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Comparative Study
. 2001 Apr 23;1538(2-3):162-71.
doi: 10.1016/s0167-4889(00)00143-9.

Molecular properties of apelin: tissue distribution and receptor binding

Y Kawamata  1 , Y Habata, S Fukusumi, M Hosoya, R Fujii, S Hinuma, N Nishizawa, C Kitada, H Onda, O Nishimura, M Fujino
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Free article
Comparative Study

Molecular properties of apelin: tissue distribution and receptor binding

Y Kawamata et al. Biochim Biophys Acta. .
Free article

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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