Water and urea permeability properties of Xenopus oocytes: expression of mRNA from toad urinary bladder

Water and urea permeability properties of Xenopus oocytes: expression of mRNA from toad urinary... expression cloning of a variety of membrane receptor proteins (1, 6, 15, 17, 22, 31, 36). Because microinjected heterologous mRNA is often translated correctly processed targeted in the , proteins can be cloned without knowledge of biochemical identity, provided that a functional or morphological assay exists for the expressed protein. In a recent study, expression of mRNA from a glucose er cDNA clone conferred a greatly increased glucose permeability a slightly increased permeability in Xenopus s (13). Expression of unfractionated mRNA from kidney reticulocyte conferred a greatly increased permeability in Xenopus s that was inhibited C26 0363-6143/91 $1.50 Copyright by mercurials (37). It has been extremely difficult to obtain reliable information about the identity of ers (for reviews, see Refs. 21, 32). Some reasons include the lack of selective inhibitors, the high endogenous permeability of bilayers in the absence of channels, the potentially low membrane density of ers. ers are present in the red blood cell (21), kidney (23, 35), amphibian urinary bladder (16, 28), possibly in other cell types (12). In the kidney collecting tubule amphibian urinary bladder, permeabilities are stimulated by vasopressin acting through an adenosine 3’,5’-cyclic monophosphate (CAMP) second messenger system. permeability is probably regulated http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png AJP - Cell Physiology The American Physiological Society

Water and urea permeability properties of Xenopus oocytes: expression of mRNA from toad urinary bladder

AJP - Cell Physiology, Volume 260: C26 – Jan 1, 1991

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Publisher
The American Physiological Society
Copyright
Copyright © 1991 the American Physiological Society
ISSN
0363-6143
eISSN
1522-1563
Publisher site
See Article on Publisher Site

Abstract

expression cloning of a variety of membrane receptor proteins (1, 6, 15, 17, 22, 31, 36). Because microinjected heterologous mRNA is often translated correctly processed targeted in the , proteins can be cloned without knowledge of biochemical identity, provided that a functional or morphological assay exists for the expressed protein. In a recent study, expression of mRNA from a glucose er cDNA clone conferred a greatly increased glucose permeability a slightly increased permeability in Xenopus s (13). Expression of unfractionated mRNA from kidney reticulocyte conferred a greatly increased permeability in Xenopus s that was inhibited C26 0363-6143/91 $1.50 Copyright by mercurials (37). It has been extremely difficult to obtain reliable information about the identity of ers (for reviews, see Refs. 21, 32). Some reasons include the lack of selective inhibitors, the high endogenous permeability of bilayers in the absence of channels, the potentially low membrane density of ers. ers are present in the red blood cell (21), kidney (23, 35), amphibian urinary bladder (16, 28), possibly in other cell types (12). In the kidney collecting tubule amphibian urinary bladder, permeabilities are stimulated by vasopressin acting through an adenosine 3’,5’-cyclic monophosphate (CAMP) second messenger system. permeability is probably regulated

Journal

AJP - Cell PhysiologyThe American Physiological Society

Published: Jan 1, 1991

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