scholarly journals Black tea polyphenols inhibit IGF-I-induced signaling through Akt in normal prostate epithelial cells and Du145 prostate carcinoma cells

2002 ◽  
Vol 23 (1) ◽  
pp. 217-221 ◽  
Author(s):  
R. D. Klein
Keyword(s):  
Epithelial Cells ◽  
Prostate Carcinoma ◽  
Black Tea ◽  
Carcinoma Cells ◽  
Tea Polyphenols ◽  
Normal Prostate ◽  
Prostate Epithelial Cells ◽  
Igf I ◽  
Black Tea Polyphenols

scholarly journals Localization of Transforming Growth Factor-β1 and Type II Receptor in Developing Normal Human Prostate and Carcinoma Tissues

1998 ◽  
Vol 46 (3) ◽  
pp. 379-388 ◽  
Author(s):  
Michael J. Gerdes ◽  
Melinda Larsen ◽  
Lauren McBride ◽  
Truong D. Dang ◽  
Bing Lu ◽  
...  
Keyword(s):  
Growth Factor ◽  
Epithelial Cells ◽  
Prostate Carcinoma ◽  
Stromal Cells ◽  
Transforming Growth Factor ◽  
Carcinoma Cells ◽  
Human Prostate ◽  
Type Ii ◽  
Normal Prostate ◽  
Normal Human

Transforming growth factor-β1 (TGF-β1) is implicated in prostate development, and elevated expression of TGF-β1 has been correlated with prostate carcinogenesis. In this study, cell type specificity of TGF-β1 and TGF-β receptor Type II (RcII) protein expression was determined by immunocytochemistry in human normal prostate and compared to prostate carcinoma tissues. Heterogeneous localization patterns of LAP-TGF-β1 (TGF-β1 precursor) and RcII were observed in both epithelial and mesenchymal cells in fetal prostate, with LAP-TGF-β1 localizing to more basal epithelial cells. Homogeneity of LAP-TGF-β1 staining was increased in neonatal, prepubertal, and adult prostate, with elevated immunoreac-tivity noted in epithelial acini relative to stromal tissue for both LAP-TGF-β1 and RcII proteins. In stromal tissues, RcII cell localization exhibited staining patterns nearly identical to smooth muscle α-actin. In prostate carcinoma, LAP-TGF-β1 localized to carcinoma cells with an increased staining heterogeneity relative to normal prostate. In contrast to normal epithelial cells, carcinoma epithelial cells exhibited low to nondetectable RcII staining. Stromal cell staining patterns for LAP-TGF-β1 and RcII in carcinoma, however, were identical to those of normal prostate stromal cells. These studies implicate both epithelial and stromal cells as sites of TGF-β1 synthesis and RcII localization in the developing and adult normal human prostate. In addition, these data indicate a loss of epithelial expression of RcII concurrent with altered LAP-TGF-β1 expression in human prostate carcinoma cells.

scholarly journals Increased expression of type 2 3α-hydroxysteroid dehydrogenase/type 5 17β-hydroxysteroid dehydrogenase (AKR1C3) and its relationship with androgen receptor in prostate carcinoma

2006 ◽  
Vol 13 (1) ◽  
pp. 169-180 ◽  
Author(s):  
K-M Fung ◽  
E N S Samara ◽  
C Wong ◽  
A Metwalli ◽  
R Krlin ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Androgen Receptor ◽  
Epithelial Cells ◽  
Prostate Carcinoma ◽  
Primary Cultures ◽  
Hydroxysteroid Dehydrogenase ◽  
Human Prostate ◽  
Normal Prostate ◽  
Prostate Epithelial Cells

Type 2 3α-hydroxysteroid dehydrogenase (3α-HSD) is a multi-functional enzyme that possesses 3α-, 17β- and 20α-HSD, as well as prostaglandin (PG) F synthase activities and catalyzes androgen, estrogen, progestin and PG metabolism. Type 2 3α-HSD was cloned from human prostate, is a member of the aldo-keto reductase (AKR) superfamily and was named AKR1C3. In androgen target tissues such as the prostate, AKR1C3 catalyzes the conversion of Δ4-androstene-3,17-dione to testosterone, 5α-dihydrotestosterone to 5α-androstane-3α,17β-diol (3α-diol), and 3α-diol to androsterone. Thus AKR1C3 may regulate the balance of androgens and hence trans-activation of the androgen receptor in these tissues. Tissue distribution studies indicate that AKR1C3 transcripts are highly expressed in human prostate. To measure AKR1C3 protein expression and its distribution in the prostate, we raised a monoclonal antibody specifically recognizing AKR1C3. This antibody allowed us to distinguish AKR1C3 from other AKR1C family members in human tissues. Immunoblot analysis showed that this monoclonal antibody binds to one species of protein in primary cultures of prostate epithelial cells and in LNCaP prostate cancer cells. Immunohistochemistry with this antibody on human prostate detected strong nuclear immunoreactivity in normal stromal and smooth muscle cells, perineurial cells, urothelial (transitional) cells, and endothelial cells. Normal prostate epithelial cells were only faintly immunoreactive or negative. Positive immunoreactivity was demonstrated in primary prostatic adenocarcinoma in 9 of 11 cases. Variable increases in immunoreactivity for AKR1C3 was also demonstrated in non-neoplastic changes in the prostate including chronic inflammation, atrophy and urothelial (transitional) cell metaplasia. We conclude that elevated expression of AKR1C3 is highly associated with prostate carcinoma. Although the biological significance of elevated AKR1C3 in prostatic carcinoma is uncertain, AKR1C3 may be responsible for the trophic effects of androgens and/or PGs on prostatic epithelial cells.

