.
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Research Article|
December 10 2013
Extended interaction network of procollagen C-proteinase enhancer-1 in the extracellular matrix
Romain Salza;
Romain Salza
*UMR 5086 CNRS-Université Lyon 1, FR 3302 Institut de Biologie et Chimie des Protéines, 7 passage du Vercors, 69367 Lyon, Cedex 07, France
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Franck Peysselon;
Franck Peysselon
*UMR 5086 CNRS-Université Lyon 1, FR 3302 Institut de Biologie et Chimie des Protéines, 7 passage du Vercors, 69367 Lyon, Cedex 07, France
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Emilie Chautard;
Emilie Chautard
*UMR 5086 CNRS-Université Lyon 1, FR 3302 Institut de Biologie et Chimie des Protéines, 7 passage du Vercors, 69367 Lyon, Cedex 07, France
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Clément Faye;
Clément Faye
*UMR 5086 CNRS-Université Lyon 1, FR 3302 Institut de Biologie et Chimie des Protéines, 7 passage du Vercors, 69367 Lyon, Cedex 07, France
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Laura Moschcovich;
Laura Moschcovich
†Maurice and Gabriela Goldschleger Eye Research Institute, Tel-Aviv University, Sackler Faculty of Medicine, Sheba Medical Center, Tel-Hashomer 52621, Israel
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Tali Weiss;
Tali Weiss
†Maurice and Gabriela Goldschleger Eye Research Institute, Tel-Aviv University, Sackler Faculty of Medicine, Sheba Medical Center, Tel-Hashomer 52621, Israel
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Laure Perrin-Cocon;
Laure Perrin-Cocon
‡Inserm U1111-UMR5308 CNRS, Lyon, France
§Université Lyon 1-ENS de Lyon, CIRI International Center for Infectiology Research, 69365 Lyon, France
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Vincent Lotteau;
Vincent Lotteau
‡Inserm U1111-UMR5308 CNRS, Lyon, France
§Université Lyon 1-ENS de Lyon, CIRI International Center for Infectiology Research, 69365 Lyon, France
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Efrat Kessler;
Efrat Kessler
†Maurice and Gabriela Goldschleger Eye Research Institute, Tel-Aviv University, Sackler Faculty of Medicine, Sheba Medical Center, Tel-Hashomer 52621, Israel
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Sylvie Ricard-Blum
Sylvie Ricard-Blum
1
*UMR 5086 CNRS-Université Lyon 1, FR 3302 Institut de Biologie et Chimie des Protéines, 7 passage du Vercors, 69367 Lyon, Cedex 07, France
1To whom correspondence should be addressed (email s.ricard-blum@ibcp.fr).
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Publisher: Portland Press Ltd
Received:
February 26 2013
Revision Received:
October 03 2013
Accepted:
October 14 2013
Accepted Manuscript online:
October 14 2013
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2014 Biochemical Society
2014
Biochem J (2014) 457 (1): 137–149.
Article history
Received:
February 26 2013
Revision Received:
October 03 2013
Accepted:
October 14 2013
Accepted Manuscript online:
October 14 2013
Citation
Romain Salza, Franck Peysselon, Emilie Chautard, Clément Faye, Laura Moschcovich, Tali Weiss, Laure Perrin-Cocon, Vincent Lotteau, Efrat Kessler, Sylvie Ricard-Blum; Extended interaction network of procollagen C-proteinase enhancer-1 in the extracellular matrix. Biochem J 1 January 2014; 457 (1): 137–149. doi: https://doi.org/10.1042/BJ20130295
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