By Kazuo Kitamura, Kenji Kangawa, Tanenao Eto (auth.), Toshio Nishikimi MD, PhD (eds.)
Adrenomedullin used to be stumbled on in 1993 in an extract of human pheochromocytoma whereas tracking cAMP degrees in rat platelets. Adrenomedullin has attracted huge curiosity between cardiologists because of its influence at the cardiovascular procedure which incorporates a lessen in blood strain in vivo; an influence on vascular tender muscle cells; raises cAMP degrees; ultimately reduces blood strain and has a task within the pathogenesis of arteriosclerosis.
Adrenomedullin in heart problems is an updated evaluate of the main suitable elements of adrenomedullin. It contains a huge diversity of fields together with biochemistry, molecular biology, body structure, pharmacology, pathophysiology of heart problems and medical functions of adrenomedullin to cardiovascular disease.
Toshio Nishikimi, MD, PhD, is an affiliate Professor within the division of high blood pressure and Cardiorenal medication, Dokkyo college tuition of medication, Tochigi, Japan.
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Extra info for Adrenomedullin in Cardiovascular Disease
Iwasaki H, Eguchi S, Shichiri M, Marumo F, and Hirata Y (1998b) Downregulation of adenylate cyclase coupled to adrenomedullin receptor in vascular smooth muscle cells. Eur J Pharmacol 352:131-134. Iwasaki H, Shichiri M, Marumo F, and Hirata Y (2001) Adrenomedullin stimulates proline-rich tyrosine kinase 2 in vascular smooth muscle cells. Endocrinology 142:564-572. Kano H, Kohno M, Yasunari K, Yokokawa K, Horio T, Ikeda M, Minami M, Hanehira T, Takeda T, and Yoshikawa J. (1996) Adrenomedullin as a novel antiproliferative factor of vascular smooth muscle cells.
IJAM binding studies obviously revealed that CGRP was about three orders of magnitude less than AM, suggesting highly specific receptors for AM. Since a wide variety of cells and tissues, including lung, heart, and vascular tissue, have both specific CGRP and AM binding sites, it is difficult to distinguish between two distinct, but very similar receptors in these tissues. Collectively, AM appears to exert its biological effect through its specific AM receptor and/or CGRP1 receptor. 08 (Kd) >1000 Upton etaL, 1997 Rat heart Shimekakeetal,1995 IQQ: concentration inhibiting binding by 50%; Ki: absolute inhibition constant; Kd: dissociation constant; *exact I Q , could not be calculated.
2001). AM rapidly (within 1 min) phosphorylates Pyk 2, followed by a gradual decline to the basal level by 10 min; the time course of Pyk 2 phophorylation was identical with its kinase activity as confirmed by immuno-complex kinase assay. Furthermore, immunoprecipitation studies revealed that Pyk 2 activation induced interaction with and activation of c-Src, a non-receptor PTK, subsequently leading to complex formation with adaptor proteins (She and Grb2). , 2001). Our data demonstrated for the first time the involvement of non-receptor PTK/ERK pathway in VSMCs in the mitogenic action by AM (Fig.