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Rat dipeptidyl peptidase IV (DPP IV) exhibits endopeptidase activity with specificity for denatured fibrillar collagens
Author(s) -
Bermpohl Felix,
Löster Klemens,
Reutter Werner,
Baum Oliver
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00515-8
Subject(s) - exopeptidase , dipeptidyl peptidase , endopeptidase , biochemistry , chemistry , proteases , serine protease , prolyl endopeptidase , protease , cathepsin c , serine , enzyme , gelatinase , protease inhibitor (pharmacology) , biology , human immunodeficiency virus (hiv) , antiretroviral therapy , viral load , immunology
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 (FAPα) represent a new subfamily of gelatinolytic integral membrane serine proteases.