By David M. Pollock (auth.), Robert F. Highsmith (eds.)

In Endothelin: Molecular Biology, body structure, and Pathology, educational, scientific, and commercial researchers summarize the dramatic fresh growth that has been documented in endothelin examine and point out the optimum course of destiny stories. The participants, hugely revered gurus of their fields in addition to energetic bench scientists, produce a severe assessment and synthesis of our wisdom of endothelin chemistry and pharmacology, its mechanism of motion, and its physiological capabilities.

Endothelin: Molecular Biology, body structure, and Pathology is bound to develop into the recent typical reference resource for either uncomplicated scientists and expert clinicians who desire a transparent suggestion of the jobs endothelin may well play in cardiovascular body structure and pathology. Biochemists, in addition to medicinal and medical chemists, interested in the improvement of gear designed to change the motion or expression of the endothelin molecule will locate the ebook wealthy in new effects and insights.

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Extra resources for Endothelin: Molecular Biology, Physiology, and Pathology

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245:229-232. 130. Stanimirovic, D. , and Spatz, M. (1994) Endothelin-1 receptor binding and cellular signal transduction in cultured human brain e'ndothelial cells. J. Neuroehem. 62:592--601. 131. De Olivera, A. , Heemskerk, F. , Correa, F. , and Saavedra, J. M. (1995) Characterization of endothelirr A receptors in cerebra1 and periphera1 arteries ofthe rat. Peptides 16:139--144. 132. , Thai, Q. , Kassell, N. , and Lee, K. S. (1994) Cerebra! microvascular responses to endothelins: the role of ETA receptors.

In contrast, perturbation of the carboxyl end of C3 by substitution of hET A residues (296-305) with corresponding residues from the ß2-adrenergic receptor or by deletion ofresidues (291-306) ofthe hETA receptor, results in receptor variants with either impaired or undetectable calcium mobilization. These data suggest that the CT portion of C3 of hET A is important for G-protein activation of phospholipase C (Fig. 5). Deletion of the CT region from N427 to C385 does not affect high-affinity ET-1 binding or calcium mobilization; however, further truncation of CT by a single residue (L384) results in an ETA receptor variant with high-affinity ET-1 binding that is unable to mobilize intracellular calcium (70).

1992) Organdistribution ofthe three rat endothelin messenger RNAs and the effects of ischemia on renal gene expression. J. Cl in. Invest. 90: 1023-1031. 79. Nunez, D. J. , Taylor, E. , Oh, V. M. , Schofield, J. , and Brown, M. J. (1991) Endothelin-1 mRNA expression in the rat kidney. Biochem. J. 275:817-819. 80. , Wang, W. , Brosius, F. , Killen, P. , Keiser, J. , Briggs, J. , and Schnermann, J. (1993) Endothelin-1 mRNA in glomerularandepithelial cells ofkidney. Am. J. Physiol. 265:F542-F550. 81.

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