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Cited by 429Vanadium and Halogenation ChemistryProtein Tyrosine PhosphatasesRedox biology and oxidative stress

The insulinomimetic agents H2O2 and vanadate stimulate protein tyrosine phosphorylation in intact cells.

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Heffetz, D, Bushkin, I, Dror, R, Zick, Y·1990·Journal of Biological Chemistry
DOI 10.1016/s0021-9258(19)39885-0
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Abstract

H2O2 and vanadate are known insulinomimetic agents. Together they induce insulin's bioeffects with a potency which exceeds that seen with insulin, vanadate, or H2O2 alone. Employing Western blotting with anti-P-Tyr antibodies, we have identified in Fao cells at least four proteins (pp180, 150, 114, and 100) whose P-Tyr content is rapidly increased upon treatment of the cells with 3 mM H2O2. Tyrosine phosphorylation of these and additional proteins was markedly potentiated (6-10-fold) when 100 microM sodium orthovanadate was added together with H2O2. The effects of H2O2 and vanadate on protein tyrosine phosphorylation were rapid and specific. The enhanced tyrosine phosphorylation was accompanied by a concomitant inhibition of a cytosolic protein tyrosine phosphatase activity. The latter was inhibited by 50% in 3 mM H2O2-treated cells. The inhibitory effect was augmented in the combined presence of H2O2 and vanadate. Half- and maximal effects of vanadate were obtained at 15 microM and 1 mM, respectively. Vanadate (1 mM) alone, added to the cells, had only a trivial effect on protein tyrosine phosphatase activity. A 45-s challenge with insulin (10(-7) M) of cells pretreated with H2O2 largely mimicked the potentiating effects of vanadate on protein tyrosine phosphorylation but not on protein tyrosine phosphatase activity. Our results suggest the involvement of multiple tyrosine-phosphorylation proteins in mediating the biological effects of H2O2/vanadate. Their enhanced phosphorylation can be attributed at least in part, to the inhibitory effects exerted by H2O2 alone, or in combination with vanadate, on protein tyrosine phosphatase activity. The similarity between proteins phosphorylated in Fao cells in response to H2O2/vanadate or H2O2/insulin, suggests that either treatment stimulates protein tyrosine kinases having similar substrate specificities. The insulin receptor kinase is a likely candidate as its activity is markedly enhanced either by insulin (plus H2O2) or by H2O2/vanadate.

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  • ROS are produced normally during mitochondrial respiration and are essential signal transducers that regulate several cell processes in skeletal muscle, including the insulin pathway.

    “However, these molecules are produced normally during mitochondrial respiration and are essential signal transducers that regulate several cell processes in SkM ([8](#B8)), including the insulin pathway ([64](#B64), [65](#B65)).”

    From Mitochondrial fatty acid oxidation in obesity (2013) · cites this paper as [65]

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Authors
Heffetz, D., Bushkin, I., Dror, R., & Zick, Y.
Affiliations
Weizmann Institute of Science (IL)
ORCID
Zick, Y
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1990-02
Volume
265
Issue
5
Pages
2896-2902
ISSN
0021-9258 (ISSN-L)
DOI
10.1016/s0021-9258(19)39885-0
OpenAlex
W1659855560
Cited by
429
References
45
Citations by year
2026: 2 · 2024: 3 · 2023: 3 · 2022: 2 · 2021: 5 · 2020: 2 · 2019: 1 · 2018: 2 · 2017: 1 · 2016: 4 · 2015: 1 · 2014: 2 · 2013: 6 · 2012: 6
FWCI
22.45
Type
journal article
Language
en
Open access
Licence
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
Topics
  • Physical Sciences › Chemistry › Inorganic Chemistry › Vanadium and Halogenation Chemistry
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
Keywords
hydrogen peroxide, sodium orthovanadate, tyrosine phosphorylation, protein tyrosine phosphatase inhibition, insulin receptor kinase, Fao cells, insulin signaling, tyrosine-phosphorylated proteins
MeSH terms
Animals, Cell Line, Humans, Hydrogen Peroxide, Insulin, Kinetics, Phosphoprotein Phosphatases, Phosphorylation, Protein-Tyrosine Kinases, Tumor Cells, Cultured, Tyrosine, Vanadates, Immunoblotting, Protein Tyrosine Phosphatases, Rats

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