Adrenomedullin/ADM: Lysates

Adrenomedullin (ADM; also AM) is a secreted, monomeric, 6 kDa member of the Adrenomedullin family of molecules. It is widely expressed, being found in smooth muscle cells, endothelium, adrenal medulla chromaffin cells, fibroblasts and keratinocytes. ADM has multiple functions, including vasodilation, the maintenance of vascular integrity, and the suppression of inflammatory mediator secretion. The human ADM preproprecursor is 185 amino acids (aa) in length. It contains a 21 aa signal sequence, a processed 20 aa peptide termed PAMP (aa 22-41), an N-terminal propeptide (aa 45-92), the ADM precursor (amidation is required for maturation) (aa 95-147), and a C-terminal propeptide (aa 148-185). The ADM precursor with a terminal Gly147 circulates naturally with bioactive, mature amidated ADM (aa 95-146). Depending upon the tissue, truncated forms of ADM likely also occur, including variants spanning aa 120-146 and 128-146. Over aa 22-147, the human ADM proprecursor shares 70% aa identity with mouse ADM proprecursor.