Poster - Thur Eve - 50: Preliminary Evaluation of Ultrasound Treatment of the Human Prostate Gland Using MRI Thermometry In Vivo

2010 ◽  
Vol 37 (7Part2) ◽  
pp. 3896-3896
Author(s):  
S McCormick ◽  
A Boyes ◽  
I Kobelevskiy ◽  
M Burtnyk ◽  
WA N'Djin ◽  
...  
Keyword(s):  
Prostate Gland ◽  
Ultrasound Treatment ◽  
Human Prostate ◽  
Preliminary Evaluation ◽  
Mri Thermometry

Transurethral in-vivo optical properties of the human prostate gland

1996 ◽  
Author(s):  
David A. Levy ◽  
Jon A. Schwartz ◽  
Martin R. Ostermeyer ◽  
Steven L. Jacques ◽  
Andrew C. von Eschenbach
Keyword(s):  
Optical Properties ◽  
Prostate Gland ◽  
Human Prostate

CHARACTERIZATION OF THE SPECIFIC ANDROGEN RECEPTORS IN THE HUMAN PROSTATE GLAND

1973 ◽  
Vol 57 (3) ◽  
pp. 371-384 ◽  
Author(s):  
W. I. P. MAINWARING ◽  
E. J. G. MILROY
Keyword(s):  
Binding Proteins ◽  
Androgen Receptors ◽  
Gradient Centrifugation ◽  
Prostate Gland ◽  
Sucrose Density Gradient ◽  
Human Prostate ◽  
Sucrose Density Gradient Centrifugation ◽  
Androgen Binding

SUMMARY A search has been conducted for specific androgen-binding proteins in soluble extracts of normal human prostate tissue and in surgical samples removed at retropubic prostatectomy for benign prostatic hyperplasia. Proteins with a particularly high affinity for a metabolite of testosterone, 5α-dihydrotestosterone, have been identified in studies on the binding of 3H-labelled steroids in vitro. The 5α-dihydrotestosterone-protein complexes have been partially characterized using sucrose density gradient centrifugation and gel-exclusion chromatography. The androgen receptors in the human prostate gland are remarkably similar to those previously described in the accessory sexual glands of experimental animals. These findings have been confirmed by the analysis of extracts of hyperplastic prostate glands labelled by the administration of [3H]testosterone in vivo. No attempt was made to correlate the degree of binding with the histological appearance of the specimens of hyperplastic prostate or to determine whether the receptors were principally present in the hyperplastic nodules. Such androgen-binding proteins were not present in serum, skeletal muscle or adipose tissue. The possible relevance of these findings to the onset of clinical disorders in the human prostate gland is briefly discussed.

scholarly journals Androgen dynamics in vitro in the human prostate gland. Effect of cyproterone and cyproterone acetate

1973 ◽  
Vol 132 (3) ◽  
pp. 465-474 ◽  
Author(s):  
Eleonora P. Giorgi ◽  
I. M. Shirley ◽  
J. K. Grant ◽  
Joan C. Stewart
Keyword(s):  
Cell Membrane ◽  
Cyproterone Acetate ◽  
Prostate Gland ◽  
Prostatic Tissue ◽  
Human Prostate ◽  
Specific Mechanism

Hyperplastic and adenocarcinomatous human prostatic tissue was superfused in vitro with radioactively labelled androst-4-ene-3,17-dione, testosterone and 5α-dihydrotestosterone (17β-hydroxy-5α-androstan-3-one), with and without addition of the anti-androgens cyproterone and cyproterone acetate. Cyproterone competitively inhibited the entry of the androgens into the majority of the tissues, whereas cyproterone acetate increased this entry. These findings indicated that transport of androstenedione, testosterone and 5α-dihydrotestosterone into prostatic tissue is performed by a specific mechanism, possibly involving a carrier situated in the cell membrane. The extent of metabolism of the three androgens was also modified: formation of 5α-dihydrotestosterone from testosterone, and of the latter from androstenedione, was decreased by cyproterone and increased by the acetate. Acetate was more effective than cyproterone in decreasing the `uptake' of the perfused androgens by the tissue; at the same time, it increased the androgen clearance from the tissue. As cyproterone acetate is the more potent of the two anti-androgens, the possibility that these findings in vitro are related to the different anti-androgenic potency exhibited by the two compounds in vivo is discussed. `Uptake' of the two anti-androgens and the response to their action on androgen dynamics were similar in adenocarcinomatous and hyperplastic glands.

