A novel kinin, Met-Ile-Ser-bradykinin (Met-T-kinin) is released from T-kininogen by an acid proteinase of granulomatous tissues in rats.
Acid proteinase of granulomatous tissues in rats with carrageenin-induced inflammation released two types of kinin from T-kininogen. The kinin was identified as Ile-Ser-bradykinin (T-kinin) and a novel kinin, Met-Ile-Ser-bradykinin (Met-T-kinin), from determination of its amino acid composition and its immunoreactivity toward anti-bradykinin antiserum. The release of T-kinin and Met-T-kinin from T-kininogen were found to occur by consecutive cleavage by cathepsin D and 72 kDa protease.
Sakamoto
W
W
Department of Biochemistry, School of Dentistry, Hokkaido University, Sapporo, Japan.
Satoh
F
F
Nagasawa
S
S
Handa
H
H
Suzuki
S
S
Uehara
S
S
Hirayama
A
A
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D016282:Aspartic Acid Endopeptidases; D001920:Bradykinin / Q000031:analogs & derivatives* / Q000302:isolation & purification; D002402:Cathepsin D / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D010450:Endopeptidases / Q000378:metabolism*; D006099:Granuloma / Q000201:enzymology*; D007704:Kininogens / Q000378:metabolism*; D008297:Male; D051381:Rats; D011919:Rats, Inbred Strains
D000596:Amino Acids; D007704:Kininogens; C053343:bradykinin, Met-Ile-Ser-; D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases; D002402:Cathepsin D; D001920:Bradykinin