The Formyl Peptide Chemoattractant Receptor is Encoded by a 2 Kilobase Messenger RNA, Expression in Xenopus oocytes
Abstract
The migration of phagocytic cells from the blood to sites of infection is an essential component of host defense. This response is mediated by a number of chemoattractants including the bacterially derived formyl peptides which activate cell surface receptors that are functionally coupled to a guanine nucleotide binding regulatory protein (G-protein). Affinity labelling of the formyl peptide chemoattractant receptor (FPCR) yields a single sized glycoprotein with relative molecular mass of 60 -80 kDa. The unglycosylated core peptide is 32 kDa. It is not known whether functional FPCR consists of this single affinity labelled peptide or requires additional subunits for activity. The Xenopus oocyte protein expression system can be used to study heterologous G-protein coupled receptors. We show that a phagocytic cell chemoattractant receptor, the FPCR, can be expressed in a functionally active form in Xenopus oocytes following injection of human myeloid cell RNA.
Document Details
- Document Type
- Technical Report
- Publication Date
- Feb 01, 1990
- Accession Number
- ADA235473
Entities
People
- Elaine K. Gallin
- H. L. Tiffany
- Harry L. Malech
- Philip M. Murphy
Organizations
- Armed Forces Radiobiology Research Institute