Degradation of type I and II collagen by human activated C1-s.
The activated first component of human complement, C1-s, was shown to cleave type I and II collagen and gelatin. The proteolytic activity was heat labile and was inhibited by a monoclonal antibody (M241) which recognized light chain of active human C1-s or by a serine protease inhibitor, DFP, but not by a chelating agent.
Yamaguchi
K
K
Division of Physiology and Pathology, National Institute of Radiological Sciences, Chiba, Japan.
Sakiyama
H
H
Matsumoto
M
M
Moriya
H
H
Sakiyama
S
S
D000595:Amino Acid Sequence; D002118:Calcium; D003094:Collagen / Q000378:metabolism*; D003173:Complement C1s / Q000378:metabolism*; D004789:Enzyme Activation; D005109:Extracellular Matrix / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D011480:Protease Inhibitors / Q000494:pharmacology; D012697:Serine Endopeptidases / Q000235:genetics / Q000378:metabolism
D011480:Protease Inhibitors; D003094:Collagen; D012697:Serine Endopeptidases; D003173:Complement C1s; D002118:Calcium