Inactivation of human plasma C1-inhibitor by human PMN leucocyte matrix metalloproteinases.
Highly purified human polymorphonuclear (PMN) leucocyte matrix metalloproteinases, collagenase and gelatinase, cleaved human plasma C1-inhibitor at the carboxyl site of Ala439 (P6). This led to a concomitant loss of C1-inhibitor activity. An additional cleavage site, at the carboxyl site of Ser441 (P4), was observed during PMN leucocyte gelatinase-induced inactivation, and a minor fragment of the plasma C1-inhibitor was generated.
Knäuper
V
V
University of Bielefeld, Faculty of Chemistry, Department of Biochemistry, Germany.
Triebel
S
S
Reinke
H
H
Tschesche
H
H
D000595:Amino Acid Sequence; D003174:Complement C1 Inactivator Proteins / Q000737:chemistry / Q000378:metabolism*; D018093:Gelatinases; D006801:Humans; D066298:In Vitro Techniques; D020781:Matrix Metalloproteinase 1; D008666:Metalloendopeptidases / Q000378:metabolism*; D003012:Microbial Collagenase / Q000378:metabolism*; D008969:Molecular Sequence Data; D009504:Neutrophils / Q000201:enzymology*; D010434:Pepsin A; D010449:Peptide Mapping
D003174:Complement C1 Inactivator Proteins; D010434:Pepsin A; D018093:Gelatinases; D008666:Metalloendopeptidases; D003012:Microbial Collagenase; D020781:Matrix Metalloproteinase 1