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Literature DB >> 209312

Cyclic AMP increase the Na+ permeability of the avian erythrocyte membrane by a process which does not involve protein phosphorylation.

Abstract

Preparations of avian erythrocyte plasma membranes have been made which are in the form of sealed vesicles. Using these preparations the permeability of the membranes to N+, K+, Mg2+ and Ca2+ was measured. Monobutyryl cyclic AMP and cyclic AMP increased the permeability to Na+ and Ca+ under conditions where no protein phosphorylation could occur. The only effect of phosphorylation of membrane proteins was to reduce Ca+ permeability. It is thus concluded that cyclic AMP increases Na+ permeability in the avian erythroycte by a direct effect which does not involve protein phosphorylation.

Entities: Chemical

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Year: 1978 PMID： 209312 DOI： 10.1007/bf00241390

Source DB: PubMed Journal: Mol Cell Biochem ISSN： 0300-8177 Impact factor: 3.396

16 in total

1. Role of light and rhodopsin phosphorylation in control of permeability of retinal rod outer segment disks to Ca2plus.

Authors: M Weller; N Virmaux; P Mandel
Journal: Nature Date: 1975-07-03 Impact factor: 49.962

2. Some calculations on the turbidity of mitochondria and bacteria.

Authors: A L KOCH
Journal: Biochim Biophys Acta Date: 1961-08-19

3. Regulation of phosphorylation of a specific protein in toad-bladder membrane by antidiuretic hormone and cyclic AMP, and its possible relationship to membrane permeability changes.

Authors: R J DeLorenzo; K G Walton; P F Curran; P Greengard
Journal: Proc Natl Acad Sci U S A Date: 1973-03 Impact factor: 11.205

4. Regulation of protein phosphorylation and membrane permeability by beta-adrenergic agents and cyclic adenosine 3':5'-monophosphate in the avian erythrocyte.

Authors: S A Rudolph; P Greengard
Journal: J Biol Chem Date: 1974-09-10 Impact factor: 5.157

1. The soluble, cyclic AMP-stimulated protein kinase catalyses the phosphorylation of different membrane proteins from those which are phosphorylated by the membrane bound enzyme.

Authors: M Carstens; M Weller
Journal: Mol Cell Biochem Date: 1981-10-30 Impact factor: 3.396

1 in total

Cyclic AMP increase the Na+ permeability of the avian erythrocyte membrane by a process which does not involve protein phosphorylation.

1. Role of light and rhodopsin phosphorylation in control of permeability of retinal rod outer segment disks to Ca2plus.

2. Some calculations on the turbidity of mitochondria and bacteria.

3. Regulation of phosphorylation of a specific protein in toad-bladder membrane by antidiuretic hormone and cyclic AMP, and its possible relationship to membrane permeability changes.

4. Regulation of protein phosphorylation and membrane permeability by beta-adrenergic agents and cyclic adenosine 3':5'-monophosphate in the avian erythrocyte.

5. The effect of epinephrine and other agents on adenyl cyclase in the cell membrane of avian erythrocytes.

6. A light-scattering technique for the study of the permeability of rat brain synaptosomes in vitro.

7. A simple method for the preparation of 32-P-labelled adenosine triphosphate of high specific activity.

8. A possible role of the phosphorylation of synaptic membrane proteins in the control of calcium ion permeability.

9. Effects of vasopressin on toad bladder membrane proteins: relationship to transport of sodium and water.

10. Phosphate binding by cerebral microsomes in relation to adenosine-triphosphatase activity.

1. The soluble, cyclic AMP-stimulated protein kinase catalyses the phosphorylation of different membrane proteins from those which are phosphorylated by the membrane bound enzyme.