Degradation of the 74 kDa form of l‐histidine decarboxylase via the ubiquitin‐proteasome pathway in a rat basophilic/mast cell line (RBL‐2H3)

FEBS Letters

Ichikawa, Atsushi¹  Ohmura, Satoshi²  Nemoto, Ken-ichi¹  Tanaka, Satoshi¹  Yamamura, Eriko¹ 

[1]Department of Physiological Chemistry, Faculty of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto 606, Japan

[2]Research Center for Biological Function, The Kitasato Institute, Minato-ku, Tokyo 108, Japan

关键词: Histidine decarboxylase;    Ubiquitin-proteasome pathway;    HDC;    l-histidine decarboxylase;    ODC;    ornithine decarboxylase;    DDC;    aromatic l-amino acid decarboxylase;    SDS-PAGE;    sodium dodecyl sulfate-polyacrylamide gel electrophoresis;    cDNA;    complementary DNA;    ATP;    adenosine triphosphate;    ATPγS;    adenosine 5′-O-(3-thiotriphosphate);    PMSF;    phenylmethylsulfonyl fluoride;    ER;    endoplasmic reticulum;    GST;    glutathione S-transferase;    ALLN;    n-acetyl leucyl leucyl norleucinal;    ALLM;    n-acetyl leucyl leucyl methional;    ZL3H;    carboxybenzyl leucyl leucyl leucinal;    ZL2H;    carboxybenzyl leucyl leucinal;   

DOI  :  10.1016/S0014-5793(97)01281-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

l-Histidine decarboxylase (HDC) is a dimer consisting of two identical 53 kDa subunits. On the other hand, the size of HDC deduced from its cDNA sequence is around 74 kDa, indicating that the translated 74 kDa form of HDC is subjected to post-translational processing to generate the 53 kDa form. However, modification of the translated 74 kDa form of HDC in histamine-forming cells is unknown. Here we demonstrate that the 74 kDa form is translated in rat basophilic leukemia cells, followed by conversion to the 53 kDa form, and that the 74 kDa form is a short half-life protein because of the degradation mediated by the ubiquitin-proteasome pathway. Degradation of the 74 kDa form was stimulated in the presence of an ATP-generating system, accompanied by ubiquitination, and inhibited by specific proteasome inhibitors such as ZL₃H and lactacystin. A significant amount of proteasome activity was detected in RBL-2H3 cells.

【 授权许可】

Unknown