Abstract
The effect of N-beta-alanyl-5-S-glutathionyl-dopa (5-S-GAD), a compound originally isolated from Sarcophaga peregrina (a flesh fly) as an antibacterial substance, on protein phosphorylation was examined using v-src-transformed NIH3T3 cell lysates. 5-S-GAD was found to inhibit tyrosine phosphorylation of protein tyrosine kinase v-src, but not serine/threonine phosphorylation of protein kinase C. The potency of this compound was comparable to that of herbimycin A. Our results suggested that a substitution at position 5 of the catechol in 5-S-GAD with the sulfur of cysteine is essential for 5-S-GAD to inhibit protein tyrosine kinase v-src.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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3T3 Cells
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Animals
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Anti-Infective Agents / isolation & purification
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Anti-Infective Agents / pharmacology*
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Calcium-Calmodulin-Dependent Protein Kinases / metabolism
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Cell Line, Transformed
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Dihydroxyphenylalanine / analogs & derivatives*
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Dihydroxyphenylalanine / isolation & purification
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Dihydroxyphenylalanine / pharmacology
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Diptera / chemistry*
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Enzyme Inhibitors / isolation & purification
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Enzyme Inhibitors / pharmacology*
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Glutathione / analogs & derivatives*
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Glutathione / isolation & purification
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Glutathione / pharmacology
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Mice
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Phosphorylation
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Protein Kinase C / metabolism
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Protein-Tyrosine Kinases / antagonists & inhibitors*
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Protein-Tyrosine Kinases / metabolism
Substances
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Anti-Infective Agents
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Enzyme Inhibitors
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N-beta-alanyl-5-S-glutathionyl-3,4-dihydroxyphenylalanine
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Dihydroxyphenylalanine
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Protein-Tyrosine Kinases
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Protein Kinase C
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Calcium-Calmodulin-Dependent Protein Kinases
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Glutathione