Document Detail


Cell surface localization of heparanase on macrophages regulates degradation of extracellular matrix heparan sulfate.
MedLine Citation:
PMID:  15004189     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Extravasation of peripheral blood monocytes through vascular basement membranes requires degradation of extracellular matrix components including heparan sulfate proteoglycans (HSPGs). Heparanase, the heparan sulfate-specific endo-beta-glucuronidase, has previously been shown to be a key enzyme in melanoma invasion, yet its involvement in monocyte extravasation has not been elucidated. We examined a potential regulatory mechanism of heparanase in HSPG degradation and transmigration through basement membranes in leukocyte trafficking using human promonocytic leukemia U937 and THP-1 cells. PMA-treated cells were shown to degrade 35S-sulfated HSPG in endothelial extracellular matrix into fragments of an approximate molecular mass of 5 kDa. This was not found with untreated cells. The gene expression levels of heparanase or the enzyme activity of the amount of cell lysates were no different between untreated and treated cells. Immunocytochemical staining with anti-heparanase mAb revealed pericellular distribution of heparanase in PMA-treated cells but not in untreated cells. Cell surface heparanase capped into a restricted area on PMA-treated cells when they were allowed to adhere. Addition of a chemoattractant fMLP induced polarization of the PMA-treated cells and heparanase redistribution at the leading edge of migration. Therefore a major regulatory process of heparanase activity in the cells seems to be surface expression and capping of the enzyme. Addition of the anti-heparanase Ab significantly inhibited enzymatic activity and transmigration of the PMA-treated cells, suggesting that the cell surface redistribution of heparanase is involved in monocyte extravasation through basement membranes.
Authors:
Norihiko Sasaki; Nobuaki Higashi; Tomohiro Taka; Motowo Nakajima; Tatsuro Irimura
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of immunology (Baltimore, Md. : 1950)     Volume:  172     ISSN:  0022-1767     ISO Abbreviation:  J. Immunol.     Publication Date:  2004 Mar 
Date Detail:
Created Date:  2004-03-08     Completed Date:  2004-07-13     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  2985117R     Medline TA:  J Immunol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  3830-5     Citation Subset:  AIM; IM    
Affiliation:
Laboratory of Cancer Biology and Molecular Immunology, Graduate School of Pharmaceutical Sciences, University of Tokyo, Tokyo, Japan.
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MeSH Terms
Descriptor/Qualifier:
Animals
Cattle
Cell Adhesion / physiology
Cell Line, Tumor
Cell Membrane / enzymology,  immunology
Cell Movement / physiology
Cells, Cultured
Endothelial Cells / drug effects,  enzymology,  metabolism
Extracellular Matrix / drug effects,  metabolism*
Gene Expression Regulation / drug effects
Glucuronidase / biosynthesis,  genetics,  metabolism*,  physiology
Heparitin Sulfate / metabolism*
Humans
Macrophages / enzymology*,  metabolism
Membrane Proteins / biosynthesis,  genetics,  metabolism*
Monocytes / enzymology,  metabolism
Subcellular Fractions / drug effects,  enzymology
Tetradecanoylphorbol Acetate / pharmacology
U937 Cells
Chemical
Reg. No./Substance:
0/Membrane Proteins; 16561-29-8/Tetradecanoylphorbol Acetate; 9050-30-0/Heparitin Sulfate; EC 3.2.1.-/heparanase; EC 3.2.1.31/Glucuronidase

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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