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J. Biol. Chem., Vol. 275, Issue 33, 25742-25750, August 18, 2000
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From the Cell surface heparan sulfate proteoglycans
(HSPGs) participate in the catabolism of many physiologically important
ligands. We previously reported that syndecan HSPGs directly mediate
endocytosis, independent of coated pits. We now studied perlecan, a
major cell surface HSPG genetically distinct from syndecans. Cells
expressing perlecan but no other proteoglycans bound, internalized, and
degraded atherogenic lipoproteins enriched in lipoprotein lipase.
Binding was blocked by heparitinase, and degradation by chloroquine.
Antibodies against
Perlecan Heparan Sulfate Proteoglycan
A NOVEL RECEPTOR THAT MEDIATES A DISTINCT PATHWAY FOR LIGAND
CATABOLISM*
§,
Dorrance H. Hamilton Research Laboratories,
Division of Endocrinology, Diabetes and Metabolic Diseases, Department
of Medicine and the Department of Pathology, Anatomy and Cell
Biology and the Kimmel Cancer Center, Jefferson Medical College, Thomas
Jefferson University, Philadelphia, Pennsylvania 19107
1 integrins reduced
initial ligand binding, consistent with their roles as cell surface
attachment sites for perlecan. By several criteria, catabolism via
perlecan was distinct from either coated pits or the syndecan pathway.
The kinetics of internalization (t1/2 = 6 h) and degradation (t1/2 ~ 18 h) were
remarkably slow, unlike the other pathways. Blockade of the low density
lipoprotein receptor-related protein did not slow
perlecan-dependent internalization. Internalization via
perlecan was inhibited by genistein but unaffected by cytochalasin D, a pattern distinct from coated pits or syndecan-mediated endocytosis. Finally, we examined cooperation between perlecan and low density lipoprotein receptors and found limited synergy. Our results
demonstrate that perlecan mediates internalization and lysosomal
delivery that is kinetically and biochemically distinct from other
known uptake pathways and is consistent with a very slow component of HSPG-dependent ligand processing found in vitro
and in vivo.
*
This work was supported in part by National Institutes of
Health Grants HL38956, HL58884, HL56984, and CA47282. Portions of this
work were presented at the 69th Scientific Sessions of the American
Heart Association (1).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 © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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