scholarly journals Androgen dynamics in vitro in the human prostate gland. Effect of oestradiol-17β

1972 ◽  
Vol 126 (1) ◽  
pp. 107-121 ◽  
Author(s):  
E. P. Giorgi ◽  
J. C. Stewart ◽  
J. K. Grant ◽  
I. M. Shirley
Keyword(s):  
Steady State ◽  
Prostate Gland ◽  
Prostatic Tissue ◽  
Human Prostate ◽  
Oestrogen Treatment

Normal, hyperplastic and adenocarcinomatous human prostatic tissue was perfused in vitro with radioactively labelled androstenedione, testosterone and 5α-dihydrotestosterone with and without added oestradiol-17β. Various parameters of tissue–steroid relationship were measured at the steady state. When oestradiol (0.11 or 0.22μmol/l) was added to the perfusing medium, the entry of the steroids into the tissue and their metabolism was increased in the majority of the glands studied. The ‘uptake’ of all the steroids varied, in response to the addition of oestradiol, in both normal and adenocarcinomatous glands in a way differing from the response of hyperplastic glands. As a consequence, the tissue clearance of the steroids, particularly of androstenedione and testosterone, increased in normal and adenocarcinomatous glands in the presence of oestradiol, and decreased in the hyperplastic tissues. At a concentration 0.33μmol/l, oestradiol decreased the entry of the steroids in all the tissues studied, while the clearance of steroids tended to decrease. The significance of these findings in terms of the regulation of androgen dynamics in vivo in the normal and diseased human prostate, with particular regard to the response to oestrogen treatment, is discussed.

The Demonstration of Human Prostatic Acid Phosphatase (Pap) With Phosphorylcholine

1976 ◽  
Vol 34 ◽  
pp. 88-89
Author(s):  
José A. Serrano ◽  
Hannah L. Wasserkrug ◽  
Anna A. Serrano ◽  
Arnold M. Seligman
Keyword(s):  
Acid Phosphatase ◽  
Prostate Gland ◽  
Prostatic Acid Phosphatase ◽  
Human Prostate ◽  
Rat Tissues ◽  
Specific Substrate ◽  
Acid Phosphatases ◽  
Lysosomal Acid ◽  
Cacodylate Buffer

As previously reported (1, 2) phosphorylcholine (PC) is a specific substrate for prostatatic acid phosphatase (PAP) as opposed to other acid phosphatases, e.g., lysosomal acid phosphatase. The specificity of PC for PAP is due to the pentavalent nitrogen in PC, a feature that renders PC resistant to hydrolysis by all other acid phosphatases. Detailed comparative cytochemical results in rat tissues are in press. This report deals with ultracytochemical results applying the method to normal and pathological human prostate gland.Fresh human prostate was obtained from 7 patients having transurethral resections or radical prostatectomies. The tissue was fixed in 3% glutaraldehyde- 0.1 M cacodylate buffer (pH 7.4) for 15 min, sectioned at 50 μm on a Sorvall TC-2 tissue sectioner, refixed for a total of 2 hr, and rinsed overnight in 0.1 M cacodylate buffer (pH 7.4)-7.5% sucrose.

629: Novel Laser Activated Gold Nanoshell Thermal Ablation of Human Prostate Cancer in Vivo

2007 ◽  
Vol 177 (4S) ◽  
pp. 210-211 ◽  
Author(s):  
Joshua M. Stern ◽  
Jennifer Stanfield ◽  
Jer-Tsang Hsieh ◽  
Jeffrey A. Cadeddu
Keyword(s):  
Prostate Cancer ◽  
Thermal Ablation ◽  
Human Prostate ◽  
Human Prostate Cancer ◽  
Gold Nanoshell
Sign in / Sign up

Export Citation Format

Share Document