Membrane orientation of the precursor 74-kDa form of L-histidine decarboxylase

K. Furuta, A. Ichikawa, K. Nakayama, Satoshi Tanaka

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)


Objective: We previously demonstrated that, when expressed in COS-7 cells, L-histidine decarboxylase (HDC), which has neither an amino terminal signal sequence nor a hydrophobic membrane anchor, was localized in the endoplasmic reticulum (ER), although its orientation in the membrane remains to be clarified. Methods & Results: Protease digestion and immunofluorescence analyses of the cells, of which plasma membrane was selectively permeabilized, revealed that the amino terminal 50-kDa portion of HDC is hardly accessible to proteases and antibodies added exogenously from the cytosolic side. Green fluorescent protein fused with the carboxyl terminal 20-kDa region of HDC at its carboxyl terminus exhibited the same characteristics as native HDC. Conclusion: These results indicate that HDC is tightly associated with the ER membrane with its carboxyl terminal region exposed on the cytosolic side.

Original languageEnglish
Pages (from-to)185-191
Number of pages7
JournalInflammation Research
Issue number5
Publication statusPublished - May 2006
Externally publishedYes


  • Endoplasmic reticulum
  • Green fluorescence protein and protease
  • Histidine decarboxylase
  • Membrane orientation

ASJC Scopus subject areas

  • Immunology
  • Pharmacology


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