Adrenomedullin (ADM), initially identified in human pheochromocytoma, participates in a wide range of physiological and pathological processes, including vasorelaxation, angiogenesis and apoptosis.
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.
Adrenomedullin (AM) is a potent hypotensive peptide recently discovered from human pheochromocytoma tissue by its stimulating activity of platelet cAMP production.
Adrenomedullin (AM) is a 52-amino acid peptide with anti-inflammatory, anti-apoptotic, and anti-oxidative properties discovered in a human pheochromocytoma.
Both protein kinase A- and C-dependent mechanisms regulate ADM mRNA expression in adrenocortical and pheochromocytoma cells supporting the suggested role for ADM as an autocrine or paracrine (or both) regulator of adrenal function.
Thirteen years after the isolation of adrenomedullin (AM) from a human pheochromocytoma, the literature is awash with reports describing its implication in countless physiological and disease mechanisms ranging from vasodilatation to cancer promotion.
Adrenomedullin (AM) is a recently discovered potent vasodilatory peptide, originally isolated in extracts of human pheochromocytoma, with activities including maintenance of cardiovascular and renal homeostasis through vasodilatation, diuresis and natriuresis.
We discovered adrenomedullin (AM) from human pheochromocytoma tissue by monitoring the elevating activity of intracellular cyclic AMP (cAMP) in rat platelets in 1993.