[Relation between the characteristic activity of the beta-adrenergic agonist isoproterenol and the percolation properties of cell membrane].
Variations in the intrinsic activity of 1-isoproterenol and in the percentage of high affinity beta-receptor complexes have been studied under a changes in the macrostructure of reticulocyte plasma membranes. The fluid lipid fraction have been reduced in the membranes for this by phospholipase A2/BSA treatment. It was accompanied by a progressive decrease in the fraction of beta-receptors that are able to form the high affinity complexes with 1-isoproterenol (receptor--regulatory N-protein complexes). Evaluated with the ability to activate the adenylate cyclase, the intrinsic activity of 1-isoproterenol was decreased from 1 to 0 under with conditions. This variations proved to correlate strongly with each other. Thus, changes in the membrane macrostructure may directly determine an efficiency of hormone actions.
Kazarov
A R
AR
Rozenkrants
A A
AA
Sobolev
A S
AS
D000262:Adenylyl Cyclases / Q000378:metabolism; D000818:Animals; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism*; D002463:Cell Membrane Permeability; D066298:In Vitro Techniques; D007545:Isoproterenol / Q000494:pharmacology*; D008563:Membrane Lipids / Q000378:metabolism; D051381:Rats; D011943:Receptors, Adrenergic, beta / Q000187:drug effects / Q000378:metabolism*; D012156:Reticulocytes / Q000187:drug effects / Q000378:metabolism
D008563:Membrane Lipids; D011943:Receptors, Adrenergic, beta; D000262:Adenylyl Cyclases; D007545:Isoproterenol
Zavisimost' kharakteristicheskoĭ aktivnosti beta-adrenergicheskogo agonista izoproterenola ot perkoliatsionnykh svoĭstv plazmaticheskoĭ membrany kletki.