Expression of prothymosin alpha is correlated with development and progression in human prostate cancers

Suzuki, Shugo; Takahashi, Satoru; Takahashi, Seishiro; Takeshita, Kentaro; Hikosaka, Atsuya; Wakita, Toshiaki; Nakatani, Naoki; Fujita, Tamio; Okamura, Takehiko; Shirai, Tomoyuki

doi:10.1002/pros.20385

Cited by 45 publications

(40 citation statements)

References 21 publications

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“…Cheung's group has shown that expression of a considerable number of genes is directly controlled by cis-or trans-acting elements of the genotype (8-10). Many studies have also demonstrated the correlation between gene expression and treatment effect (11)(12)(13)(14)(15)(16)(17)(18)(19). The present study links genotype to gene expression to cell line treatment response and ultimately identified genetic variants that influence drug-induced cytotoxicity.…”

Section: Discussionmentioning

confidence: 92%

A genome-wide approach to identify genetic variants that contribute to etoposide-induced cytotoxicity

Huang

Duan

Bleibel

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

179

191

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Large interindividual variance has been observed in sensitivity to drugs. To comprehensively decipher the genetic contribution to these variations in drug susceptibility, we present a genome-wide model using human lymphoblastoid cell lines from the International HapMap consortium, of which extensive genotypic information is available, to identify genetic variants that contribute to chemotherapeutic agent-induced cytotoxicity. Our model inte- HapMap ͉ pharmacogenomics ͉ toxicity ͉ whole-genome association

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Section: Discussionmentioning

confidence: 92%

A genome-wide approach to identify genetic variants that contribute to etoposide-induced cytotoxicity

Huang

Duan

Bleibel

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

179

191

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“…In the only article-to our knowledge-reporting on the immunochemical localization of ProTa in prostatic tissue samples, Suzuki et al (2006) studied a large number of normal prostate, benign prostatic hyperplasia, and prostate cancer samples. According to the results of that study, ProTa-like immunoreactivity was observed mainly in the cell nucleus, whereas a weak cytoplasmic staining was also observed; this may be attributed to the antibody the authors used (commercially available monoclonal antibody to ProTa, clone 2F11), which, if identical to the one first described by Sukhacheva et al (2002), recognizes an epitope on the N terminus of the ProTa molecule (aa 1-31) and might, therefore, bind to cytoplasmic Ta1 as well.…”

Section: Discussionmentioning

confidence: 99%

Immunocytological and Preliminary Immunohistochemical Studies of Prothymosin α, a Human Cancer–associated Polypeptide, With a Well-characterized Polyclonal Antibody

Klimentzou

Drougou

Fehrenbacher

et al. 2008

J Histochem Cytochem.

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Prothymosin α (ProTα) is a nuclear polypeptide of great biological and, possibly clinical, importance, because its expression levels have been associated with early diagnosis/prognosis of human cancer. It is therefore interesting to raise easily available and cost-effective antibodies that would be applied to develop reliable ProTα immunodiagnostics. In this study, New Zealand white rabbits and laying hens were parallel immunized against intact ProTα or the synthetic fragments ProTα[1-28], ProTα[87-109], and ProTα[101-109], all conjugated to keyhole limpet hemocyanin (KLH). The corresponding antibodies G and Y were immunochemically evaluated in parallel with ELISA and Western blot systems and applied to fluorescence immunocytology experiments using various cancer cell lines and normal cells. The antibody G raised against ProTα[101-109]/KLH had excellent functional characteristics in the Western blot and immunocytology experiments, where the fluorescent signal was almost exclusively shown in the cell nucleus independently of the cells assayed. The above antibody has been applied to preliminary IHC staining of human cancer prostate tissues, leading to a high percentage of clearly and intensively stained nuclei in the adenocarcinoma tissue; this antibody can be further used in cancer tissue immunostaining and in research concerning the role of ProTa in tumorigenesis.

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“…Its presence in the nuclear compartment, also supported by the putative bipartite NLS, is well reported in literature and is associated with several functions (Martini and Katzenellenbogen, 2003;Karapetian et al, 2005;Mosoian et al, 2006), including its correlation with development and progression of prostate cancer (Suzuki et al, 2006). In addition, its involvement in chromatin remodeling, owing to the acidic residues clustered in the central part of the molecule, is also described.…”

Section: Prothymosin a Expression In The Frog Testismentioning

confidence: 91%

Evidence for the involvement of prothymosin α in the spermatogenesis of the frog Rana esculenta

Ferrara¹,

Izzo²,

Liguori³

et al. 2008

J. Exp. Zool.

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Prothymosin alpha (PTMA) is a small acidic protein abundantly and ubiquitously expressed in mammals and involved in different biological activities. Until now, its specific function in spermatogenesis has never been properly investigated. Recently, the isolation of a cDNA encoding for PTMA from the testis of the frog Rana esculenta has been reported: ptma transcript is highly expressed throughout the frog reproductive cycle, peaking in September/October, in concomitance with the germ cell maturation; it is specifically localized in the cytoplasm of primary and secondary spermatocytes and, at a lower level, in the interstitial compartment, in Leydig cells.In this article we support the involvement of PTMA in the meiotic phases of frog spermatogenesis. The expression of ptma mRNA increases in the testis of frogs treated with the antiandrogen cyproterone acetate, which blocks the II meiotic division and induces an increase in SPC cysts; on the contrary, it highly decreases in the testis of animals kept at 4 degrees C and treated with human corionic gonadotropin, in concomitance with the induced block of spermatogenesis and the disappearance of meiotic cells in the tubules. Furthermore, for the first time we have also evidenced by immunohistochemistry the expression of PTMA in the nuclei of secondary spermatocytes, spermatids, and spermatozoa, as well as in the cytoplasm of interstitial Leydig cells. Taken together our data suggest for an important role of PTMA in germ cell maturation and/or differentiation during R. esculenta spermatogenesis.

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Expression of prothymosin alpha is correlated with development and progression in human prostate cancers

Abstract: The present study clearly demonstrated that PTMA expression is intimately involved in the differentiation and progression of human prostate cancers, and could be a target for therapy and diagnostic purposes.

Cited by 45 publications

References 21 publications

A genome-wide approach to identify genetic variants that contribute to etoposide-induced cytotoxicity

A genome-wide approach to identify genetic variants that contribute to etoposide-induced cytotoxicity

Immunocytological and Preliminary Immunohistochemical Studies of Prothymosin α, a Human Cancer–associated Polypeptide, With a Well-characterized Polyclonal Antibody

Evidence for the involvement of prothymosin α in the spermatogenesis of the frog Rana esculenta

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