Control of placental alkaline phosphatase gene expression in HeLa cells: induction of synthesis by prednisolone and sodium butyrate

Biochemistry ◽  
1987 ◽  
Vol 26 (12) ◽  
pp. 3596-3602 ◽  
Author(s):  
Janice Yang Chou ◽  
Shori Takahashi
Keyword(s):  
Gene Expression ◽  
Alkaline Phosphatase ◽  
Sodium Butyrate ◽  
Hela Cells ◽  
Placental Alkaline Phosphatase

Induction of alkaline phosphatase activity in HeLa cells by sodium butyrate

In Vitro ◽  
1979 ◽  
Vol 15 (11) ◽  
pp. 861-864 ◽  
Author(s):  
Walker Wharton ◽  
Cathryn A. Hart ◽  
Barry Goz
Keyword(s):  
Alkaline Phosphatase ◽  
Phosphatase Activity ◽  
Alkaline Phosphatase Activity ◽  
Sodium Butyrate ◽  
Hela Cells

Independent regulation by sodium butyrate of gonadotropin alpha gene expression and cell cycle progression in HeLa cells

1984 ◽  
Vol 4 (5) ◽  
pp. 829-839
Author(s):  
R B Darnell
Keyword(s):  
Gene Expression ◽  
Cell Cycle ◽  
Sodium Butyrate ◽  
Hela Cells ◽  
Cell Cycle Progression ◽  
Direct Action ◽  
Cell Types ◽  
Neoplastic Cell ◽  
Alpha Subunit ◽  
Alpha Gene

Sodium butyrate alters the growth and gene expression of a variety of differentiating and neoplastic cell types. For example, addition of 5 mM butyrate to HeLa cells is reported to both induce gonadotropin alpha subunit biosynthesis and block cell cycling in G1. We have studied these two actions of butyrate on HeLa cells and found that they are regulated in distinct ways. The induction of alpha subunit synthesis was due to an increase in the rate of transcription of the alpha gene. Using synchronized populations of HeLa cells, we determined that butyrate stimulates alpha transcription throughout the cell cycle. In contrast, treated cells arrest in G1 only if exposed to butyrate for a discrete period during the previous S phase. We conclude that butyrate inhibits DNA synthesis through a cell cycle-specific action that is independent from its direct action to stimulate transcription of the gonadotropin alpha gene.

scholarly journals Alkaline phosphatase protein increases in response to prednisolone in HeLa cells

1981 ◽  
Vol 200 (2) ◽  
pp. 461-464 ◽  
Author(s):  
W C Hanford ◽  
R H Kottel ◽  
W H Fishman
Keyword(s):  
Alkaline Phosphatase ◽  
Hela Cells ◽  
Specific Protein ◽  
Active State ◽  
Placental Alkaline Phosphatase ◽  
Prednisolone Treatment ◽  
Presence And Absence ◽  
Alkaline Phosphatase Isoenzyme

Quantification of term-placental alkaline phosphatase isoenzyme protein in HeLa TCRC-1 cells grown in the presence and absence of prednisolone indicates that there is a net increase in amount of enzyme-specific protein in prednisolone-stimulated cells. In a similar analysis of HeLa D98AH2 cells, prednisolone treatment causes the appearance of term-placental alkaline phosphatase protein and the loss of the intestinal isoenzyme protein. These results support the interpretation that the response of these cells to corticosteroids is the net accumulation of alkaline phosphatase protein rather than the modification of pre-existing enzyme to a more active state.

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