Selective inhibition of the insulin-stimulated phosphorylation of the 95,000 dalton subunit of the insulin receptor by TAME or BAEE

Added Nα-p-tosyl-l-arginine methyl ester or Nα-benzoyl-l-arginine ethyl ester inhibited the stimulation by insulin of phosphorylation of the 95,000 dalton subunit of the insulin receptor both in a partially purified insulin receptor fraction from rat adipocytes and in a highly purified insulin recep...

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Veröffentlicht in:Biochemical and biophysical research communications 1984-03, Vol.119 (2), p.465-472
Hauptverfasser: Tamura, Shinri, Schwartz, Charles F.W., Whipple, Judith H., Dubler, Robert E., Fujita-Yamaguchi, Yoko, Larner, Joseph
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container_end_page 472
container_issue 2
container_start_page 465
container_title Biochemical and biophysical research communications
container_volume 119
creator Tamura, Shinri
Schwartz, Charles F.W.
Whipple, Judith H.
Dubler, Robert E.
Fujita-Yamaguchi, Yoko
Larner, Joseph
description Added Nα-p-tosyl-l-arginine methyl ester or Nα-benzoyl-l-arginine ethyl ester inhibited the stimulation by insulin of phosphorylation of the 95,000 dalton subunit of the insulin receptor both in a partially purified insulin receptor fraction from rat adipocytes and in a highly purified insulin receptor preparation from human placenta. N-α-p-tosyl-l-lysine chloromethyl ketone, Nα-p-tosyl-l-lysine methyl ester, or N-acetyl-l-phenylalanine ethyl ester were much less potent, while N-benzoyl-l-alanine methyl ester was without effect. Inhibition of the phosphorylation by the arginine analogues did not require preincubation of the insulin receptor with inhibitors in the presence of insulin prior to phosphorylation. Inhibition by Nα-p-tosyl-l-arginine methyl ester was decreased by preincubation of the receptor fraction with cold ATP and MnCl 2. These results suggest that Nα-p-tosyl-1-arginine methyl ester inhibits an initial ATP and Mn 2+ dependent reaction in insulin-stimulated phosphorylation process.
doi_str_mv 10.1016/S0006-291X(84)80272-7
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N-α-p-tosyl-l-lysine chloromethyl ketone, Nα-p-tosyl-l-lysine methyl ester, or N-acetyl-l-phenylalanine ethyl ester were much less potent, while N-benzoyl-l-alanine methyl ester was without effect. Inhibition of the phosphorylation by the arginine analogues did not require preincubation of the insulin receptor with inhibitors in the presence of insulin prior to phosphorylation. Inhibition by Nα-p-tosyl-l-arginine methyl ester was decreased by preincubation of the receptor fraction with cold ATP and MnCl 2. 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N-α-p-tosyl-l-lysine chloromethyl ketone, Nα-p-tosyl-l-lysine methyl ester, or N-acetyl-l-phenylalanine ethyl ester were much less potent, while N-benzoyl-l-alanine methyl ester was without effect. Inhibition of the phosphorylation by the arginine analogues did not require preincubation of the insulin receptor with inhibitors in the presence of insulin prior to phosphorylation. Inhibition by Nα-p-tosyl-l-arginine methyl ester was decreased by preincubation of the receptor fraction with cold ATP and MnCl 2. 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subjects adipocytes
Adipose Tissue - metabolism
Animals
arginine
Arginine - analogs & derivatives
Arginine - pharmacology
insulin
Insulin - pharmacology
Macromolecular Substances
Male
man
Molecular Weight
Phosphorylation
placenta
Rats
Rats, Inbred Strains
Receptor, Insulin - drug effects
Receptor, Insulin - metabolism
Tosylarginine Methyl Ester - pharmacology
title Selective inhibition of the insulin-stimulated phosphorylation of the 95,000 dalton subunit of the insulin receptor by TAME or BAEE
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