Chymase bound to heparin is resistant to its natural inhibitors and capable of proteolyzing high density lipoproteins in aortic intimal fluid

Atherosclerosis

Volumn 155, Issue 1, 2001, Pages 87-97

  Lindstedt, Leena ^a   Lee, Miriam ^a   Kovanen, Petri T ^a  

^a WIHURI RESEARCH INSTITUTE   (Finland)

Author keywords

Chymase; Enzyme immobilization; Heparin proteoglycans; High density lipoprotein; Mast cell

Indexed keywords

ALPHA 1 ANTITRYPSIN; ALPHA 2 MACROGLOBULIN; CHYMASE; CHYMOTRYPSIN INHIBITOR; EGLIN C; HEPARIN DERIVATIVE; HIGH DENSITY LIPOPROTEIN; LOW DENSITY LIPOPROTEIN; PROTEINASE INHIBITOR; PROTEOGLYCAN;

ANIMAL CELL; ANIMAL EXPERIMENT; ARTERY INTIMA; ARTICLE; CONTROLLED STUDY; ENZYME BINDING; ENZYME IMMOBILIZATION; HUMAN; HUMAN CELL; INTERSTITIAL FLUID; MALE; MAST CELL DEGRANULATION; NONHUMAN; NORMAL HUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN DEGRADATION; PROTEINASE INHIBITION; RAT;

ALPHA 1-ANTITRYPSIN; ALPHA-MACROGLOBULINS; ANIMALS; AORTA; CELL DEGRANULATION; CHYMASES; CHYMOTRYPSIN; EXTRACELLULAR SPACE; HEPARIN; HUMANS; LIPOPROTEINS, HDL; LIPOPROTEINS, HDL3; MALE; MAST CELLS; PROTEINS; PROTEOGLYCANS; RATS; RATS, WISTAR; SECRETORY VESICLES; SERINE ENDOPEPTIDASES; SERINE PROTEINASE INHIBITORS; SERPINS; TUNICA INTIMA;

EID: 0035118748     PISSN: 00219150     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0021-9150(00)00544-X     Document Type: Article

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