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Volumn 1846, Issue 1, 2014, Pages 88-98

Cellular prostatic acid phosphatase, a PTEN-functional homologue in prostate epithelia, functions as a prostate-specific tumor suppressor

Author keywords

CPAcP; ErbB 2; Phosphoinositide phosphatase; Prostate cancer; Protein tyrosine phosphatase; Tumor suppressor

Indexed keywords

ACID PHOSPHATASE PROSTATE ISOENZYME; EPIDERMAL GROWTH FACTOR RECEPTOR 2; HISTONE DEACETYLASE INHIBITOR; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PHOSPHOPROTEIN PHOSPHATASE 2A; PROTEIN KINASE B;

EID: 84905841664     PISSN: 0304419X     EISSN: 18792561     Source Type: Journal    
DOI: 10.1016/j.bbcan.2014.04.006     Document Type: Review
Times cited : (33)

References (154)
  • 3
    • 33750299450 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: from genes, to function, to disease
    • Tonks N.K. Protein tyrosine phosphatases: from genes, to function, to disease. Nat. Rev. Mol. Cell Biol. 2006, 7:833-846.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 833-846
    • Tonks, N.K.1
  • 5
    • 66949135016 scopus 로고    scopus 로고
    • Revisiting histidine-dependent acid phosphatases: a distinct group of tyrosine phosphatases
    • Veeramani S., Lee M.S., Lin M.F. Revisiting histidine-dependent acid phosphatases: a distinct group of tyrosine phosphatases. Trends Biochem. Sci. 2009, 34:273-278.
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 273-278
    • Veeramani, S.1    Lee, M.S.2    Lin, M.F.3
  • 6
    • 0242690301 scopus 로고    scopus 로고
    • Receptor protein tyrosine phosphatase alpha signaling is involved in androgen depletion-induced neuroendocrine differentiation of androgen-sensitive LNCaP human prostate cancer cells
    • Zhang X.Q., Kondrikov D., Yuan T.C., Lin F.F., Hansen J., Lin M.F. Receptor protein tyrosine phosphatase alpha signaling is involved in androgen depletion-induced neuroendocrine differentiation of androgen-sensitive LNCaP human prostate cancer cells. Oncogene 2003, 22:6704-6716.
    • (2003) Oncogene , vol.22 , pp. 6704-6716
    • Zhang, X.Q.1    Kondrikov, D.2    Yuan, T.C.3    Lin, F.F.4    Hansen, J.5    Lin, M.F.6
  • 7
    • 35948929512 scopus 로고    scopus 로고
    • Neuroendocrine-like prostate cancer cells: neuroendocrine transdifferentiation of prostate adenocarcinoma cells
    • Yuan T.C., Veeramani S., Lin M.F. Neuroendocrine-like prostate cancer cells: neuroendocrine transdifferentiation of prostate adenocarcinoma cells. Endocr. Relat. Cancer 2007, 14:531-547.
    • (2007) Endocr. Relat. Cancer , vol.14 , pp. 531-547
    • Yuan, T.C.1    Veeramani, S.2    Lin, M.F.3
  • 9
    • 22144484150 scopus 로고    scopus 로고
    • Androgen deprivation therapy for prostate cancer
    • Sharifi N., Gulley J.L., Dahut W.L. Androgen deprivation therapy for prostate cancer. JAMA 2005, 294:238-244.
    • (2005) JAMA , vol.294 , pp. 238-244
    • Sharifi, N.1    Gulley, J.L.2    Dahut, W.L.3
  • 10
    • 79959194682 scopus 로고    scopus 로고
    • Overcoming chemotherapy resistance in prostate cancer
    • Madan R.A., Pal S.K., Sartor O., Dahut W.L. Overcoming chemotherapy resistance in prostate cancer. Clin. Cancer Res. 2011, 17:3892-3902.
    • (2011) Clin. Cancer Res. , vol.17 , pp. 3892-3902
    • Madan, R.A.1    Pal, S.K.2    Sartor, O.3    Dahut, W.L.4
  • 12
    • 77954946655 scopus 로고    scopus 로고
    • Human prostatic acid phosphatase, an authentic tyrosine phosphatase, dephosphorylates ErbB-2 and regulates prostate cancer cell growth
    • Chuang T.D., Chen S.J., Lin F.F., Veeramani S., Kumar S., Batra S.K., Tu Y., Lin M.F. Human prostatic acid phosphatase, an authentic tyrosine phosphatase, dephosphorylates ErbB-2 and regulates prostate cancer cell growth. J. Biol. Chem. 2010, 285:23598-23606.
