Molecular characterization of cDNA for phospholipase A2-activating protein

A. K. Chopra, D. A. Ribardo, T. G. Wood, D. J. Prusak, X. J. Xu, J. W. Peterson

Research output: Contribution to journalArticle

12 Scopus citations

Abstract

A phospholipase A2-activating protein (PLAP) cDNA was cloned and sequenced from a human monocyte cDNA library, and expressed as a histidine- tagged fusion protein. The DNA-deduced aa sequence of human PLAP was 80,826 Da; however, SDS-PAGE analysis revealed a 72-74 kDa protein which matched the size of native PLAP from human monocytes. Anti-sense plap oligonucleotide blocked cholera toxin-induced release of 3H-labeled arachidonic acid from cells, indicating a potential role for PLAP in regulating phospholipase A2 activity.

Original languageEnglish (US)
Pages (from-to)125-130
Number of pages6
JournalBiochimica et Biophysica Acta - Gene Structure and Expression
Volume1444
Issue number1
DOIs
StatePublished - Jan 18 1999

Keywords

  • 3'-Rapid amplification of cDNA ends
  • Anti-sense plap oligonucleotide
  • CDNA cloning sequencing, and expression
  • Phospholipase A-activating protein
  • Phospholipase A-activating protein cDNA
  • Reverse transcriptase polymerase chain reaction

ASJC Scopus subject areas

  • Structural Biology
  • Biophysics
  • Biochemistry
  • Genetics

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