Evidence map›Paper›PMID 11129957›Full record

ArticleMolecular and cellular biochemistry2000

Role of endogenous regucalcin in protein tyrosine phosphatase regulation in the cloned rat hepatoma cells (H4-II-E).

S Inagaki, H Misawa, M Yamaguchi

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Article in Molecular and cellular biochemistry, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 39% of its field
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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3 · Its place in the literature

Who cites it

4 citing papers in PubMed, 20 citations in OpenAlex.

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4 · The record

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5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

S InagakiLaboratory of Endocrinology and Molecular Metabolism, Graduate School of Nutritional Sciences, University of Shizuoka, Japan.
H Misawa
M Yamaguchi
University of Shizuoka · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Regucalcin, a regulatory protein of Ca2+ signaling, is mainly present in liver cells. The role of regucalcin in hepatoma cells, however, has not been clarified. The role of endogenous regucalcin in the regulation of protein tyrosine phosphatase activity in the cloned rat hepatoma cells (H4-II-E) was investigated. Hepatoma cells were cultured for 3 days in a medium containing serum (10% fetal bovine serum). After subconfluency, the cells were used for the assay of protein phosphatase activity toward phosphotyrosine. The expression of regucalcin in hepatoma cells was detected by Western blotting using anti-regucalcin antibody. Protein tyrosine phosphatase activity was exhibited in the cytosol of hepatoma cells. The enzyme activity in the cytosol of hepatoma cells was significantly elevated by the addition of calcium chloride (10(-6)-10(-4) M) in the reaction mixture. This elevation was completely blocked by the addition of trifluoperazine (TFP: 2.5 x 10(-6) M), an antagonist of calmodulin. The addition of regucalcin (10(-7) M) caused a complete inhibition of the calcium (10(-4) M)-increased enzyme activity. The presence of anti-regucalcin monoclonal antibody (25, 50, and 100 ng/ml) in the enzyme reaction mixture produced a significant increase in protein tyrosine phosphatase activity in the cytosols of hepatoma cells and normal liver cells. This increase was completely prevented by regucalcin addition. The effect of antibody (50 ng/ml) in elevating the enzyme activity was partly inhibited by vanadate (10(-4) M). Protein tyrosine phosphatase activity was significantly elevated by the culture with Bay K 8644, a Ca2+-channel agonist. This increase was blocked by TFP addition in the enzyme reaction mixture, and it was enhanced in the presence of anti-regucalcin antibody. The present study demonstrates that regucalcin is expressed in hepatoma cells (H4-II-E), and that the protein may have an inhibitory effect on Ca2+/calmodulin-dependent protein tyrosine phosphatase activity in the cells.

Indexed as

3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl esterAnimalsAntibodies, MonoclonalBlotting, WesternCalciumCalcium-Binding ProteinsCalcium Channel BlockersCalcium ChlorideCarboxylic Ester HydrolasesCarcinoma, HepatocellularClone CellsElectrophoresis, Polyacrylamide GelEnzyme InhibitorsIntracellular Signaling Peptides and ProteinsLiver NeoplasmsMale3-Pyridinecarboxylic acid, 1,4-dihydro-2,6-dimethyl-5-nitro-4-(2-(trifluoromethyl)phenyl)-, Methyl esteralcohol sulfotransferaseAntibodies, MonoclonalCalciumCalcium-Binding ProteinsCalcium Channel BlockersCalcium ChlorideCarboxylic Ester HydrolasesEnzyme InhibitorsIntracellular Signaling Peptides and ProteinsProtein Tyrosine PhosphatasesRgn protein, ratSulfotransferasesVanadates

Identifiers

PMID11129957
OpenAlexW195406790

What OpenQuestion holds

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Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.