Increased cyclic adenosine 3',5'-monophosphate inhibits G protein-coupled activation of phospholipase C in rat FRTL-5 thyroid cells.
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چکیده
منابع مشابه
Effects of adenosine 5'-monophosphate and adenosine 3',5'-cyclic monophosphate on l cells.
The adenine nucleotides, 5'-AMP and 3',5'-cyclic AMP block L cells in the S-phase of the cell cycle. The intracellular level of cyclic AMP is reduced after incubation of cells with 5'-AMP, and rates of uridine transport are increased after incubation with either 5'-AMP or cyclic AMP. On the contrary, cyclic AMP levels are increased and uridine transport decreased in cells treated with an inhibi...
متن کاملDifferential binding of cyclic adenosine 3' ,5'-monophosphate to the cyclic adenosine 3' ,5'-monophosphate receptor protein in Escherichia coli.
Binding of cyclic adenosine 3' ,5'-monophosphate (cAMP) by the cAMP receptor protein in crude cell-free extracts of Escherichia coli was characterized. When cell were grown in glucose, binding was inhibited 50% relative to extracts from cells grown with succinate as carbon source . This inhibition could be relieved by dialysis.
متن کاملRenal Effects of Adenosine 3 ' , 5 ' - Cyclic Monophosphate and Dibutyryl Adenosine 3 , 5 ' - Cyclic Monophosphate
An abstract of this work appeared in 1970 Abstracts, The American Society of Nephrology. Received for publication 27 October 1970 and in revised form 28 January 1971. similar to the effect of renal arterial infusion of isoproterenol. The results suggest that synthesis of cyclic AMP in proximal renal tubule cells in response to stimulation of beta adrenergic or other receptors can mediate a decr...
متن کاملActivation by cyclic 3':5'-adenosine monophosphate of tyrosine hydroxylase in the rat brain.
Membrane-permeable derivatives of cyclic AMP (cAMP) produced concentration-dependent increases in activity of tyrosine hydroxylase (L-tyrosine, tetrahydropteridine:oxygen oxidoreductase (3-hydroxylating), EC 1.14.16.2) in membrane-limited nerve endings (synaptosomes) prepared from three regions of rat brain. Increased hydroxylation occurred even after preincubation and removal of dibutyryl cycl...
متن کاملPhosphorylation of endogenous protein of rat brain by cyclic adenosine 3',5'-monophosphate-dependent protein kinase.
The ability of proteins in various subcellular fractions of the rat cerebrum to act as substrates for a partially purified cyclic adenosine 3’,5’-monophosphate (cyclic AMP)-dependent protein kinase has been studied in vitro. Distribution of substrates generally paralleled the distribution of activity of protein kinase as well as of adenylate cyclase and cyclic nucleotide phosphodiesterase. Alth...
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ژورنال
عنوان ژورنال: Endocrinology
سال: 1996
ISSN: 0013-7227,1945-7170
DOI: 10.1210/endo.137.8.8754735