Preferential alkaline phosphatase isoenzyme induction by sodium butyrate |
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Authors: | Fritz Herz Murray Halwer |
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Affiliation: | Department of Pathology, Montefiore Medical Center, Albert Einstein College of Medicine, Bronx, NY 10467 U.S.A. |
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Abstract: | SW-620, a continuous cell line derived from a poorly differentiated human colon carcinoma, produces two alkaline phosphatases. Under basal conditions the heat-stable, term-placental is the major isoenzyme and the heat-labile, liver/bone/kidney form represents a minor component. Exposing SW-620 cells to sodium butyrate causes induction of increased levels of activity accompanied by a striking shift in isoenzyme distribution not observed heretofore. The activity increase is accounted for entirely by augmentation of the liver/bone/kidney isoenzyme, with the term-placental form not being affected. Two other known alkaline phosphatase inducers, prednisolone and hyperosmolality, do not influence specific activity and isoenzyme distribution. The preferential induction of the liver/bone/kidney form of alkaline phosphatase in SW-620 cells may reflect a butyrate-elicited expression of a more differentiated state. |
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Keywords: | Alkaline phosphatase isozyme Sodium butyrate Enzyme induction (SW-620 cell) |
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