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By J. X. Thomas Jr. Ph.D., M. W. Gerdisch (auth.), Gerd Heusch, John Ross Jr. (eds.)

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However, much less is known regarding the coupling of lXI-adrenergic receptors to intracellular events. For example, although 1X2-adrenergic receptors appear to couple through G i and, thereby, produce an inhibitory effect on adenylate cyclase, the Gprotein which couples intracellular events to IXI -adrenergic receptors has not been characterized fully [8]. The IXI -adrenergic receptor is a complex glycoprotein of a molecular weight of about 85 KDa [14]. The overall structure of the lXI-adrenergic receptor has recently been obtained after cloning of the receptor protein, which indicates that the structure is very similar to other surface membrane receptors, including the Pl- and 1l2-adrenergic receptors, the muscarinic receptor subtypes, and the serotonin receptor subtypes, among others [45, 46].

D. DaTorre Cardiovascular Division, Department of Internal Medicine and Department of Pharmacology, Washington University School of Medicine, st. Louis, Missouri, USA Summary The lXI-adrenergic receptor exists as at least two distinct subtypes, IX la and IXlb' Based on hydrophobic exclusion studies and limited proteolysis of the cloned receptor, it appears to possess characteristics analogous to other membrane-bound receptors including seven membrane spanning domains, three extracellular, and three intracellular loops, with extensive glycosylation near the extracellular amino terminus.

B. Corr, K. A. Yamada and S. D. DaTorre Cardiovascular Division, Department of Internal Medicine and Department of Pharmacology, Washington University School of Medicine, st. Louis, Missouri, USA Summary The lXI-adrenergic receptor exists as at least two distinct subtypes, IX la and IXlb' Based on hydrophobic exclusion studies and limited proteolysis of the cloned receptor, it appears to possess characteristics analogous to other membrane-bound receptors including seven membrane spanning domains, three extracellular, and three intracellular loops, with extensive glycosylation near the extracellular amino terminus.

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