Characterization of a Prostate-specific Tyrosine Phosphatase by Mutagenesis and Expression in Human Prostate Cancer Cells

Zhang, Xiu Qing; Lee, Ming Shyue; Zelivianski, Stanislav; Lin, Ming‐Fong

doi:10.1074/jbc.m006661200

Cited by 39 publications

(46 citation statements)

References 57 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Furthermore, point mutations are found in PAcP mRNA isolated from cancerous tissues, although the biological significance remains to be clarified (Vihko et al, 1988). Several lines of evidence support the notion that cPAcP functions as a neutral PTPase in prostate epithelial cells Clinton, 1986, 1988;Vihko et al, 1993;Landry et al, 1996) and downregulates cell growth by dephosphorylating phosphotyrosine (p-Tyr) of ErbB-2 protein (Lin et al, 1994;Lin and Meng, 1996;Meng and Lin, 1998;Zhang et al, 2001). It is further proposed that the interaction of cPAcP and ErbB-2 is involved in regulating androgen stimulation of human prostate cancer cell proliferation Meng et al, 2000).…”

Section: Introductionmentioning

confidence: 97%

Tyrosine-317 of p52Shc mediates androgen-stimulated proliferation signals in human prostate cancer cells

2004

Self Cite

View full text Add to dashboard Cite

Section: Introductionmentioning

confidence: 97%

Tyrosine-317 of p52Shc mediates androgen-stimulated proliferation signals in human prostate cancer cells

2004

Self Cite

View full text Add to dashboard Cite

“…PAcP is classically categorized as a histidine-AcP because it uses a histidyl residue as the phosphate acceptor during the hydrolysis of small organic compounds (Van Etten 1982, Ostanin et al 1994, Zhang et al 2001. Results of several studies indicate that cPAcP exhibits protein tyrosine phosphatase (PTP) activity.…”

Section: Cpacp: a Neutral Histidine-dependent Protein Phosphatase In mentioning

confidence: 99%

“…Dotted lines indicate the active reaction between the p-Tyr moiety and specific amino acid residues of cPAcP. significant (detectable) AcP or PTP activities, whereas the C183A and C281A mutants essentially retained both activities completely (Zhang et al 2001). It should be noted that Asp 258 is conserved in the PTP family (Ostanin et al 1994).…”

Section: Structural Analysis Of Cpacpmentioning

confidence: 99%

“…Histidine (H12) and aspartate (D258) residues have been shown to be critical for the tyrosine dephosphorylation reaction by PAcP. His 12 serves as the phosphate acceptor and Asp 258 serves as the proton donor for the hydrolysis and release of the phosphate moiety from the enzyme , Ostanin et al 1994, Zhang et al 2001. Molecules depicted in red represent the phosphotyrosine residue in HER-2 protein.…”

Section: Structural Analysis Of Cpacpmentioning

confidence: 99%

See 1 more Smart Citation

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

Self Cite

107

View full text Add to dashboard Cite

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.

show abstract

“…Increased activation of MAPKs by growth factors such as EGF, transforming growth factor (TGF)-·, IGF-I/II, basic fibroblast growth factor or oncogenes (e.g. Her2/NEU) (18) correlates with higher Gleason score and tumor progression in vivo (19). Bakin and coworkers (20) have demonstrated a crucial role of chronic activation of MAPK signaling in the progression of LNCaP tumors by promoting hypersensitivity to sub-physiological androgen levels.…”

Section: Introductionmentioning

confidence: 99%

Akacid-medical-formulation, a novel biocidal oligoguanidine with antitumor activity reduces S-phase in prostate cancer cell lines through the Erk 1/2 mitogen-activated protein kinase pathway

Neuwirt

Müller²,

Cavarretta³

et al. 2006

Int J Oncol

View full text Add to dashboard Cite

Abstract. Oligomeric guanidines are highly efficient biocides against a broad spectrum of microorganisms. However, their antitumor effects have not been studied so far. We investigated an antiproliferative effect of Akacid-medical-formulation (AMF), a member of the oligoguanidine family of biocides, against solid cancer cell lines and primary cells by measuring [3 H]-thymidine incorporation. Additionally, we examined cell cycle distribution in two AMF-sensitive prostate cancer cell lines (DU-145, LNCaP) using flow cytometry. Finally, the influence of AMF on cell cycle regulatory molecules and intracellular kinase cascade-related signaling molecules was assessed. We found that AMF has variable antiproliferative effects on all tested cells. In DU-145 and LNCaP cells, flow cytometric studies showed a reduction of S-phase with a maximum extent of 24 and 58%, respectively. This was associated with a decrease in expression of cyclin D1, cyclindependent kinases 2 and 4, while having varying effects on expression of cyclin E and p27. Additionally, reduced phosphorylation of Erk1 and Erk2 was found, whereas expression of phospho-Akt1 remained unchanged. Herein we report for the first time that AMF exerts potent antiproliferative activity against various malignant cell lines, including those of prostate. We therefore recommend further investigation of the anticancer activity of this biocidal oliguanidine.

show abstract

Characterization of a Prostate-specific Tyrosine Phosphatase by Mutagenesis and Expression in Human Prostate Cancer Cells

Cited by 39 publications

References 57 publications

Tyrosine-317 of p52Shc mediates androgen-stimulated proliferation signals in human prostate cancer cells

Tyrosine-317 of p52Shc mediates androgen-stimulated proliferation signals in human prostate cancer cells

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

Akacid-medical-formulation, a novel biocidal oligoguanidine with antitumor activity reduces S-phase in prostate cancer cell lines through the Erk 1/2 mitogen-activated protein kinase pathway

Contact Info

Product

Resources

About