Abstract
Recoverin, a new calcium binding protein from bovine rod photoreceptor cells, activates guanylyl cyclase below a free calcium concentration of 200 nM. We show here that recoverin is phosphorylated by an endogenous kinase and Mg-ATP at the same decreased calcium concentration. The calcium-dependent activation of guanylyl cyclase is enhanced in the presence of ATP. We suggest that phosphorylation of recoverin reinforces the stimulation of guanylyl cyclase at decreased calcium concentrations.
MeSH terms
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Adenosine Triphosphate / metabolism
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Adenosine Triphosphate / pharmacology
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Animals
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Calcium / pharmacology*
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Calcium-Binding Proteins / metabolism*
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Calcium-Binding Proteins / pharmacology
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Cattle
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Enzyme Activation / drug effects
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Eye Proteins*
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Guanylate Cyclase / metabolism*
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Hippocalcin
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Lipoproteins*
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Nerve Tissue Proteins*
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Phosphorylation
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Photoreceptor Cells / enzymology*
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Protein Kinases / metabolism
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Recoverin
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Rod Cell Outer Segment / chemistry
Substances
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Calcium-Binding Proteins
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Eye Proteins
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Lipoproteins
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Nerve Tissue Proteins
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Recoverin
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Hippocalcin
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Adenosine Triphosphate
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Protein Kinases
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Guanylate Cyclase
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Calcium