Isolation of chymase complexed with physiological inhibitor similar to secretory leukocyte protease inhibitor (SLPI) from hamster cheek pouch tissues.
A low molecular weight protein complexed with chymase was isolated from hamster cheek pouch tissues. This protein had an apparent molecular mass of about 10 kDa on SDS-PAGE and the N-terminal sequence showed some homology to secretory leukocyte protease inhibitor (SLPI), which is known as the predominant inhibitor of neutrophil elastase and cathepsin G. Remarkably enhanced inhibition of chymase activity was achieved in the presence of heparin, indicating that the functional property was also similar to SLPI. These findings suggest that this SLPI-like protein is a candidate for a physiological inhibitor of chymase.
Takao
K
K
Department of Pharmacology, Osaka Medical College, Japan.
Takai
S
S
Ishihara
T
T
Mita
S
S
Miyazaki
M
M
D000595:Amino Acid Sequence; D000818:Animals; D002610:Cheek; D053818:Chymases; D006224:Cricetinae; D004591:Electrophoresis, Polyacrylamide Gel; D046911:Macromolecular Substances; D008297:Male; D008647:Mesocricetus; D008969:Molecular Sequence Data; D008970:Molecular Weight; D053491:Proteinase Inhibitory Proteins, Secretory; D011506:Proteins / Q000737:chemistry; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D015842:Serine Proteinase Inhibitors / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism
D046911:Macromolecular Substances; D053491:Proteinase Inhibitory Proteins, Secretory; D011506:Proteins; D015842:Serine Proteinase Inhibitors; D012697:Serine Endopeptidases; D053818:Chymases