Molecular cloning and functional expression of rat leukotriene A4hydrolase using the polymerase chain reaction

Naomasa Makitala, Colin D. Funku, Enyu Imaic, Richard L. Hoover, Kamal F. Badra

Research output: Contribution to journalArticle

Abstract

We isolated a cDNA encoding rat leukotriene A4 (LTA4) hydrolase from mesangial cells by the polymerase chain reaction according to the human amino acid sequence. The deduced amino acid sequence shows that rat LTA, hydrolase is a 609 amino acid protein with an M, 69 kDa. Comparison of human LTA4 hydrolase revealed 93% homology, and include zinc-binding motifs of aminopeptidases. COS-7 cells transfected with the cDNA revealed substantial LTA4 hydrolase activity, and their activities were abolished by preincubation with captopril, representing the first reported cDNA expression of recombinant enzyme in mammalian cells. RNA blot analysis indicated that LTA4 hydrolase was expressed in glomerular endothelial, epithelial and mesangial cells.

Original languageEnglish (US)
Pages (from-to)273-277
Number of pages5
JournalFEBS Letters
Volume299
Issue number3
DOIs
StatePublished - 1992
Externally publishedYes

Keywords

  • Captopril
  • cDNA cloning
  • Glomerular cell
  • Leukotricne A hydrolase
  • PCR (polymerase chain reaction)

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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