    • (2010) J. Biol. Chem. , vol.285 , pp. 23598-23606
    • Chuang, T.D.1    Chen, S.J.2    Lin, F.F.3    Veeramani, S.4    Kumar, S.5    Batra, S.K.6    Tu, Y.7    Lin, M.F.8
  • 17
    • 0025940113 scopus 로고
    • Wild-type p53 suppresses growth of human prostate cancer cells containing mutant p53 alleles
    • 4716-420
    • Isaacs W.B., Carter B.S., Ewing C.M. Wild-type p53 suppresses growth of human prostate cancer cells containing mutant p53 alleles. Cancer Res. 1991, 51:4716-420.
    • (1991) Cancer Res. , vol.51
    • Isaacs, W.B.1    Carter, B.S.2    Ewing, C.M.3
  • 23
    • 0032473921 scopus 로고    scopus 로고
    • Analysis of PTEN and the 10q23 region in primary prostate carcinomas
    • Feilotter H.E., Nagai M.A., Boag A.H., Eng C., Mulligan L.M. Analysis of PTEN and the 10q23 region in primary prostate carcinomas. Oncogene 1998, 16:1743-1748.
    • (1998) Oncogene , vol.16 , pp. 1743-1748
    • Feilotter, H.E.1    Nagai, M.A.2    Boag, A.H.3    Eng, C.4    Mulligan, L.M.5
  • 24
    • 0041914332 scopus 로고    scopus 로고
    • The role of PTEN in the progression and survival of prostate cancer
    • Deocampo N.D., Huang H., Tindall D.J. The role of PTEN in the progression and survival of prostate cancer. Minerva Endocrinol. 2003, 28:145-153.
    • (2003) Minerva Endocrinol. , vol.28 , pp. 145-153
    • Deocampo, N.D.1    Huang, H.2    Tindall, D.J.3
  • 25
    • 30944461586 scopus 로고    scopus 로고
    • PTEN and GSK3beta: key regulators of progression to androgen-independent prostate cancer
    • Mulholland D.J., Dedhar S., Wu H., Nelson C.C. PTEN and GSK3beta: key regulators of progression to androgen-independent prostate cancer. Oncogene 2006, 25:329-337.
    • (2006) Oncogene , vol.25 , pp. 329-337
    • Mulholland, D.J.1    Dedhar, S.2    Wu, H.3    Nelson, C.C.4
  • 30
    • 36849061167 scopus 로고    scopus 로고
    • Genome-wide expression profiling reveals transcriptomic variation and perturbed gene networks in androgen-dependent and androgen-independent prostate cancer cells
    • Singh A.P., Bafna S., Chaudhary K., Venkatraman G., Smith L., Eudy J.D., Johansson S.L., Lin M.F., Batra S.K. Genome-wide expression profiling reveals transcriptomic variation and perturbed gene networks in androgen-dependent and androgen-independent prostate cancer cells. Cancer Lett. 2008, 259:28-38.
    • (2008) Cancer Lett. , vol.259 , pp. 28-38
    • Singh, A.P.1    Bafna, S.2    Chaudhary, K.3    Venkatraman, G.4    Smith, L.5    Eudy, J.D.6    Johansson, S.L.7    Lin, M.F.8    Batra, S.K.9
  • 31
    • 79956052944 scopus 로고    scopus 로고
    • Modulation of protein phosphatase 2A activity alters androgen-independent growth of prostate cancer cells: therapeutic implications
    • Bhardwaj A., Singh S., Srivastava S.K., Honkanen R.E., Reed E., Singh A.P. Modulation of protein phosphatase 2A activity alters androgen-independent growth of prostate cancer cells: therapeutic implications. Mol. Cancer Ther. 2011, 10:720-731.
