Nitroprusside stimulates the cysteine-specific mono(ADP-ribosylation) of glyceraldehyde-3-phosphate dehydrogenase from human erythrocytes

Alexander Ya Kots, Alexander Skurat, Edward A. Sergienko, Tamara V. Bulargina, Eugene S. Severin

Research output: Contribution to journalArticle

81 Citations (Scopus)

Abstract

In human erythrocyte membranes incubated with [adenylate-32P]NAD the 36 kDa protein is predominantly labeled. The labeling is greatly stimulated by nitroprusside in the presence of dithiothreitol. We have purified the 36 k Da protein and identified this modification as crysteine-specific mono(ADP-ribosylation) because: (i) labeling occured only when [32P]NAD was replaced by adenine [U-14C]NAD, but not by [carbonyl-14C]NAD; (ii) treatment of the prelabeled protein with snake venom phosphodiesterase led to releasing 5′-[32P]AMP; (iii) the bond between the protein and the nucleotide was hydrolyzed by HgCl2, but was resistant to hydroxylamine. The 36 kDa protein reacted on Western blots with two different monoclonal antibodies (MAbs) against glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and was immunoprecipitated by both MAbs.

Original languageEnglish (US)
Pages (from-to)9-12
Number of pages4
JournalFEBS Letters
Volume300
Issue number1
DOIs
StatePublished - Mar 23 1992
Externally publishedYes

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Glyceraldehyde-3-Phosphate Dehydrogenases
Nitroprusside
Adenosine Diphosphate
Cysteine
Erythrocytes
NAD
Proteins
Labeling
Monoclonal Antibodies
Mercuric Chloride
Hydroxylamine
Dithiothreitol
Erythrocyte Membrane
Adenine
Adenosine Monophosphate
Nucleotides
Western Blotting
Membranes

Keywords

  • ADP-ribosylation
  • Glyceraldehyde-3-phosphate dehydrogenase
  • Human erythrocyte
  • Sodium nitroprusside

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Nitroprusside stimulates the cysteine-specific mono(ADP-ribosylation) of glyceraldehyde-3-phosphate dehydrogenase from human erythrocytes. / Kots, Alexander Ya; Skurat, Alexander; Sergienko, Edward A.; Bulargina, Tamara V.; Severin, Eugene S.

In: FEBS Letters, Vol. 300, No. 1, 23.03.1992, p. 9-12.

Research output: Contribution to journalArticle

Kots, Alexander Ya ; Skurat, Alexander ; Sergienko, Edward A. ; Bulargina, Tamara V. ; Severin, Eugene S. / Nitroprusside stimulates the cysteine-specific mono(ADP-ribosylation) of glyceraldehyde-3-phosphate dehydrogenase from human erythrocytes. In: FEBS Letters. 1992 ; Vol. 300, No. 1. pp. 9-12.
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AU - Severin, Eugene S.

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N2 - In human erythrocyte membranes incubated with [adenylate-32P]NAD the 36 kDa protein is predominantly labeled. The labeling is greatly stimulated by nitroprusside in the presence of dithiothreitol. We have purified the 36 k Da protein and identified this modification as crysteine-specific mono(ADP-ribosylation) because: (i) labeling occured only when [32P]NAD was replaced by adenine [U-14C]NAD, but not by [carbonyl-14C]NAD; (ii) treatment of the prelabeled protein with snake venom phosphodiesterase led to releasing 5′-[32P]AMP; (iii) the bond between the protein and the nucleotide was hydrolyzed by HgCl2, but was resistant to hydroxylamine. The 36 kDa protein reacted on Western blots with two different monoclonal antibodies (MAbs) against glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and was immunoprecipitated by both MAbs.

AB - In human erythrocyte membranes incubated with [adenylate-32P]NAD the 36 kDa protein is predominantly labeled. The labeling is greatly stimulated by nitroprusside in the presence of dithiothreitol. We have purified the 36 k Da protein and identified this modification as crysteine-specific mono(ADP-ribosylation) because: (i) labeling occured only when [32P]NAD was replaced by adenine [U-14C]NAD, but not by [carbonyl-14C]NAD; (ii) treatment of the prelabeled protein with snake venom phosphodiesterase led to releasing 5′-[32P]AMP; (iii) the bond between the protein and the nucleotide was hydrolyzed by HgCl2, but was resistant to hydroxylamine. The 36 kDa protein reacted on Western blots with two different monoclonal antibodies (MAbs) against glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and was immunoprecipitated by both MAbs.

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