Opposite effects of unmodified prolactin and a molecular mimic of phosphorylated prolactin on morphology and the expression of prostate specific genes in the normal rat prostate

The Prostate ◽  
2002 ◽  
Vol 54 (1) ◽  
pp. 25-33 ◽  
Author(s):  
Xiaolei Xu ◽  
Wei Wu ◽  
Valencia Williams ◽  
Amy Khong ◽  
Yen-Hao Chen ◽  
...  
Keyword(s):  
Normal Rat ◽  
Rat Prostate ◽  
Phosphorylated Prolactin

Lycopene reduced gene expression of steroid targets and inflammatory markers in normal rat prostate

2004 ◽  
Vol 19 (2) ◽  
pp. 1-24 ◽  
Author(s):  
Angelika Herzog ◽  
Ulrich Siler ◽  
Volker Spitzer ◽  
Nicole Seifert ◽  
Athanasios Denelavas ◽  
...  
Keyword(s):  
Gene Expression ◽  
Inflammatory Markers ◽  
Normal Rat ◽  
Rat Prostate

The development of vascular supply of normal rat prostate during the sexual maturation: An angiographic study

The Prostate ◽  
1992 ◽  
Vol 21 (1) ◽  
pp. 1-14 ◽  
Author(s):  
M. Scolnik ◽  
A. Abramovici ◽  
C. Servadio ◽  
G. Tykochinsky
Keyword(s):  
Sexual Maturation ◽  
Vascular Supply ◽  
Angiographic Study ◽  
Normal Rat ◽  
Rat Prostate

Time Lapse Videomicroscopic Identification of Dunning R-3327 Adenocarcinoma and Normal Rat Prostate Cells

1987 ◽  
Vol 137 (3) ◽  
pp. 544-547 ◽  
Author(s):  
James L. Mohler ◽  
Alan W. Partin ◽  
William B. Isaacs ◽  
Donald S. Coffey
Keyword(s):  
Time Lapse ◽  
Prostate Cells ◽  
Normal Rat ◽  
Rat Prostate

Expression and localization of inhibin/activin subunits and activin receptors in the normal rat prostate

Life Sciences ◽  
1997 ◽  
Vol 60 (6) ◽  
pp. 397-401 ◽  
Author(s):  
Shao-Yao Ying ◽  
Zhong Zhang ◽  
Guo Huang
Keyword(s):  
Normal Rat ◽  
Rat Prostate ◽  
Activin Receptors

THE ACTION OF THE GONADOTROPHINS ON THE RAT PROSTATE IN TISSUE CULTURE

1960 ◽  
Vol XXXIII (IV) ◽  
pp. 545-551 ◽  
Author(s):  
Stig Bengmark ◽  
Barbro Ingemanson ◽  
Bengt Källén
Keyword(s):  
Growth Rate ◽  
Culture Medium ◽  
Female Rats ◽  
Rat Serum ◽  
Male And Female Rats ◽  
Different Seasons ◽  
Normal Rat ◽  
Rat Prostate ◽  
Rates Of Growth

ABSTRACT The growth rate of rat prostatic tissue in vitro has been studied. It is significantly lower in cultures made with serum taken from castrated male and female rats during the first two weeks after castration as compared with the rate in cultures made from normal rat serum. This effect can be compensated for by substitution with testosterone propionate to the male serum donors. Addition of follicle stimulating hormone (FSH) to the culture medium causes a significant reduction of the growth rate. Effective concentrations are 0.01 to 0.1 μg/ml. This effect disappears after inactivation of the FSH solution at 70° for one hour. Higher concentrations of FSH do not produce such an arrest. It is suggested that the growth retarding effect of serum or plasma from castrated animals is due to the increased content of FSH. It is further suggested that this method might be of interest for the quantitative study of circulating gonadotrophins. An example is given in which the rates of growth in plasma from cockerels bled at different seasons of the year are compared.