    • (2011) Mol. Cancer Ther. , vol.10 , pp. 720-731
    • Bhardwaj, A.1    Singh, S.2    Srivastava, S.K.3    Honkanen, R.E.4    Reed, E.5    Singh, A.P.6
  • 32
    • 84879687996 scopus 로고    scopus 로고
    • Impaired expression of protein phosphatase 2A subunits enhances metastatic potential of human prostate cancer cells through activation of AKT pathway
    • Pandey P., Seshacharyulu P., Das S., Rachagani S., Ponnusamy M.P., Yan Y., Johansson S.L., Datta K., Lin M.F., Batra S.K. Impaired expression of protein phosphatase 2A subunits enhances metastatic potential of human prostate cancer cells through activation of AKT pathway. Br. J. Cancer 2013, 108:2590-2600.
    • (2013) Br. J. Cancer , vol.108 , pp. 2590-2600
    • Pandey, P.1    Seshacharyulu, P.2    Das, S.3    Rachagani, S.4    Ponnusamy, M.P.5    Yan, Y.6    Johansson, S.L.7    Datta, K.8    Lin, M.F.9    Batra, S.K.10
  • 33
    • 84878431342 scopus 로고    scopus 로고
    • Phosphatase: PP2A structural importance, regulation and its aberrant expression in cancer
    • Seshacharyulu P., Pandey P., Datta K., Batra S.K. Phosphatase: PP2A structural importance, regulation and its aberrant expression in cancer. Cancer Lett. 2013, 335:9-18.
    • (2013) Cancer Lett. , vol.335 , pp. 9-18
    • Seshacharyulu, P.1    Pandey, P.2    Datta, K.3    Batra, S.K.4
  • 38
    • 0035321378 scopus 로고    scopus 로고
    • The interaction between beta-catenin, GSK3beta and APC after motogen induced cell-cell dissociation, and their involvement in signal transduction pathways in prostate cancer
    • Davies G., Jiang W.G., Mason M.D. The interaction between beta-catenin, GSK3beta and APC after motogen induced cell-cell dissociation, and their involvement in signal transduction pathways in prostate cancer. Int. J. Oncol. 2001, 18:843-847.
    • (2001) Int. J. Oncol. , vol.18 , pp. 843-847
    • Davies, G.1    Jiang, W.G.2    Mason, M.D.3
  • 40
    • 84879968416 scopus 로고    scopus 로고
    • Methylation of APC and GSTP1 in non-neoplastic tissue adjacent to prostate tumour and mortality from prostate cancer
    • Richiardi L., Fiano V., Grasso C., Zugna D., Delsedime L., Gillio-Tos A., Merletti F. Methylation of APC and GSTP1 in non-neoplastic tissue adjacent to prostate tumour and mortality from prostate cancer. PLoS One 2013, 8:e68162.
    • (2013) PLoS One , vol.8
    • Richiardi, L.1    Fiano, V.2    Grasso, C.3    Zugna, D.4    Delsedime, L.5    Gillio-Tos, A.6    Merletti, F.7
  • 42
    • 77953621325 scopus 로고    scopus 로고
    • Candidate gene association studies: successes and failures
    • Pasche B., Yi N. Candidate gene association studies: successes and failures. Curr. Opin. Genet. Dev. 2010, 20:257-261.
    • (2010) Curr. Opin. Genet. Dev. , vol.20 , pp. 257-261
    • Pasche, B.1    Yi, N.2
  • 45
    • 34547843479 scopus 로고    scopus 로고
    • The Wnt/beta-catenin pathway in Wilms tumors and prostate cancers
    • Tycko B., Li C.M., Buttyan R. The Wnt/beta-catenin pathway in Wilms tumors and prostate cancers. Curr. Mol. Med. 2007, 7:479-489.
    • (2007) Curr. Mol. Med. , vol.7 , pp. 479-489
    • Tycko, B.1    Li, C.M.2    Buttyan, R.3
  • 46
    • 0018759696 scopus 로고
    • Human prostatic acid phosphatases: purification of a minor enzyme and comparisons of the enzymes
    • Vihko P. Human prostatic acid phosphatases: purification of a minor enzyme and comparisons of the enzymes. Invest. Urol. 1979, 16:349-352.
    • (1979) Invest. Urol. , vol.16 , pp. 349-352
    • Vihko, P.1
  • 47
    • 0020331699 scopus 로고
    • Human prostatic acid phosphatase: a histidine phosphatase
    • Van Etten R.L. Human prostatic acid phosphatase: a histidine phosphatase. Ann. N. Y. Acad. Sci. 1982, 390:27-51.
