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Title: The extracellular glycoprotein SPARC interacts with platelet-derived growth factor (PDGF)-AB and -BB and inhibits the binding of PDGF to its receptors

Abstract

Interactions among growth factors, cells, and extracellular matrix are critical to the regulation of directed cell migration and proliferation associated with development wound healing, and pathologic processes. Here the authors report the association of PDGF-AB and -BB, but not PDGF-AA, with the extracellular glycoprotein SPARC. Complexes of SPARC and {sup 125}I-labeled PDGF-BB or -AB were specifically immunoprecipitated by anti-SPARC immunoglobulins. {sup 125}I-PDGF-BB and -AB also bound specifically to SPARC that was immobilized on microtiter wells or bound to nitrocellulose after transfer from SDS/polyacrylamide gels. The binding of PDGF-BB to SPARC was pH-dependent; significant binding was detectable only above pH 6.6. Enhanced expression of both PDGF-B chain and SPARC was seen in advanced lesions of atherosclerosis. They suggest that the coordinate expression of SPARC and PDGF-B-containing dimers following vascular injury may regulate the activity of specific dimeric forms of PDGF in vivo.

Authors:
; ; ; ;  [1]
  1. Univ. of Washington, Seattle (United States)
Publication Date:
OSTI Identifier:
5617894
Resource Type:
Journal Article
Journal Name:
Proceedings of the National Academy of Sciences of the United States of America; (United States)
Additional Journal Information:
Journal Volume: 89:4; Journal ID: ISSN 0027-8424
Country of Publication:
United States
Language:
English
Subject:
59 BASIC BIOLOGICAL SCIENCES; BLOOD PLATELETS; CYTOCHEMISTRY; GROWTH FACTORS; RADIORECEPTOR ASSAY; GLYCOPROTEINS; IODINE 125; RECEPTORS; BETA DECAY RADIOISOTOPES; BIOCHEMISTRY; BIOLOGICAL MATERIALS; BLOOD; BLOOD CELLS; BODY FLUIDS; CHEMISTRY; DAYS LIVING RADIOISOTOPES; ELECTRON CAPTURE RADIOISOTOPES; INTERMEDIATE MASS NUCLEI; INTERNAL CONVERSION RADIOISOTOPES; IODINE ISOTOPES; ISOTOPE APPLICATIONS; ISOTOPES; MATERIALS; MEMBRANE PROTEINS; MITOGENS; NUCLEI; ODD-EVEN NUCLEI; ORGANIC COMPOUNDS; PROTEINS; RADIOISOTOPES; TRACER TECHNIQUES; 550201* - Biochemistry- Tracer Techniques

Citation Formats

Raines, E W, Lane, T F, Iruela-Arispe, M L, Ross, R, and Sage, E H. The extracellular glycoprotein SPARC interacts with platelet-derived growth factor (PDGF)-AB and -BB and inhibits the binding of PDGF to its receptors. United States: N. p., 1992. Web. doi:10.1073/pnas.89.4.1281.
Raines, E W, Lane, T F, Iruela-Arispe, M L, Ross, R, & Sage, E H. The extracellular glycoprotein SPARC interacts with platelet-derived growth factor (PDGF)-AB and -BB and inhibits the binding of PDGF to its receptors. United States. https://doi.org/10.1073/pnas.89.4.1281
Raines, E W, Lane, T F, Iruela-Arispe, M L, Ross, R, and Sage, E H. 1992. "The extracellular glycoprotein SPARC interacts with platelet-derived growth factor (PDGF)-AB and -BB and inhibits the binding of PDGF to its receptors". United States. https://doi.org/10.1073/pnas.89.4.1281.
@article{osti_5617894,
title = {The extracellular glycoprotein SPARC interacts with platelet-derived growth factor (PDGF)-AB and -BB and inhibits the binding of PDGF to its receptors},
author = {Raines, E W and Lane, T F and Iruela-Arispe, M L and Ross, R and Sage, E H},
abstractNote = {Interactions among growth factors, cells, and extracellular matrix are critical to the regulation of directed cell migration and proliferation associated with development wound healing, and pathologic processes. Here the authors report the association of PDGF-AB and -BB, but not PDGF-AA, with the extracellular glycoprotein SPARC. Complexes of SPARC and {sup 125}I-labeled PDGF-BB or -AB were specifically immunoprecipitated by anti-SPARC immunoglobulins. {sup 125}I-PDGF-BB and -AB also bound specifically to SPARC that was immobilized on microtiter wells or bound to nitrocellulose after transfer from SDS/polyacrylamide gels. The binding of PDGF-BB to SPARC was pH-dependent; significant binding was detectable only above pH 6.6. Enhanced expression of both PDGF-B chain and SPARC was seen in advanced lesions of atherosclerosis. They suggest that the coordinate expression of SPARC and PDGF-B-containing dimers following vascular injury may regulate the activity of specific dimeric forms of PDGF in vivo.},
doi = {10.1073/pnas.89.4.1281},
url = {https://www.osti.gov/biblio/5617894}, journal = {Proceedings of the National Academy of Sciences of the United States of America; (United States)},
issn = {0027-8424},
number = ,
volume = 89:4,
place = {United States},
year = {Sat Feb 15 00:00:00 EST 1992},
month = {Sat Feb 15 00:00:00 EST 1992}
}