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

Satoshi Tanaka, Ken Ichi Nemoto, Eriko Yamamura, Satoshi Ohmura, Atsushi Ichikawa

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

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 pest-translational processing to generate the 53 kDa form. However, modification of tile translated 74 kDa form of HDC in histamine-forming cells is unknown. Here we demonstrate that the 73 kBa 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.

Original languageEnglish
Pages (from-to)203-207
Number of pages5
JournalFEBS Letters
Volume417
Issue number2
DOIs
Publication statusPublished - Nov 10 1997

Keywords

  • Histidine decarboxylase
  • Ubiquitin-proteasome pathway

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Fingerprint Dive into the research topics of 'Degradation of the 74 kDa form of L-histidine decarboxylase via the ubiquitin-proteasome pathway in a rat basophilic/mast cell line (RBL-2H3)'. Together they form a unique fingerprint.

  • Cite this