Molecular cloning and characterization of the platelet-activating factor receptor gene expressed in the human heart

T Sugimoto, H Tsuchimochi, CGA McGregor… - Biochemical and …, 1992 - Elsevier
T Sugimoto, H Tsuchimochi, CGA McGregor, H Mutoh, T Shimizu, Y Kurachi
Biochemical and biophysical research communications, 1992Elsevier
PAF decreases cardiac contractility and blood pressure. To characterize the cardiac PAF
receptor, we screened a human ventricular cDNA library in a low stringency condition, using
a PCR product derived from guinea pig lung PAF receptor as a probe. Four clones were
obtained and named HV1–4. In Xenopus oocytes injected with cRNA derived from HV3 or 4
but not from HV1 or 2, PAF elicited a Ca 2+-activated Cl-current. HV3 and HV4 were
duplicate clones, encoding a 342 amino-acid polypeptide which was identical to that of the …
Abstract
PAF decreases cardiac contractility and blood pressure. To characterize the cardiac PAF receptor, we screened a human ventricular cDNA library in a low stringency condition, using a PCR product derived from guinea pig lung PAF receptor as a probe. Four clones were obtained and named HV1–4. In Xenopus oocytes injected with cRNA derived from HV3 or 4 but not from HV1 or 2, PAF elicited a Ca2+-activated Cl-current. HV3 and HV4 were duplicate clones, encoding a 342 amino-acid polypeptide which was identical to that of the human leukocyte PAF receptor. However, a portion of the 5′ untranslated region of HV3 (or 4) was different from that of the leukocyte receptor cDNA. Northern blotting of human ventricles and atria using the HV3 insert showed a single band of ∼4 kb. These results suggest a tissue-specific translational mechanism responsible for regulation of the expression of the PAF receptor mRNA in these tissues.
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