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Glutathione S-transferases in human prostate.
K D Tew1, M L Clapper, R E Greenberg
1Department of Pharmacology, Fox Chase Cancer Center, Philadelphia, PA 19111.
Biochimica Et Biophysica Acta
|October 8, 1987
Summary
This study analyzed glutathione S-transferase (GST) activity in human prostate tissues, finding four GSTs (Ya, Yb, Yb
Area of Science:
- Biochemistry
- Molecular Biology
- Urology
Background:
- Glutathione S-transferases (GSTs) are crucial enzymes involved in detoxification.
- Understanding GST expression in the human prostate is important for disease research.
Purpose of the Study:
- To characterize glutathione S-transferase activity and isoenzymes in normal and benign prostatic hypertrophy (BPH) tissues.
- To compare GST subunit profiles between normal prostate and BPH.
Main Methods:
- Enzyme activity assays using 1-chloro-2,4-dinitrobenzene (CDNB).
- Purification via glutathione-Sepharose affinity chromatography.
- Analysis using one- and two-dimensional electrophoresis and Western blotting.
Main Results:
- GST activity was quantified in BPH samples (mean 137 +/- 44 nmol/min per mg).
- Purified GST preparations showed at least seven polypeptides (Mr 24,000-28,500, pI neutral to basic).
- Western blot analysis indicated cross-reactivity with five human GST isoenzymes in both normal and BPH tissues.
Conclusions:
- Human prostate expresses at least four GST isoenzymes: Ya, Yb, Yb', and Yf.
- These isoenzymes represent major GST classes (alpha, mu, pi).
- GST profiles are similar, but not identical, between normal prostate and BPH.