Differential effects of sodium butyrate and hyperosmolality on the modulation of alkaline phosphatases of LoVo cells

Herz, Fritz; Halwer, Murray

doi:10.1016/0014-4827(90)90276-g

Cited by 18 publications

(15 citation statements)

References 14 publications

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“…To test these hypotheses, in vitro protein phosphatase activities have been assayed on HTC cell extracts. Although our data suggested that the implied phosphatase could be either PP1 or PP2A, alkaline and acid phosphatase activities have also been measured because it has been previously described that sodium butyrate could induce alkaline phosphatase activities in a cell line derived from a human colon carcinoma metastasis (50). Both activities have been determined using classical methods, as described under "Materials and Methods."…”

Section: Resultsmentioning

confidence: 99%

The Effects of Sodium Butyrate on Transcription Are Mediated through Activation of a Protein Phosphatase

Cuisset¹,

Tichonicky²,

Jaffray³

et al. 1997

Journal of Biological Chemistry

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In this study we have investigated the molecular mechanism by which sodium butyrate modulates gene expression when added to cultured cells. As a model system we used hepatoma tissue culture cells in which sodium butyrate treatment increases histone H1°mRNA level and decreases c-myc mRNA level. Because we observed that stimulation of histone H1°gene expression could take place in the absence of protein neosynthesis, we hypothesized that sodium butyrate induced a posttranslational modification of a factor involved in the transcription process. Using different types of well known kinase and phosphatase inhibitors, we studied the implication of kinase or phosphatase activity in this pathway. Interestingly, cell treatment with potent serine-threonine-phosphatase inhibitors, calyculin A or okadaic acid, prevented the regulation of both histone H1°and c-myc gene expressions by sodium butyrate. On the other hand, the tyrosine phosphatase inhibitor, vanadate, or the protein kinase C inhibitor, staurosporine, did not significantly modify sodium butyrate effects. Using protein phosphatase 1 and 2A for in vitro assays, we found a 45% increase of phosphatase activity after cell treatment by sodium butyrate, possibly due to a protein phosphatase 1-type protein phosphatase. These data strongly suggest that signaling pathway(s) triggered by sodium butyrate to modulate gene expression involve(s) a serine-threonine-phosphatase activity.

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Section: Resultsmentioning

confidence: 99%

The Effects of Sodium Butyrate on Transcription Are Mediated through Activation of a Protein Phosphatase

Cuisset¹,

Tichonicky²,

Jaffray³

et al. 1997

Journal of Biological Chemistry

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“…ALP activity was measured in a dynamics assay using a Screen Master 3000 Semi-automatic Biochemistry Analyser (Hospitex Diagnostics, Firenze, Italy). The relative enzyme activity was expressed as ALP/ total protein (U/g) 11,12 . Six wells of a 12-well plate were used for each dose and timed treatment.…”

Section: Dna Fragmentationmentioning

confidence: 99%

Inhibition of growth and increase of alkaline phosphatase activity in cultured human oral cancer cells by all-trans retinoic acid

Xiao

Guo

Lou

et al. 2006

International Journal of Oral and Maxillofacial Surgery

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“…Finally, the ALP activities were measured by dynamics assay with a Screen Master 3000 semiautomatic biochemistry analyzer (Hospitex Diagnostics, Florence, Italy). The relative enzyme activity was expressed as U/g [17,18] . Six wells of a 12-well plate were used for each dose and treatment time.…”

Section: Determination Of Relative Alp Activitiesmentioning

confidence: 99%

Anticancer effect of aloe-emodin on cervical cancer cells involves G₂/M arrest and induction of differentiation

Guo

Xiao

Liu

et al. 2007

Acta Pharmacologica Sinica

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Aim: The aim of this study was to investigate the effects of aloe-emodin, a natural compound from the root and rhizome of Rheum palmatum, on the growth of human cervical cancer cells, HeLa. Methods: HeLa cells were treated with various concentrations of aloe-emodin for 1-5 d, and cell growth was measured by 3-(4, 5-dimethylthiazol-2-yl)-2, 5-diphenyl tetrazolium bromide assay. The long-term growth effect was investigated by crystal violet assay. The distributions of the cell cycle and apoptosis were analyzed by flow cytometry. The alkaline phosphatase (ALP) activity was analyzed by a chemical analyzer. Finally, Western blotting was used to indicate the abundant changes of protein kinase C (PKC), cmyc, cyclins, cyclin-dependent kinases (CDK), and proliferating cell nuclear antigen (PCNA). Results: Aloe-emodin inhibited the growth of HeLa cells in a dosedependent manner at concentrations ranging between 2.5 and 40 µmol/L. The flow cytometric analysis showed that HeLa cells were arrested at the G 2 /M phase. This effect was associated with the decrease in cyclin A and CDK2, and the increase in cyclin B1 and CDK1. More importantly, the ALP activity was found to be increased by aloe-emodin treatment, and accompanied by the inhibition of PCNA expression. In addition, aloe-emodin suppressed the expression of PKCα and c-myc. Conclusion: These findings provide a possible mechanistic explanation for the growth inhibitory effect of aloe-emodin on HeLa, which includes cell cycle arrest and inducing differentiation.

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Differential effects of sodium butyrate and hyperosmolality on the modulation of alkaline phosphatases of LoVo cells

Cited by 18 publications

References 14 publications

The Effects of Sodium Butyrate on Transcription Are Mediated through Activation of a Protein Phosphatase

The Effects of Sodium Butyrate on Transcription Are Mediated through Activation of a Protein Phosphatase

Inhibition of growth and increase of alkaline phosphatase activity in cultured human oral cancer cells by all-trans retinoic acid

Anticancer effect of aloe-emodin on cervical cancer cells involves G₂/M arrest and induction of differentiation

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Differential effects of sodium butyrate and hyperosmolality on the modulation of alkaline phosphatases of LoVo cells

Cited by 18 publications

References 14 publications

The Effects of Sodium Butyrate on Transcription Are Mediated through Activation of a Protein Phosphatase

The Effects of Sodium Butyrate on Transcription Are Mediated through Activation of a Protein Phosphatase

Inhibition of growth and increase of alkaline phosphatase activity in cultured human oral cancer cells by all-trans retinoic acid

Anticancer effect of aloe-emodin on cervical cancer cells involves G2/M arrest and induction of differentiation

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Anticancer effect of aloe-emodin on cervical cancer cells involves G₂/M arrest and induction of differentiation