Characterization and expression of the complementary DNA encoding rat histidine decarboxylase

David R. Joseph, Patrick M. Sullivan, Yan Min Wang, Christine Kozak, David A. Fenstermacher, Mark E. Behrendsen, Cynthia A. Zahnow

Research output: Contribution to journalArticle

Abstract

Histamine is a neurotransmitter in the central nervous system and an important modulator of gastric acid secretion, vasomotor control, inflammation, and allergic reactions. In biological systems the formation of histamine from its precursor histidine is catalyzed by the enzyme L-histidine decarboxylase (HDC; L-histidine carboxy-lyase, EC 4.1.1.22). We have cloned HDC-encoding cDNA from a fetal rat liver cDNA library (phage A gt11) and have deduced the amino acid sequence from the nucleotide sequence. The clone was proven to be HOC cDNA by expression of active recombinant enzyme in COS cells and by chromosomal mapping. The cDNA encodes a protein of Mr 73,450 (655 amino acid residues). The discrepancy between this molecular weight and the size of the purified fetal liver protein subunits [Taguchi, Y., Watanabe, T., Kubota, H., Hayashi, H. & Wada, H. (1984) J. Biol. Chem. 259, 5214-5221] (Mr = 54,000) suggests that HDC may be posttranslationally processed. The 469 amino acid residues from the amino-terminal portion of the protein share 50% identity with rat and Drosophila L-dopa decarboxylases and much less homology with other characterized amino acid decarboxylases.

Original languageEnglish (US)
Pages (from-to)733-737
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume87
Issue number2
DOIs
StatePublished - 1990

Keywords

  • Amino acid sequence
  • Chromosomal mapping
  • Dopa decarboxylase
  • Fetal liver
  • Histamine

ASJC Scopus subject areas

  • General

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