Prostate Specific Antigen and Prostatic Acid Phosphatase Immunoreactivity as Prognostic Indicators of Advanced Prostatic Carcinoma

Sakai, Hideki; Minami, Yuzo; Yushita, Yoshiaki; Kanetake, Hiroshi; Saito, Yutaka

doi:10.1016/s0022-5347(17)36285-7

Cited by 32 publications

(17 citation statements)

References 16 publications

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“…Of the remaining proteins identified, PAP may be noted. This protease is of interest because it is used as a marker for prostate cancer [3,18]. In this study we found that the expression level of PAP is decreased approximately twofold in prostatic carcinomas.…”

Section: Resultsmentioning

confidence: 63%

“…Because of the relative lack of clinical symptoms, prostatic neoplasia are often detected at a late stage in tumor development. Important tools in prostate cancer diagnosis are serum markers such as prostate-specific antigen (PSA) and prostatic acid phosphatase (PAP) [2,3]. However, diagnosis based on PSA levels in the range of 4 -20 ng PSA/ml serum does not differentiate neoplasia from hyperplasia [2,4], and when high PSA levels are detected, the tumor often displays extracapsular progression, which means poor prognosis [5].…”

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confidence: 99%

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Identification of proteins in human prostate tumor material by two-dimensional gel electrophoresis and mass spectrometry

Alaiya¹,

Oppermann

Langridge³

et al. 2001

CMLS, Cell. Mol. Life Sci.

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Protein patterns in cells collected from benign prostatic tissues and prostate carcinomas were analyzed using two-dimensional polyacrylamide gel electrophoresis and mass spectrometry. Polypeptide expression was evaluated by computer-assisted image analysis (PDQUEST). Proteins expressed by prostate tumors were identified via in-gel digestion and subsequent matrix-assisted laser desorption/ionization mass spectrometry. In addition to cytoskeletal and mitochondrial proteins, a 40-kDa protein was identified as prostatic acid phosphatase (PAP). PAP expression decreased approximately twofold between benign and malignant tissue. Increased expression of heat shock protein 70 and decreased expression of tropomyosin 1 were also observed in the malignant tissue. The analysis of prostate material by two-dimensional gel electrophoresis and mass spectrometry shows that particular proteins are of interest as markers of disease.

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Section: Resultsmentioning

confidence: 63%

mentioning

confidence: 99%

Identification of proteins in human prostate tumor material by two-dimensional gel electrophoresis and mass spectrometry

Alaiya¹,

Oppermann

Langridge³

et al. 2001

CMLS, Cell. Mol. Life Sci.

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“…Taken together, these results provide a mechanistic explanation for the apparent paradox arising from clinical observations in advanced hormone-refractory prostate cancer that they express functional AR, but are nevertheless androgen independent. In those cells, the expression of cPAcP is decreased, indicating that HER-2 is activated by tyrosine phosphorylation (Loor et al 1981, Pontes et al 1981, Solin et al 1990, Sakai et al 1993, while the HER-2 gene is not amplified (Table 3; Signoretti et al 2000, Osman et al 2001. Furthermore, in prostate cancer specimens, the phosphorylation level of ERK/MAPK is elevated (Gioeli et al 1999, Price et al 1999 with the elevation of serum PSA (Chu & Lin 1998).…”

Section: Cpacp: a Negative Regulator Of Cell Proliferationmentioning

confidence: 99%

Cellular prostatic acid phosphatase: a protein tyrosine phosphatase involved in androgen-independent proliferation of prostate cancer

Veeramani

Yuan

Chen

et al. 2005

Endocr Relat Cancer

107

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Human prostatic acid phosphatase (PAcP) was used as a valuable surrogate marker for monitoring prostate cancer prior to the availability of prostate-specific antigen (PSA). Even though the level of PAcP is increased in the circulation of prostate cancer patients, its intracellular level and activity are greatly diminished in prostate cancer cells. Recent advances in understanding the function of the cellular form of PAcP (cPAcP) have shed some light on its role in prostate carcinogenesis, which may have potential applications for prostate cancer therapy. It is now evident that cPAcP functions as a neutral protein tyrosine phosphatase (PTP) in prostate cancer cells and dephosphorylates HER-2/ErbB-2/Neu (HER-2: human epidermal growth factor receptor-2) at the phosphotyrosine (p-Tyr) residues. Dephosphorylation of HER-2 at its p-Tyr residues results in the down-regulation of its specific activity, which leads to decreases in growth and tumorigenicity of those cancer cells. Conversely, decreased cPAcP expression correlates with hyperphosphorylation of HER-2 at tyrosine residues and activation of downstream extracellular signal-regulated kinase (ERK)/mitogen activated protein kinase (MAPK) signaling, which results in prostate cancer progression as well as androgenindependent growth of prostate cancer cells. These in vitro results on the effect of cPAcP on androgen-independent growth of prostate cancer cells corroborate the clinical findings that cPAcP level is greatly decreased in advanced prostate cancer and provide insights into one of the molecular mechanisms involved in prostate cancer progression. Results from experiments using xenograft animal models further indicate a novel role of cPAcP as a tumor suppressor. Future studies are warranted to clarify the use of cPAcP as a therapeutic agent in human prostate cancer patients.

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“…Shc and ERK/MAPK phosphorylation is clinically significant, because in clinical PCa specimens, cPAcP is decreased (Loor et al, 1981;Pontes et al, 1981;Solin et al, 1990;Sakai et al, 1993;Lin et al, 2001) and p66 Shc protein level and ERK/MAPK phosphorylation are elevated (Gioeli et al, 1999;Price et al, 1999;Lee et al, 2004a). This phenomenon is also similar to the observation in breast cancer cells that increased expression of p66…”

Section: Conversely In P66mentioning

confidence: 99%

Expression of p66Shc protein correlates with proliferation of human prostate cancer cells

et al. 2005

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Prostate Specific Antigen and Prostatic Acid Phosphatase Immunoreactivity as Prognostic Indicators of Advanced Prostatic Carcinoma

Cited by 32 publications

References 16 publications

Identification of proteins in human prostate tumor material by two-dimensional gel electrophoresis and mass spectrometry

Identification of proteins in human prostate tumor material by two-dimensional gel electrophoresis and mass spectrometry

Cellular prostatic acid phosphatase: a protein tyrosine phosphatase involved in androgen-independent proliferation of prostate cancer

Expression of p66Shc protein correlates with proliferation of human prostate cancer cells

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