    • (1982) Ann. N. Y. Acad. Sci. , vol.390 , pp. 27-51
    • Van Etten, R.L.1
  • 48
    • 0020538393 scopus 로고
    • Purification and characterization of a new human prostatic acid phosphatase isoenzyme
    • Lin M.F., Lee C.L., Li S.S., Chu T.M. Purification and characterization of a new human prostatic acid phosphatase isoenzyme. Biochemistry 1983, 22:1055-1062.
    • (1983) Biochemistry , vol.22 , pp. 1055-1062
    • Lin, M.F.1    Lee, C.L.2    Li, S.S.3    Chu, T.M.4
  • 49
    • 0022977209 scopus 로고
    • Age-related changes in tissue levels of prostatic acid phosphatase and prostate specific antigen
    • Goldfarb D.A., Stein B.S., Shamszadeh M., Petersen R.O. Age-related changes in tissue levels of prostatic acid phosphatase and prostate specific antigen. J. Urol. 1986, 136:1266-1269.
    • (1986) J. Urol. , vol.136 , pp. 1266-1269
    • Goldfarb, D.A.1    Stein, B.S.2    Shamszadeh, M.3    Petersen, R.O.4
  • 50
    • 0016207892 scopus 로고
    • Clinical significance of the human acid phosphatases: a review
    • Yam L.T. Clinical significance of the human acid phosphatases: a review. Am. J. Med. 1974, 56:604-616.
    • (1974) Am. J. Med. , vol.56 , pp. 604-616
    • Yam, L.T.1
  • 51
    • 33646518377 scopus 로고    scopus 로고
    • Tissue-specificity of prostate specific antigens: comparative analysis of transcript levels in prostate and non-prostatic tissues
    • Cunha A.C., Weigle B., Kiessling A., Bachmann M., Rieber E.P. Tissue-specificity of prostate specific antigens: comparative analysis of transcript levels in prostate and non-prostatic tissues. Cancer Lett. 2006, 236:229-238.
    • (2006) Cancer Lett. , vol.236 , pp. 229-238
    • Cunha, A.C.1    Weigle, B.2    Kiessling, A.3    Bachmann, M.4    Rieber, E.P.5
  • 53
    • 78650359938 scopus 로고
    • Significance of increased phosphatase activity at the site of osteoplastic metastases secondary to carcinoma of the prostate gland
    • Gutman E.B., Sproul E.E., Gutman A.B. Significance of increased phosphatase activity at the site of osteoplastic metastases secondary to carcinoma of the prostate gland. Am. J. Cancer 1936, 28:485-495.
    • (1936) Am. J. Cancer , vol.28 , pp. 485-495
    • Gutman, E.B.1    Sproul, E.E.2    Gutman, A.B.3
  • 54
    • 84928580276 scopus 로고
    • Studies on prostatic cancer: the effect of castration, of estrogen and of androgen injection on serum phosphatases in metastatic carcinoma of the prostate
    • Huggins C., Hodges C.V. Studies on prostatic cancer: the effect of castration, of estrogen and of androgen injection on serum phosphatases in metastatic carcinoma of the prostate. Cancer Res. 1941, 1:293-297.
    • (1941) Cancer Res. , vol.1 , pp. 293-297
    • Huggins, C.1    Hodges, C.V.2
  • 55
    • 0018932104 scopus 로고
    • Isolation of prostatic acid phosphatase-binding immunoglobulin G from human sera and its potential for use as a tumor-localizing reagent
    • Papsidero L.D., Wojcieszyn J.W., Horoszewicz J.S., Leong S.S., Murphy G.P., Chu T.M. Isolation of prostatic acid phosphatase-binding immunoglobulin G from human sera and its potential for use as a tumor-localizing reagent. Cancer Res. 1980, 40:3032-3035.
    • (1980) Cancer Res. , vol.40 , pp. 3032-3035
    • Papsidero, L.D.1    Wojcieszyn, J.W.2    Horoszewicz, J.S.3    Leong, S.S.4    Murphy, G.P.5    Chu, T.M.6
  • 57
    • 0031923726 scopus 로고    scopus 로고
    • PSA and acid phosphatase in the diagnosis of prostate cancer
    • Chu T.M., Lin M.F. PSA and acid phosphatase in the diagnosis of prostate cancer. J. Clin. Lig. Assay 1998, 21:24-34.
