Rat dipeptidyl peptidase IV (DPP IV) exhibits endopeptidase activity with specificity for denatured fibrillar collagens

FEBS Letters

Bermpohl, Felix¹  Löster, Klemens¹  Baum, Oliver¹  Reutter, Werner¹ 

[1] Institut für Molekularbiologie und Biochemie, Freie Universität Berlin, Arnimallee 22, D-14195 Berlin-Dahlem, Germany

关键词: Dipeptidyl peptidase IV;    Endopeptidase;    Collagen degradation;    Gelatin zymography;    Gelatinolytic integral membrane serine protease;    DFP;    diisopropyl fluorophosphate;    DMSO;    dimethyl sulfoxide;    DPP IV;    dipeptidyl peptidase IV;    DTT;    dithiothreitol;    ECM;    extracellular matrix;    EDTA;    ethylenediaminetetraacetic acid;    FAPα;    fibroblast activation protein α;    kDa;    kilodalton;    mAb;    monoclonal antibody;    PMSF;    phenylmethylsulfonyl fluoride;    M r;    relative molecular mass;    NEM;    N-ethylmaleimide;    SDS-PAGE;    sodium dodecyl sulfate-polyacrylamide gel electrophoresis;    TBS;    Tris buffered saline;    TPCK;    tosyl-phenylalanine chloromethyl ketone;   

DOI  :  10.1016/S0014-5793(98)00515-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown