?-Adrenergic agonists increase phosphorylation of elongation factor 2 in cardiomyocytes without eliciting calcium-independent eEF2 kinase activity
?-Adrenergic agonists increase phosphorylation of elongation factor 2 in cardiomyocytes without eliciting calcium-independent eEF2 kinase activity
The ?-adrenergic agonist isoproterenol increased the phosphorylation of elongation factor eEF2 in ventricular cardiomyocytes from adult rats (ARVC). Phosphorylation of eEF2 inhibits its activity, and protein synthesis was inhibited in ARVC concomitantly with increased eEF2 phosphorylation. eEF2 kinase activity in ARVC extracts was completely dependent upon Ca2+/calmodulin. In contrast to other cell types, however, treatments designed to raise intracellular cAMP failed to induce Ca2+/calmodulin-independent activity. Instead, they increased maximal eEF2 kinase activity. Similar data were obtained when partially purified ARVC eEF2 kinase was treated with cAMP-dependent protein kinase in vitro. These data suggest that ARVC possess a distinct isoform of eEF2 kinase.
protein synthesis, elongation, myocyte, heart, kinase, calcium
225-228
McLeod, Laura E.
b927ae59-bc6a-446b-a0dc-cb17b6390d31
Wang, Lijun
55ff0417-5993-46ee-8e5f-01a972c72f6a
Proud, Christopher G.
59dabfc8-4b44-4be8-a17f-578a58550cb3
2 February 2001
McLeod, Laura E.
b927ae59-bc6a-446b-a0dc-cb17b6390d31
Wang, Lijun
55ff0417-5993-46ee-8e5f-01a972c72f6a
Proud, Christopher G.
59dabfc8-4b44-4be8-a17f-578a58550cb3
McLeod, Laura E., Wang, Lijun and Proud, Christopher G.
(2001)
?-Adrenergic agonists increase phosphorylation of elongation factor 2 in cardiomyocytes without eliciting calcium-independent eEF2 kinase activity.
FEBS Letters, 489 (2-3), .
(doi:10.1016/S0014-5793(01)02100-7).
Abstract
The ?-adrenergic agonist isoproterenol increased the phosphorylation of elongation factor eEF2 in ventricular cardiomyocytes from adult rats (ARVC). Phosphorylation of eEF2 inhibits its activity, and protein synthesis was inhibited in ARVC concomitantly with increased eEF2 phosphorylation. eEF2 kinase activity in ARVC extracts was completely dependent upon Ca2+/calmodulin. In contrast to other cell types, however, treatments designed to raise intracellular cAMP failed to induce Ca2+/calmodulin-independent activity. Instead, they increased maximal eEF2 kinase activity. Similar data were obtained when partially purified ARVC eEF2 kinase was treated with cAMP-dependent protein kinase in vitro. These data suggest that ARVC possess a distinct isoform of eEF2 kinase.
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Published date: 2 February 2001
Keywords:
protein synthesis, elongation, myocyte, heart, kinase, calcium
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Local EPrints ID: 56746
URI: http://eprints.soton.ac.uk/id/eprint/56746
ISSN: 0014-5793
PURE UUID: 67f836b8-4c9d-496d-9fde-f0fe3f3b57df
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Date deposited: 07 Aug 2008
Last modified: 15 Mar 2024 11:03
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Contributors
Author:
Laura E. McLeod
Author:
Lijun Wang
Author:
Christopher G. Proud
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