    • (1998) J. Clin. Lig. Assay , vol.21 , pp. 24-34
    • Chu, T.M.1    Lin, M.F.2
  • 58
    • 0038136985 scopus 로고    scopus 로고
    • Suppression of LNCaP prostate cancer xenograft tumors by a prostate-specific protein tyrosine phosphatase, prostatic acid phosphatase
    • Igawa T., Lin F.F., Rao P., Lin M.F. Suppression of LNCaP prostate cancer xenograft tumors by a prostate-specific protein tyrosine phosphatase, prostatic acid phosphatase. Prostate 2003, 55:247-258.
    • (2003) Prostate , vol.55 , pp. 247-258
    • Igawa, T.1    Lin, F.F.2    Rao, P.3    Lin, M.F.4
  • 60
  • 61
    • 0026764468 scopus 로고
    • Structure of human prostatic acid phosphatase gene
    • Sharief F.S., Li S.S. Structure of human prostatic acid phosphatase gene. Biochem. Biophys. Res. Commun. 1992, 184:1468-1476.
    • (1992) Biochem. Biophys. Res. Commun. , vol.184 , pp. 1468-1476
    • Sharief, F.S.1    Li, S.S.2
  • 62
    • 0023472927 scopus 로고
    • Demonstration of prostatic-type acid phosphatase in non-lysosomal granules in the crypt epithelium of the human duodenum
    • Drenckhahn D., Waheed A., van Etten R. Demonstration of prostatic-type acid phosphatase in non-lysosomal granules in the crypt epithelium of the human duodenum. Histochemistry 1987, 88:47-52.
    • (1987) Histochemistry , vol.88 , pp. 47-52
    • Drenckhahn, D.1    Waheed, A.2    van Etten, R.3
  • 63
    • 0023232942 scopus 로고
    • Structures of the carbohydrate moieties of human prostatic acid phosphatase elucidated by 1H nuclear magnetic resonance spectroscopy
    • Risley M.J., Van Etten R.L. Structures of the carbohydrate moieties of human prostatic acid phosphatase elucidated by 1H nuclear magnetic resonance spectroscopy. Arch. Biochem. Biophys. 1987, 258:404-412.
    • (1987) Arch. Biochem. Biophys. , vol.258 , pp. 404-412
    • Risley, M.J.1    Van Etten, R.L.2
  • 64
    • 0027381611 scopus 로고
    • Evaluation of PAP and PSA gene expression in prostatic hyperplasia and prostatic carcinoma using northern-blot analyses, in situ hybridization and immunohistochemical stainings with monoclonal and bispecific antibodies
    • Hakalahti L., Vihko P., Henttu P., Autio-Harmainen H., Soini Y., Vihko R. Evaluation of PAP and PSA gene expression in prostatic hyperplasia and prostatic carcinoma using northern-blot analyses, in situ hybridization and immunohistochemical stainings with monoclonal and bispecific antibodies. Int. J. Cancer 1993, 55:590-597.
    • (1993) Int. J. Cancer , vol.55 , pp. 590-597
    • Hakalahti, L.1    Vihko, P.2    Henttu, P.3    Autio-Harmainen, H.4    Soini, Y.5    Vihko, R.6
  • 65
    • 0025676484 scopus 로고
    • Is the subunit of prostatic phosphatase active? Reversible denaturation of prostatic acid phosphatase
    • Kuciel R., Bakalova A., Mazurkiewicz A., Bilska A., Ostrowski W. Is the subunit of prostatic phosphatase active? Reversible denaturation of prostatic acid phosphatase. Biochem. Int. 1990, 22:329-334.
    • (1990) Biochem. Int. , vol.22 , pp. 329-334
    • Kuciel, R.1    Bakalova, A.2    Mazurkiewicz, A.3    Bilska, A.4    Ostrowski, W.5
  • 67
    • 0035855198 scopus 로고    scopus 로고
    • Cooperative kinetics of human prostatic acid phosphatase
    • Luchter-Wasylewska E. Cooperative kinetics of human prostatic acid phosphatase. Biochim. Biophys. Acta 2001, 1548:257-264.
