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 language | English (US) |
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Pages (from-to) | 125-130 |
Number of pages | 6 |
Journal | Biochimica et Biophysica Acta - Gene Structure and Expression |
Volume | 1444 |
Issue number | 1 |
DOIs | |
State | Published - 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