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Molecular properties of apelin: tissue distribution and receptor binding.

Y. Kawamata,Y. Habata,S. Fukusumi,M. Hosoya,Ryo Fujii,S. Hinuma,N. Nishizawa,C. Kitada,H. Onda,O. Nishimura,M. Fujino

Published 2001 in Biochimica et Biophysica Acta

ABSTRACT

We analyzed the tissue distribution of apelin mRNA in rats by a quantitative reverse transcription-polymerase chain reaction and that of immunoreactive apelin (ir-apelin) by an enzyme immunoassay (EIA) using a monoclonal antibody. The expression levels of apelin mRNA and ir-apelin seemed to be consistent among tissues: they were highly expressed in the lung and mammary gland. By the combination of gel filtration and EIA, we found that the molecular forms of apelin differ among respective tissues: apelin molecules with sizes close to apelin-36 (long forms) were major components in the lung, testis, and uterus, but both long and short (whose sizes were close to [<Glu(65)]apelin-13) forms were detected in the mammary gland. In Scatchard analyses, the radioiodinated apelin-36 analogue bound to the receptor, APJ, with high affinity. In competitive binding assays, apelin-36 and apelin-19 far more efficiently inhibited the binding of the labeled apelin-36 analogue with APJ than [<Glu(65)]apelin-13. In analyses for the dissociation of apelin from APJ, unlabeled apelin-36 replaced more rapidly the labeled apelin-36 analogue bound with APJ than [<Glu(65)]apelin-13. Our results demonstrate that the long and short forms of apelin differently interact with APJ.

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