Purification of a serine-proteinase inhibitor from human articular cartilage. Identity with the acid-stable proteinase inhibitor of mucous secretions.
An inhibitor of the serine proteinases human leucocyte elastase (EC 3.4.21.37), of cathepsin G (EC 3.4.21.20) and of trypsin (EC 3.4.21.4) has been purified from human articular cartilage. The apparent Mr of the cationic (pI greater than 10) protein was determined to 15,000 by SDS/PAGE. It was shown to cross-react in Western blot with a specific antibody to a recombinant-derived serine-proteinase inhibitor of human mucous secretions. Identity of both inhibitors is indicated by the determination of the N-terminal amino acid sequence of the cartilage-derived serine-proteinase inhibitor. In all 24 residues the cartilage inhibitor was shown to be identical with the human secretory leucocyte proteinase inhibitor ('SLPI'). The inhibitor molecule may play a crucial role in the protection of cartilage matrix proteins against proteolytic attack.
Böhm
B
B
Max-Planck-Society, University Erlangen-Nürnberg, Federal Republic of Germany.
Deutzmann
R
R
Burkhardt
H
H
D000293:Adolescent; D000595:Amino Acid Sequence; D015153:Blotting, Western; D002358:Cartilage, Articular / Q000737:chemistry*; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D006801:Humans; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009093:Mucus / Q000187:drug effects / Q000378:metabolism*; D009842:Oligopeptides; D010196:Pancreatic Elastase / Q000037:antagonists & inhibitors; D010446:Peptide Fragments / Q000302:isolation & purification; D012689:Sequence Homology, Nucleic Acid; D015842:Serine Proteinase Inhibitors / Q000302:isolation & purification* / Q000494:pharmacology
D009842:Oligopeptides; D010446:Peptide Fragments; D015842:Serine Proteinase Inhibitors; D010196:Pancreatic Elastase