The overall objective of this project is to understand the biochemical processes of androgen actions in accessory genital organs, especially the rat prostate.
The specific aim of this project has been and will be to purify and characterize: (a) the androgen receptor, (b) the nuclear acceptor protein that promote the receptor interaction with chromatin, (c) alpha-protein, a major secretory protein, and (d) an androgen sensitive specific spermine-binding protein. Alpha-protein and the spermine-binding protein have been purified to homogeneous forms and their partial amino acid sequences have been determined. The roles of some of these proteins in the intracellular regulation of the receptor activity in the prostate will be investigated further.
| Anderegg, R J; Carr, S A; Huang, I Y et al. (1988) Correction of the cDNA-derived protein sequence of prostatic spermine binding protein: pivotal role of tandem mass spectrometry in sequence analysis. Biochemistry 27:4214-21 |
| Chang, C S; Saltzman, A G; Hiipakka, R A et al. (1987) Prostatic spermine-binding protein. Cloning and nucleotide sequence of cDNA, amino acid sequence, and androgenic control of mRNA level. J Biol Chem 262:2826-31 |
| Goueli, S A; Davis, A T; Hiipakka, R A et al. (1985) Polyamine-stimulated phosphorylation of prostatic spermine-binding protein is mediated only by cyclic AMP-independent protein kinases. Biochem J 230:293-302 |
| Liao, S; Witte, D (1985) Autoimmune anti-androgen-receptor antibodies in human serum. Proc Natl Acad Sci U S A 82:8345-8 |
