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J. Biol. Chem., Vol. 277, Issue 22, 19461-19469, May 31, 2002
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From the Center for Research in Skeletal Development and Pediatric
Orthopedics, Shriners Hospitals for Children, Tampa, Florida 33612 and
the Heparan sulfate proteoglycans are thought to
mediate the action of growth factors. The heparan sulfate-containing
proteoglycans in extracts of the bovine fetal rib growth plate were
detected using the monoclonal antibody 3G10, which recognizes a
neoepitope generated by heparitinase digestion (David, G., Bai, X. M., Van der Schueren, B., Cassiman, J. J., and Van den Berghe, H. (1992) J. Cell Biol. 119, 961-975). The heparan
sulfate proteoglycans that react with this antibody were identified
using antisera to known proteoglycans; purified using CsCl density
gradient centrifugation, molecular sieve, and ion exchange
chromatography; and then characterized. The major heparan sulfate
proteoglycans in the growth plate had core proteins of 200 kDa and
larger and were identified as perlecan and aggrecan. These two heparan
sulfate proteoglycans could be effectively separated from each other by
CsCl density gradient centrifugation alone. Perlecan contained 25%
heparan sulfate and 75% chondroitin sulfate. The heparan sulfate
chains on growth plate perlecan were considerably smaller than the
chondroitin sulfate chains, and the heparan sulfate disaccharide
content was different than that found for heparan sulfate from either
kidney, tumor tissue, or growth plate aggrecan. Aggrecan contained only 0.1% heparan sulfate, which was localized to the CS-1 domain of aggrecan. These results indicate that perlecan and aggrecan would be
the principal candidate proteoglycans involved in the action of heparan
sulfate-binding proteins in the developing growth plate.
Isolation and Identification of the Major Heparan Sulfate
Proteoglycans in the Developing Bovine Rib Growth Plate*
,, and§
Department of Biochemistry and Molecular Biology,
College of Medicine, University of South Florida,
Tampa, Florida 33612
*
This work was supported by funding from Shriners Hospitals
for Children, North America.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.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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