|Other Names||ADM, Adrenomedullin, AM, Proadrenomedullin N-20 terminal peptide, ProAM N-terminal 20 peptide, PAMP, ProAM-N20, ADM, AM|
|Storage||Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C.|
|Precautions||This product is for research use only. Not for use in diagnostic or therapeutic procedures.|
|Function||AM and PAMP are potent hypotensive and vasodilatator agents. Numerous actions have been reported most related to the physiologic control of fluid and electrolyte homeostasis. In the kidney, am is diuretic and natriuretic, and both am and pamp inhibit aldosterone secretion by direct adrenal actions. In pituitary gland, both peptides at physiologically relevant doses inhibit basal ACTH secretion. Both peptides appear to act in brain and pituitary gland to facilitate the loss of plasma volume, actions which complement their hypotensive effects in blood vessels.|
|Tissue Location||Highest levels found in pheochromocytoma and adrenal medulla. Also found in lung, ventricle and kidney tissues|
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ADM, a hypotensive peptide found in human pheochromocytoma, consists of 52 amino acids, has 1 intramolecular disulfide bond, and shows a slight homology with the calcitonin gene-related peptide. It may function as a hormone in circulation control because it is found in blood in a considerable concentration. The precursor, called preproadrenomedullin, is 185 amino acids long. By RNA-blot analysis, human adrenomedullin mRNA was found to be highly expressed in several tissues. Genomic ADM DNA consists of 4 exons and 3 introns, with the 5-prime flanking region containing TATA, CAAT, and GC boxes.
Kim, S.M., et al. FEBS Lett. 584(1):213-218(2010)Oie, E., et al. Basic Res. Cardiol. 105(1):89-98(2010)Nomura, I., et al. Regul. Pept. 158 (1-3), 127-131 (2009)
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