Microarray reveals positive effects of green and black tea polyphenols on TNF[alpha]-induced changes of gene expression

2013 ◽  
Author(s):  
Husna Zulkipli ◽  
Norita Salim ◽  
Gabriele Anisah Froemming ◽  
Aletza Mohd Ismail ◽  
Hapizah Nawawi
Keyword(s):  
Gene Expression ◽  
Black Tea ◽  
Tea Polyphenols ◽  
Tnf Alpha ◽  
Positive Effects ◽  
Black Tea Polyphenols ◽  
Green And Black Tea ◽  
Induced Changes

scholarly journals A Network Biology Approach Identifies Molecular Cross-Talk between Normal Prostate Epithelial and Prostate Carcinoma Cells

2016 ◽  
Vol 12 (4) ◽  
pp. e1004884 ◽  
Author(s):  
Victor Trevino ◽  
Alberto Cassese ◽  
Zsuzsanna Nagy ◽  
Xiaodong Zhuang ◽  
John Herbert ◽  
...  
Keyword(s):  
Cross Talk ◽  
Prostate Carcinoma ◽  
Network Biology ◽  
Carcinoma Cells ◽  
Normal Prostate

Nuclear Magnetic Resonance Spectroscopic Based Studies of the Metabolism of Black Tea Polyphenols in Humans

2005 ◽  
Vol 53 (5) ◽  
pp. 1428-1434 ◽  
Author(s):  
Clare A. Daykin ◽  
John P. M. Van Duynhoven ◽  
Anneke Groenewegen ◽  
Markus Dachtler ◽  
Johan M. M. Van Amelsvoort ◽  
...  
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Black Tea ◽  
Tea Polyphenols ◽  
Black Tea Polyphenols ◽  
Nuclear Magnetic

scholarly journals Production Mechanisms of Black Tea Polyphenols

2020 ◽  
Vol 68 (12) ◽  
pp. 1131-1142
Author(s):  
Takashi Tanaka ◽  
Yosuke Matsuo
Keyword(s):  
Black Tea ◽  
Tea Polyphenols ◽  
Black Tea Polyphenols ◽  
Production Mechanisms

scholarly journals Proteolytic cleavage and truncation of NDRG1 in human prostate cancer cells, but not normal prostate epithelial cells

2013 ◽  
Vol 33 (3) ◽  
Author(s):  
Mohammad K. Ghalayini ◽  
Qihan Dong ◽  
Des R. Richardson ◽  
Stephen J. Assinder
Keyword(s):  
Prostate Cancer ◽  
Epithelial Cells ◽  
Western Blot ◽  
Cancer Cells ◽  
Blot Analysis ◽  
Western Blot Analysis ◽  
Metastasis Suppressor ◽  
Normal Prostate ◽  
Truncated Protein ◽  
Prostate Epithelial Cells

NDRG1 (N-myc downstream regulated gene-1) is a metastasis suppressor that is down-regulated in prostate cancer. NDRG1 phosphorylation is associated with inhibition of metastasis and Western blots indicate two bands at ~41 and ~46 kDa. Previous investigations by others suggest the higher band is due to NDRG1 phosphorylation. However, the current study using a dephosphorylation assay and the Phos-tag (phosphate-binding tag) SDS/PAGE assay, demonstrated that the 46 kDa NDRG1 protein band was not due to phosphorylation. Further experiments showed that the NDRG1 protein bands were not affected upon glycosidase treatment, despite marked effects of these enzymes on the glycosylated protein, fetuin. Analysis using RT–PCR (reverse transcriptase–PCR) demonstrated only a single amplicon, and thus, the two bands could not result from an alternatively spliced NDRG1 transcript. Western-blot analysis of prostate cancer cell lysates identified the 41 kDa band to be a truncated form of NDRG1, with MS confirming the full and truncated proteins to be NDRG1. Significantly, this truncated protein was not present in normal human PrECs (prostate epithelial cells). Western-blot analysis using anti-NDRG1 raised to its N-terminal sequence failed to detect the truncated protein, suggesting that it lacked N-terminus amino acids (residues 1–49). Sequence analysis predicted a pseudotrypsin protease cleavage site between Cys49–Gly50. Such cleavage of NDRG1 in cancer cells may result in loss of NDRG1 tumour suppressive activity.

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