mersalyl and Prostatic-Neoplasms

With a technique adapted for needle biopsies from human prostate, androgen receptors have been quantitated in normal, hyperplastic, and carcinomatous samples. An important improvement in the yield of cytosol specific binding sites was obtained when samples were pre-incubated with the mercurial reagent mersalyl, which dissociates endogenously bound hormone receptor complexes, before the binding assay with 3H-methyltrienolone (3H-R1881). Androgen receptors in normal prostate tissue were found to be highest (7.81 +/- 1.12 pmoles/g tissue), and significantly different from hyperplastic prostate (2.02 +/- 0.55 pmoles/g tissue, p less than 0.025), but not from carcinomatous samples (4.47 +/- 0.79 pmoles/g tissue). Mean values for hyperplastic and carcinoma were not statistically distinguishable (p less than 0.1). The clinical response to hormone therapy in 85% of 13 patients with prostatic adenocarcinoma reflected the prostatic androgen receptor content. Orchidectomy followed by estrogen administration for several months leads to a dramatic fall (8-fold) in total androgen receptors in carcinomatous prostate, while estrogen alone did not seem to produce a significant effect. These preliminary data suggest that androgen could directly regulate its binding sites, as demonstrated earlier for other animal target organs.

Topics: Adult; Aged; Androgens; Binding Sites; Humans; Male; Mersalyl; Middle Aged; Orchiectomy; Organomercury Compounds; Prostate; Prostatic Hyperplasia; Prostatic Neoplasms; Receptors, Androgen; Receptors, Estrogen

Topics: Adenocarcinoma; Animals; Biopsy, Needle; Cell Nucleus; Freeze Drying; Humans; Male; Mersalyl; Prostate; Prostatic Hyperplasia; Prostatic Neoplasms; Rats; Receptors, Androgen; Receptors, Steroid