scholarly journals High Levels of Glutaminase II Pathway Enzymes in Normal and Cancerous Prostate Suggest a Role in ‘Glutamine Addiction’

Biomolecules ◽  
2019 ◽  
Vol 10 (1) ◽  
pp. 2 ◽  
Author(s):  
Thambi Dorai ◽  
Bhuvaneswari Dorai ◽  
John T. Pinto ◽  
Michael Grasso ◽  
Arthur J. L. Cooper
Keyword(s):  
Prostate Cancer ◽  
Cancer Cells ◽  
Tca Cycle ◽  
Salvage Pathway ◽  
Dehydrogenase Reaction ◽  
Mammalian Tissues ◽  
Normal Rat ◽  
Rat Prostate ◽  
New Perspective ◽  
Immunohistochemical Analyses

Many tumors readily convert l-glutamine to α-ketoglutarate. This conversion is almost invariably described as involving deamidation of l-glutamine to l-glutamate followed by a transaminase (or dehydrogenase) reaction. However, mammalian tissues possess another pathway for conversion of l-glutamine to α-ketoglutarate, namely the glutaminase II pathway: l-Glutamine is transaminated to α-ketoglutaramate, which is then deamidated to α-ketoglutarate by ω-amidase. Here we show that glutamine transaminase and ω-amidase specific activities are high in normal rat prostate. Immunohistochemical analyses revealed that glutamine transaminase K (GTK) and ω-amidase are present in normal and cancerous human prostate and that expression of these enzymes increases in parallel with aggressiveness of the cancer cells. Our findings suggest that the glutaminase II pathway is important in providing anaplerotic carbon to the tricarboxylic acid (TCA) cycle, closing the methionine salvage pathway, and in the provision of citrate carbon in normal and cancerous prostate. Finally, our data also suggest that selective inhibitors of GTK and/or ω-amidase may be clinically important for treatment of prostate cancer. In conclusion, the demonstration of a prominent glutaminase II pathway in prostate cancer cells and increased expression of the pathway with increasing aggressiveness of tumor cells provides a new perspective on ‘glutamine addiction’ in cancers.

FUNCTIONAL HETEROGENEITY OF THE THYROID AND POSSIBLE PRESENCE OF IODOTYROSINE-LIKE COMPOUNDS IN NORMAL SERUM

1965 ◽  
Vol 48 (2) ◽  
pp. 199-208 ◽  
Author(s):  
J. D. Wiener
Keyword(s):  
Human Subjects ◽  
Thyroid Tissue ◽  
Normal Serum ◽  
Schematic Model ◽  
Functional Heterogeneity ◽  
Rat Serum ◽  
Iodine Metabolism ◽  
Normal Rat ◽  
Isotope Equilibrium ◽  
Equilibrium Experiment

ABSTRACT After the administration of 131I to normal animals or human subjects, labelled thyroxine and triiodothyronine, but at most traces of labelled iodotyrosines can be detected in the serum. However, several investigators using various methods claim to have found considerable amounts of one or both of these iodotyrosines when assaying the stable (non-radioactive) iodinated compounds in the serum. Considering the available evidence as convincing for the present, an attempt has been made to explain this discrepancy. A schematic model of the thyroidal iodine metabolism is proposed, based on (a) the hypothesis that the iodotyrosines are present in the circulation in a »masked« form (i. e. protected against deiodination), and (b) the known functional heterogeneity of the thyroid tissue. This heterogeneity should be of a qualitative as well as quantitative nature. As the physical decay rate of 131I is short in comparison with the turnover rate of the masked iodotyrosine pool, an isotope equilibrium experiment with rats was carried out, using the long-lived isotope 125I. The results of this experiment, viewed together with those of a similar investigation published by others, seem to lend support to the proposed mechanism. The presence of non-negligible amounts of a diiodotyrosine-like compound in normal rat serum seems fairly well established.

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