Nuclear Androgen Receptor Content in Biopsy Specimens From Histologically Normal, Hyperplastic, and Cancerous Human Prostatic Tissue

Aubel, O. G. J. M. van; Vries, Joan Bolt-de; Blankenstein, M.A.; Kate, Fiebo J.W. ten; Schröder, Fritz H.

doi:10.1016/s0022-5347(17)47330-7

Cited by 4 publications

(5 citation statements)

References 8 publications

(15 reference statements)

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“…The binding data (Kd and capacity) of the PC-82 androgen receptor are quite comparable to those published for the other human prostatic carcinoma models, such as the in vivo HONDA tumor [17] and the in vitro cell line LNCaP [18,19]. In addition, the data are also comparable to those published for human carcinomas, BPH-tissue, and normal prostate tissues [20,21]. Of the tested androgens R1881 showed the highest affinity for the androgen receptor, but this steroid was not analyzed for growth stimulatory action on the tumor.…”

Section: Discussionsupporting

confidence: 79%

Characterization of androgen receptors in a transplantable human prostatic adenocarcinoma (PC‐82)

et al. 1987

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The transplantable human prostatic adenocarcinoma, PC-82, has been shown to be a suitable model for the study of several aspects of androgen-regulated tumor growth. This tumor contains an androgen receptor, and the purpose of the present investigation was to characterize this androgen receptor with respect to hormone specificity, sedimentation coefficient, dissociation constant, Stokes radius, ionic properties, and molecular mass. Cytosol was prepared from tumor tissues grown in athymic nude mice, which were castrated 10 days before harvesting the tumor. Scatchard plot analysis revealed a binding protein with a Kd of 0.1 nM for R1881 (methyltrienolone) and binding capacity of 120 fmol/mg protein. The receptor showed a high affinity for R1881, testosterone, and 5 alpha-dihydrotestosterone, respectively, whereas no or little affinity was found for progesterone and estradiol. In the presence of 10 mM molybdate the androgen receptor in PC-82 cytosol eluted from an FPLC anion exchange column (Mono Q) at 0.32 M NaCl, which is identical to what has been found for androgen receptors from rat prostate and calf uterine cytosol. Photoaffinity labeling of the [3H]R1881-androgen receptor complex and subsequent analysis on SDS-polyacrylamide gels resulted in a covalently labeled protein with a molecular mass of approximately 50 kD. The androgen receptor of the PC-82 tumor had a sedimentation coefficient of 4S and a Stokes radius of 3.3 nm at high ionic strength (0.4 M NaCl). It is concluded that the PC-82 tumor contains a binding protein with the properties described for androgen receptors present in prostate tissue.

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Section: Discussionsupporting

confidence: 79%

Characterization of androgen receptors in a transplantable human prostatic adenocarcinoma (PC‐82)

et al. 1987

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“…Androgen receptors (AR), although intuitively implicated in prostatic dysfunction, have not yet been definitively involved as evidenced by disagreement concerning their relevance to prostate pathology [17,[20][21][22][23][24]45,46]. The necessity to assay AR within a reproducible framework has been emphasised [47], but achievement of such an ideal is hindered by nonuniform distribution of AR among areas of the same prostate [48], between different prostate tissue types [15][16][17]49301, and possibly among different subnuclear compartments [8,9,50,51].…”

Section: Discussionmentioning

confidence: 99%

Association states of androgen receptors in nuclei of human benign hypertrophic prostate

Kyprianou

Davies

1986

The Prostate

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Androgen receptors (AR) were quantified in nuclei purified from unfractionated benign hypertrophic prostate (bph) tissue and from separated epithelium and stroma from bph specimens. Both epithelial and stromal cell nuclei contained AR, although concentrations in epithelial cell nuclei were higher and more variable. Variations in AR levels in epithelial cell nuclei reflected variations in unfractionated-tissue nuclei. Nuclear AR were further characterized regarding extractability with or resistance to 0.6 mol/lKCl and micrococcal nuclease. Nuclei from unfractionated tissue, epithelium, and stroma contained populations of AR susceptible and refractory to solubilization with KC1 and nuclease. Nuclease- and salt-sensitive populations of AR were similar numerically. The observed variability in epithelial cell nuclear AR was attributable to a wide range of solubilizable AR. Nuclease-digestion profiles and sedimentation analyses revealed that this wide range was not due to AR associated with soluble chromatin oligomers but to AR not detectably associated with other nuclear components. In contrast, AR in stromal cell nuclei was predominantly resistant to KC1 and nuclease, and variability in total nuclear AR concentration was due to variation in the nonextractable population.

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“…Control slides were treated in an identical manner, except that nonspecific mouse antibodies were used as the first step. (43,44). Double-labeling studies.…”

Section: Methodsmentioning

confidence: 99%

Presence of estrogen‐binding sites on macrophage‐like synoviocytes and cd8+, cd29+, cd45ro+ t lymphocytes in normal and rheumatoid synovium

Cutolo

Accardo

Villaggio

et al. 1993

Arthritis & Rheumatism

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Objective. To study the presence of estrogenbinding sites (EBS) in the synovial tissues of male and female patients with rheumatoid arthritis (RA) and in age-and sex-matched healthy controls.Methods. Both type 1 (high affinity, low binding capacity) and type 2 (reduced affinity, higher binding capacity) EBS were investigated in both soluble and nuclear fractions of homogenized synovial tissue sam- ples by a dextran-coated charcoal method. To determine what type of synovial cell was positive for EBS, cryosections of synovial tissues were immunostained with a specific monoclonal anti-estrogen receptor antibody (anti-ER MAb) using both immunofluorescence and immunoperoxidase techniques. Double immunostaining with the anti-ER MAb and with specific MAb to detect different macrophage antigens (Ber-MAC3, MAC387, CD68) and CDS+ T cell subsets (CD29+, CD45RO+ and CD29-, CD45RO-) was performed.Results. Higher affinity EBS were found mostly in nuclear cell fractions of either RA or control synovial tissues (28 of the 33). These EBS were present to a lesser extent in soluble cell fractions (11 of the 33). Immunostaining showed the estrogen receptor-positive cells to be the macrophage-like synoviocytes and the CD8+, CD29+ T cells both in RA and in control synovial tissues. Higher nuclear content of EBS was consistent with more intense nuclear staining of synoviocytes and T cells.Conclusion. It is conceivable that the immunomodulatory activity exerted by estrogens is at least partly mediated through their interaction with EBS that are present on macrophage-like synoviocytes, functioning as antigen-processing and antigen-presenting cells, and on antigen-experienced (memory) CDS+ T lymphocytes (CD29+, CD45RO+).Females have better humoral immune responses and are more susceptible to autoimmune diseases than males. This sex-related dimorphism in immune capabilities is thought to be related to the physiologic effects of the sex hormones on the immune system (1-6). Generally, estrogens have immunostimulatory effects, whereas androgens are immunosup-

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Nuclear Androgen Receptor Content in Biopsy Specimens From Histologically Normal, Hyperplastic, and Cancerous Human Prostatic Tissue

Cited by 4 publications

References 8 publications

Characterization of androgen receptors in a transplantable human prostatic adenocarcinoma (PC‐82)

Characterization of androgen receptors in a transplantable human prostatic adenocarcinoma (PC‐82)

Association states of androgen receptors in nuclei of human benign hypertrophic prostate

Presence of estrogen‐binding sites on macrophage‐like synoviocytes and cd8+, cd29+, cd45ro+ t lymphocytes in normal and rheumatoid synovium

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