PMID: 7017731Apr 1, 1981Paper

Released protease-nexin regulates cellular binding, internalization, and degradation of serine proteases

Proceedings of the National Academy of Sciences of the United States of America
D A LowD D Cunningham

Abstract

Protease-nexin (PN), a component released by normal human fibroblasts into culture medium, forms covalent linkages with thrombin (Th) and the urinary plasminogen activator urokinase, apparently with their catalytic site serines. The present studies explored the function of PN by examining the interaction of protease-PN complexes with human fibroblasts and the consequences of this interaction. Th-PN and urokinase-PN complexes bind to cells via the PN portion of the complexes. The binding is selectively inhibited by heparin. Because PN has a heparin-binding site, this indicates that protease-PN complexes might bind to a cellular heparin-like site. After binding, the complexes are internalized. By inhibiting endocytosis with phenylarsine oxide, which does not affect cellular binding of Th-PN complexes, we showed that complexes must be internalized before they are degraded. Kinetic analysis of internalization and degradation of Th-PN showed that complexes are internalized more rapidly than they dissociate from the cell surface; by 120 min of incubation at 37 degrees C most cell-bound Th-PN complexes are degraded to amino acids. The results are summarized in a model showing how PN mediates the cellular binding, internalization, and ...Continue Reading

References

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Citations

May 6, 1999·Journal of Cellular Physiology·C MbebiM Verdière-Sahuqué
Jan 1, 1990·Journal of Cellular Physiology·D Gurwitz, D D Cunningham
Jan 1, 1985·Cancer Metastasis Reviews·I A Ramshaw, P Badenoch-Jones
Apr 1, 1984·Molecular and Cellular Biochemistry·M TrowbridgeJ Tepperman
Apr 1, 1989·Developmental Biology·S Pino-Heiss, G Schubiger
Jan 1, 1991·Pharmacology & Therapeutics·R Eisenstein
Oct 30, 1989·Biochimica Et Biophysica Acta·K KitagawaL I Tanner
Nov 21, 2000·Minerva medica·M CamiciR Di Mitri
May 7, 1992·The New England Journal of Medicine·A H Schmaier, W Van Nostrand
Apr 1, 1982·Proceedings of the National Academy of Sciences of the United States of America·D J Knauer, D D Cunningham
Apr 1, 1983·Proceedings of the National Academy of Sciences of the United States of America·J L GrossM D Lane
Sep 1, 1986·Proceedings of the National Academy of Sciences of the United States of America·D H Farrell, D D Cunningham
Nov 1, 1989·Proceedings of the National Academy of Sciences of the United States of America·S L WagnerD D Cunningham
Oct 25, 1994·Proceedings of the National Academy of Sciences of the United States of America·Y LiuP G Nelson
Apr 1, 1987·The Journal of Cell Biology·F BlasiK Danø
Jul 1, 1989·The Journal of Cell Biology·S Verrall, N W Seeds
Dec 1, 1982·The Journal of Cell Biology·D H Carney, J S Bergmann
Feb 1, 1987·The Journal of Experimental Medicine·A WohlwendJ D Vassalli
Dec 31, 1992·Annals of the New York Academy of Sciences·D D Cunningham
Feb 15, 2012·Molecular and Cellular Biology·Sonia SelbonneVéronique Arocas
Jan 1, 1994·Annals of the Rheumatic Diseases·R MorrisC J Morris
Dec 12, 1985·Biochimica Et Biophysica Acta·E Van Obberghen-Schilling, J Pouysségur
Mar 30, 1982·Biochemical and Biophysical Research Communications·D A Low, D D Cunningham
Jul 17, 2013·Journal of Thrombosis and Haemostasis : JTH·J A Huntington
May 30, 1989·Biochemical and Biophysical Research Communications·D GurwitzD D Cunningham
Mar 1, 1989·Experimental Cell Research·K Leroy-ViardM C Guillin
Mar 1, 1991·Experimental Cell Research·K KudahlO Sonne
Dec 17, 1985·Biochemical and Biophysical Research Communications·A Bajpai, J B Baker

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