Rat dipeptidyl peptidase IV (DPP IV) exhibits endopeptidase activity with specificity for denatured fibrillar collagens.
Dipeptidyl peptidase IV (DPP IV, CD 26) is an integral membrane serine protease exhibiting a well characterized exopeptidase activity. The present study shows that DPP IV also possesses a novel gelatinase activity and therefore endopeptidase activity, which was directly demonstrated by gelatin zymography. Protease inhibitor profile analysis showed that the endo- and exopeptidase activities of DPP IV share a common active site. Substrate specificity was detected for denatured collagen types I, II, III and V suggesting that DPP IV might contribute to collagen trimming and metabolism. On the basis of these data we propose that DPP IV and the recently sequenced gelatinolytic seprase (FAPalpha) represent a new subfamily of gelatinolytic integral membrane serine proteases.
Bermpohl
F
F
Institut für Molekularbiologie und Biochemie, Freie Universität Berlin, Berlin-Dahlem, Germany.
Löster
K
K
Reutter
W
W
Baum
O
O
D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D003094:Collagen / Q000378:metabolism*; D018819:Dipeptidyl Peptidase 4 / Q000302:isolation & purification / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000378:metabolism; D007672:Kidney Cortex / Q000201:enzymology; D007700:Kinetics; D011480:Protease Inhibitors / Q000494:pharmacology*; D011489:Protein Denaturation; D051381:Rats; D013379:Substrate Specificity
D011480:Protease Inhibitors; D003094:Collagen; D010450:Endopeptidases; D018819:Dipeptidyl Peptidase 4