Inactivation of substance P by granulation tissue-derived gelatinase.
An active gelatinase has been purified from the conditioned medium of granulation tissue culture formed by carrageenin injection in rats. The purified gelatinase gave a single band corresponding to a M(r) of 57 kDa on both sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and SDS-gelatin PAGE. The granulation tissue-derived gelatinase selectively cleaved the Gln6-Phe7 bond of substance P (SP) with a Km of 0.17 mM and a Vmax of 0.027 nmol SP7-11/min/micrograms protein, resulting in the generation of biologically inactive fragments, SP1-6 and SP7-11. Our data suggest that the gelatinase produced by granulation tissue participates in the inactivation of SP in the inflammatory site.
D000818:Animals; D002216:Captopril / Q000494:pharmacology; D046508:Culture Techniques; D004591:Electrophoresis, Polyacrylamide Gel; D005780:Gelatin / Q000378:metabolism; D006097:Granulation Tissue / Q000201:enzymology*; D006868:Hydrolysis; D007700:Kinetics; D008297:Male; D010446:Peptide Fragments / Q000378:metabolism; D011480:Protease Inhibitors / Q000378:metabolism*; D051381:Rats; D017208:Rats, Wistar; D013373:Substance P / Q000031:analogs & derivatives / Q000037:antagonists & inhibitors* / Q000302:isolation & purification / Q000378:metabolism; D015244:Thiorphan / Q000494:pharmacology
D010446:Peptide Fragments; D011480:Protease Inhibitors; D013373:Substance P; C061335:substance P (7-11); C078436:Substance P (1-6); D005780:Gelatin; D002216:Captopril; D015244:Thiorphan