Adrenomedullin

Title: Adrenomedullin
Literature References: Hypotensive peptide originally isolated from human pheochromocytoma; subsequently found in all tissues with highest levels in heart, kidney, lung and adrenal gland. Highly conserved among species, human form is a 52-amino acid peptide; shares some sequence homology with calcitonin gene related peptide and amylin, q.v. Plasma levels are elevated in patients with hypertension and heart failure. Biological effects include vasodilation, diuresis and increased cardiac output; also exhibits antiproliferative and anti-apoptotic effects in the myocardium and stimulates angiogenesis. Isoln and hypotensive activity: K. Kitamura et al., Biochem. Biophys. Res. Commun. 192, 553 (1993). RIA determn in plasma: L. K. Lewis et al., Clin. Chem. 44, 571 (1998). Review of biosynthesis, pharmacology and bioactivities: J. P. Hinson et al., Endocr. Rev. 21, 138-167 (2000). Series of articles on physiological roles: Regul. Pept. 112 1-196 (2003). Review of clinical relevance and therapeutic potential: D. C. Bunton et al., Pharmacol. Ther. 103, 179-201 (2004); S. A. Hamid, G. F. Baxter, ibid. 105, 95-112 (2005).
Aequorin Affinin Aflatoxins B Aflatoxins G Aflatoxins M

Adrenomedullin
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols ADM (; AM)
External IDs OMIM: 103275 MGI: 108058 HomoloGene: 873 GeneCards: ADM Gene
RNA expression pattern
PBB GE ADM 202912 at tn.png
More reference expression data
Orthologs
Species Human Mouse
Entrez 133 11535
Ensembl ENSG00000148926 ENSMUSG00000030790
UniProt P35318 P97297
RefSeq (mRNA) NM_001124 NM_009627
RefSeq (protein) NP_001115 NP_033757
Location (UCSC) Chr 11:
10.33 – 10.33 Mb
Chr 7:
110.63 – 110.63 Mb
PubMed search [1] [2]

Adrenomedullin is a peptide hormone that in humans is encoded by the ADM gene.

is a peptide associated with pheochromocytoma- a tumour arising from adrenal medulla. It was discovered in 1993.[1]

Adrenomedullin (AM) is a ubiquitously expressed peptide initially isolated from phaechromyctoma.[2] A second peptide AM2 has been identified, exhibiting a similar functions.[3]