Format

Send to

Choose Destination
Biochem Biophys Res Commun. 1993 Jul 30;194(2):720-5.

Cloning and characterization of cDNA encoding a precursor for human adrenomedullin.

Author information

1
First Department of Internal Medicine, Miyazaki Medical College, Japan.

Erratum in

  • Biochem Biophys Res Commun 1994 Jul 15;202(1):643.

Abstract

Adrenomedullin is a novel hypotensive peptide recently isolated from human pheochromocytoma. Since a high concentration of immunoreactive adrenomedullin was found in pheochromocytoma tissue, the cDNA library of pheochromocytoma was constructed, and the cDNA clone encoding an adrenomedullin precursor was isolated and sequenced. The precursor for human adrenomedullin (human preproadrenomedullin) is 185 amino acids in length, including an adrenomedullin sequence. Proadrenomedullin (proAM) contains a unique twenty amino acid sequence followed by Gly-Lys-Arg in the N-terminal region. It is possible that a novel 20 residues peptide, termed "proadrenomedullin N-terminal 20 peptide" (proAM-N20) whose carboxy terminus may be Arg-NH2, is processed from proadrenomedullin. By RNA blot analysis, human adrenomedullin mRNA was found to be highly expressed in several tissues including adrenal medulla, ventricle, lung and kidney as well as pheochromocytoma.

PMID:
7688224
DOI:
10.1006/bbrc.1993.1881
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for Elsevier Science
Loading ...
Support Center