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Phosphorylation of prostatic nuclear matrix proteins is under androgenic control
Archives of Biochemistry and Biophysics
|November 1, 1984
Summary
Androgen deprivation significantly reduces the rate of nuclear protein phosphorylation in rats, impacting nuclear matrix proteins. This suggests androgenic control over protein kinase activity crucial for initial androgen action.
Area of Science:
- Molecular Biology
- Cell Biology
- Endocrinology
Background:
- Nuclear phosphoproteins play a role in cellular regulation.
- The nuclear matrix is involved in organizing nuclear functions.
- Androgen receptors are critical for male sexual development and function.
Purpose of the Study:
- To investigate the effect of androgen deprivation on nuclear phosphoprotein phosphorylation.
- To determine if protein kinase activity associated with the nuclear matrix is under androgenic control.
Main Methods:
- Isolation of nuclear matrix fraction from rat ventral prostatic nuclei.
- Labeling of nuclear phosphoproteins using [gamma-32P]ATP.
- Analysis of protein phosphorylation rates before and after androgen deprivation.
Main Results:
- A significant portion of radioactivity was found in nuclear matrix phosphoproteins.
- Androgen deprivation markedly reduced the rate, but not the extent, of nuclear protein phosphorylation.
- Nuclear matrix proteins showed a profound reduction in 32P incorporation after androgen deprivation.
Conclusions:
- The cAMP-independent protein kinase activity phosphorylating nuclear matrix proteins is androgenically controlled.
- This androgenic control may be relevant to initial events in androgen action within the nuclear matrix.