Modification of glucose-6-phosphate dehydrogenase by 4-hydroxy-2-nonenal

Formation of cross-linked protein that inhibits the multicatalytic protease

Bertrand Friguet, Earl R. Stadtman, Luke I. Szweda

Research output: Contribution to journalArticle

300 Citations (Scopus)

Abstract

Incubation of glucose-6-phosphate dehydrogenase (Glu-6-PDH) from Leuconostoc mesenteroides with the lipid peroxidation product 4-hydroxy-2-nonenal leads to the formation of cross-linked protein. This is accompanied by the appearance of protein-associated fluorescence with excitation and emission maxima of 340 and 415 nm, respectively, and with the disappearance of histidine and lysine residues. Cross-linked protein is less susceptible than native Glu-6-PDH to proteolysis by the multicatalytic protease, a multienzymic proteolytic complex involved in the intracellular degradation of damaged proteins. In addition, 4-hydroxy-2-nonenal-modified Glu-6-PDH inhibits the multicatalytic protease and can therefore prevent the efficient degradation of oxidized protein. These findings may have important implications for the accumulation of altered protein and fluorescent material in vivo, processes that are believed to be involved in age- and disease-related impairment of cellular function.

Original languageEnglish (US)
Pages (from-to)21639-21643
Number of pages5
JournalJournal of Biological Chemistry
Volume269
Issue number34
StatePublished - Aug 26 1994

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Glucosephosphate Dehydrogenase
Peptide Hydrolases
Proteolysis
Proteins
Histidine
Lipid Peroxidation
Lysine
Degradation
Fluorescence
4-hydroxy-2-nonenal
Lipids

ASJC Scopus subject areas

  • Biochemistry

Cite this

Modification of glucose-6-phosphate dehydrogenase by 4-hydroxy-2-nonenal : Formation of cross-linked protein that inhibits the multicatalytic protease. / Friguet, Bertrand; Stadtman, Earl R.; Szweda, Luke I.

In: Journal of Biological Chemistry, Vol. 269, No. 34, 26.08.1994, p. 21639-21643.

Research output: Contribution to journalArticle

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