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Isolation and properties of platelet-activating factor receptor cDNAs
M Nakamura1, Z Honda, T Matsumoto
1Department of Biochemistry, Faculty of Medicine, University of Tokyo, Japan.
Journal of Lipid Mediators
|March 1, 1993
Summary
Researchers cloned the platelet-activating factor (PAF) receptor from guinea pig and human cells. This G-protein-linked receptor plays a role in cellular signaling and may be involved in desensitization processes.
Area of Science:
- Molecular Biology
- Biochemistry
- Pharmacology
Background:
- Platelet-activating factor (PAF) is a potent lipid mediator involved in various physiological and pathological processes.
- Understanding the PAF receptor's structure and function is crucial for developing targeted therapies.
Purpose of the Study:
- To clone and characterize the cDNA encoding the platelet-activating factor (PAF) receptor from guinea pig and human sources.
- To investigate the signaling pathways activated by the PAF receptor.
Main Methods:
- Cloning of guinea pig PAF receptor cDNA using a Xenopus laevis oocyte expression system.
- Isolation of human PAF receptor cDNA using a guinea pig cDNA probe.
- Expression of receptors in COS-7 cells and oocytes for functional analysis.
Main Results:
- Both guinea pig and human PAF receptors consist of 342 amino acids with seven transmembrane domains, belonging to the G-protein-linked receptor superfamily.
- High amino acid identity (83% overall, 91% in transmembrane domains) was observed between the two receptors.
- PAF receptor activation led to inositol 1,4,5-trisphosphate production and was mediated by G-proteins, as evidenced by inhibition of Cl- current.
Conclusions:
- The study successfully cloned and characterized both guinea pig and human PAF receptors.
- Conserved serine and threonine residues suggest a role in receptor desensitization.
- Evidence supports the involvement of G-proteins in PAF-induced phosphoinositide turnover.