NDLI: Transfer of glucagon receptor from liver membranes to a foreign adenylate cyclase by a membrane fusion procedure.

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Transfer of glucagon receptor from liver membranes to a foreign adenylate cyclase by a membrane fusion procedure.

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Transfer of glucagon receptor from liver membranes to a foreign adenylate cyclase by a membrane fusion procedure.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Schramm, M.
Abstract	Previous work had demonstrated the coupling of a beta-adrenergic receptor on an erythrocyte with the adenylate cyclase [ATP pyrophosphate-lyase (cyclizing), EC 4.6.1.1] of a tissue culture cell when the two cells were fused by Sendai virus. The validity of this finding for animal tissues in general, for membrane preparations, and for peptide hormone receptors could hitherto not be assessed. Available fusion procedures worked efficiently only with certain intact cells from tissue culture and with erythrocytes. In the present work a membrane fusion method was developed that causes the transfer of the glucagon receptor from purified rat liver membranes to Friend erythroleukemia cells; even direct transfer to a membrane fraction prepared from Friend cells became feasible. It can therefore be concluded that a peptide hormone receptor in a normal tissue membrane has properties similar to those demonstrated for a beta-adrenergic receptor in an erythrocyte: it exists in the membrane as a dissociable independent unit that can readily couple with the adenylate cyclase of a foreign cell. The efficiency of the membrane fusion procedure is due to the combined action of polyethylene glycol, phospholipids, stearylamine, and ATP in a salt medium. The method promises to be applicable to membranes of various cells and tissues, and it can probably be used to analyze hormone receptors and adenylate cyclase systems in states of malfunction by transfer to their respective counterpart in a normal cell membrane. Studies in biochemical hybridization of membrane components need not be limited to hormone activation of adenylate cyclase. With the aid of the membrane fusion method, this approach could be applied to any dissociable multicomponent system in biological membranes.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	3
Volume Number	76
Language	English
Publisher	National Academy of Sciences
Publisher Date	1979-07-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Adenylate Cyclase Metabolism Glucagon Liver Receptors, Cell Surface Animals Cell Fusion Cell Line Cell Membrane Drug Effects Ultrastructure Ethylmaleimide Pharmacology Membrane Lipids Phospholipids Receptors, Adrenergic, Beta Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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