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Volume 352, Issue 2 p. 105-108
Full-length article
Free Access

Distribution and characterization of immunoreactive rat adrenomedullin in tissue and plasma

Junichiro Sakata

Junichiro Sakata

First Department of Internal Medicine, Miyazaki Medical College, Kihara Kiyotake, Miyazaki 889-16, Japan

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Toru Shimokubo

Toru Shimokubo

First Department of Internal Medicine, Miyazaki Medical College, Kihara Kiyotake, Miyazaki 889-16, Japan

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Kazuo Kitamura

Kazuo Kitamura

First Department of Internal Medicine, Miyazaki Medical College, Kihara Kiyotake, Miyazaki 889-16, Japan

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Masatoshi Nishizono

Masatoshi Nishizono

First Department of Internal Medicine, Miyazaki Medical College, Kihara Kiyotake, Miyazaki 889-16, Japan

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Yoshinari Iehiki

Yoshinari Iehiki

First Department of Internal Medicine, Miyazaki Medical College, Kihara Kiyotake, Miyazaki 889-16, Japan

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Kenji Kangawa

Kenji Kangawa

National Cardiovascular Center Research Institute, Fujishirodai, Suita, Osaka 565, Japan

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Hisayuki Matsuo

Hisayuki Matsuo

National Cardiovascular Center Research Institute, Fujishirodai, Suita, Osaka 565, Japan

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Tanenao Eto

Tanenao Eto

First Department of Internal Medicine, Miyazaki Medical College, Kihara Kiyotake, Miyazaki 889-16, Japan

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First published: September 26, 1994
Citations: 214
Corresponding author. Fax: (81) (985) 85 6596.

Abstract

Adrenomedullin is a new bioactive peptide recently isolated from pheochromocytoma. We report on the rat adrenomedullin distribution and molecular forms in various tissues and plasma. Using a sensitive radioimmunoassay system for rat adrenomedullin, high concentrations of immunoreactive rat adrenomedullin were detected in adrenal gland, lung and cardiac atrium. In lung and atrium, the immunoreactivity concentration in rat was about 6–10 times higher than that in human. The mean plasma concentration of immunoreactive rat adrenomedullin was 3.60 ±0.34 fmol/ml (mean ± S.D.). Analysis in adrenal gland, lung and atrium with reverse-phase and gel-filtration high-performance liquid chromatography showed that most immunoreactive rat adrenomedullin emerged as a single peak at a position exactly identical to that of the authentic rat adrenomedullin peptide, synthesized according to the sequence predicted from the cDNA.