Dipeptidyl peptidase IV (CD 26) and aminopeptidase N (CD 13) catalyzed hydrolysis of cytokines and peptides with N‐terminal cytokine sequences

FEBS Letters

Hoffmann, T.¹  Faust, J.²  Ansorge, S.¹  Neubert, K.² 

[1] Department of Internal Medicine, Division of Experimental Immunology, Otto-von-Guericke-University Magdeburg, Leipziger Str. 44, 39120 Magdeburg, Germany;Department of Biochemistry/Biotechnology, Institute of Biochemistry, Martin-Luther-University Halle-Wittenberg, Weinbergweg 16a, 06120 Halle, Germany

关键词: Dipeptidyl peptidase IV;    Aminopeptidase N;    Cytokine;    Cytokine partial sequence;    AP-N;    aminopeptidase N;    DP IV;    dipeptidyl peptidase IV;    Fmoc;    fluorenylmethoxycarbonyl;    G-CSF;    granulocyte colony stimulating factor;    GM-CSF;    granulocyte-macrophage colony stimulating factor;    IL;    interleukin;    g;    glycosylated;    mIL;    murine interleukin;    MNC;    mononuclear cells;    nIL;    natural interleukin;    POE;    polyoxyethylene;    rIL;    recombinant interleukin;    TGF-β;    transforming growth factor;    TNF;    tumour necrosis factor;   

DOI  :  10.1016/0014-5793(93)81609-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A number of natural cytokines are characterized as having dipeptidyl peptidase (DP) IV susceptible N-terminal peptide sequences. Here we demonstrate that oligopeptides with sequences analogous to the N-terminal part of human IL-1β, IL-2, TNF-β and murine IL-6 were hydrolyzed by purified DP IV and aminopeptidase N (AP-N). The rate of DP IV-catalyzed hydrolysis of these peptides was negatively correlated with their chain length. In contrast to these results, no degradation was found under our conditions for the intact recombinant cytokines, IL-1α, IL-1β, IL-2, G-CSF and for natural IL-2, independent of whether DP IV and AP-N were used separately or in combination.

【 授权许可】

Unknown