    • (2001) Biochim. Biophys. Acta , vol.1548 , pp. 257-264
    • Luchter-Wasylewska, E.1
  • 68
    • 0025915380 scopus 로고
    • Covalent structure, disulfide bonding, and identifi cation of reactive surface and active site residues of human prostatic acid phosphatase
    • Van Etten R.L., Davidson R., Stevis P.E., MacArthur H., Moore D.L. Covalent structure, disulfide bonding, and identifi cation of reactive surface and active site residues of human prostatic acid phosphatase. J. Biol. Chem. 1991, 266:2313-2319.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2313-2319
    • Van Etten, R.L.1    Davidson, R.2    Stevis, P.E.3    MacArthur, H.4    Moore, D.L.5
  • 69
    • 0027201613 scopus 로고
    • Three-dimensional structure of rat acid phosphatase
    • Schneider G., Lindqvist Y., Vihko P. Three-dimensional structure of rat acid phosphatase. EMBO J. 1993, 12:2609-2615.
    • (1993) EMBO J. , vol.12 , pp. 2609-2615
    • Schneider, G.1    Lindqvist, Y.2    Vihko, P.3
  • 70
    • 0028307624 scopus 로고
    • Heterologous expression of human prostatic acid phosphatase and site-directed mutagenesis of the enzyme active site
    • Ostanin K., Saeed A., van Etten R.L. Heterologous expression of human prostatic acid phosphatase and site-directed mutagenesis of the enzyme active site. J. Biol. Chem. 1994, 269:8971-8978.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8971-8978
    • Ostanin, K.1    Saeed, A.2    van Etten, R.L.3
  • 71
    • 0035951769 scopus 로고    scopus 로고
    • Characterization of a prostate-specific tyrosine phosphatase by mutagenesis and expression in human prostate cancer cells
    • Zhang X.Q., Lee M.S., Zelivianski S., Lin M.F. Characterization of a prostate-specific tyrosine phosphatase by mutagenesis and expression in human prostate cancer cells. J. Biol. Chem. 2001, 276:2544-2550.
    • (2001) J. Biol. Chem. , vol.276 , pp. 2544-2550
    • Zhang, X.Q.1    Lee, M.S.2    Zelivianski, S.3    Lin, M.F.4
  • 72
    • 0028128764 scopus 로고
    • Site-directed mutagenesis of prostatic acid phosphatase. Catalytically important aspartic acid 258, substrate specificity, and oligomerization
    • Porvari K.S., Herrala A.M., Kurkela R.M., Taavitsainen P.A., Lindqvist Y., Schneider G., Vihko P.T. Site-directed mutagenesis of prostatic acid phosphatase. Catalytically important aspartic acid 258, substrate specificity, and oligomerization. J. Biol. Chem. 1994, 269:22642-22646.
    • (1994) J. Biol. Chem. , vol.269 , pp. 22642-22646
    • Porvari, K.S.1    Herrala, A.M.2    Kurkela, R.M.3    Taavitsainen, P.A.4    Lindqvist, Y.5    Schneider, G.6    Vihko, P.T.7
  • 73
    • 0037457813 scopus 로고    scopus 로고
    • Crystal structures of human prostatic acid phosphatase in complex with a phosphate ion and alpha-benzylaminobenzylphosphonic acid update the mechanistic picture and offer new insights into inhibitor design
    • Ortlund E., LaCount M.W., Lebioda L. Crystal structures of human prostatic acid phosphatase in complex with a phosphate ion and alpha-benzylaminobenzylphosphonic acid update the mechanistic picture and offer new insights into inhibitor design. Biochemistry 2003, 42:383-389.
    • (2003) Biochemistry , vol.42 , pp. 383-389
    • Ortlund, E.1    LaCount, M.W.2    Lebioda, L.3
  • 74
    • 0021140996 scopus 로고
    • Distribution of prostatic acid phosphatase isoenzymes in normal and cancerous states
    • Lad P.M., Learn D.B., Cooper J.F., Reisinger D.M. Distribution of prostatic acid phosphatase isoenzymes in normal and cancerous states. Clin. Chim. Acta 1984, 141:51-65.
    • (1984) Clin. Chim. Acta , vol.141 , pp. 51-65
    • Lad, P.M.1    Learn, D.B.2    Cooper, J.F.3    Reisinger, D.M.4
  • 76
    • 0019817112 scopus 로고
    • Clomiphene citrate administration to normogonadotropic subfertile men: blood hormone changes and activation of acid phosphatase in seminal fluid
    • Ronnberg L., Vihko P., Sajanti E., Vihko R. Clomiphene citrate administration to normogonadotropic subfertile men: blood hormone changes and activation of acid phosphatase in seminal fluid. Int. J. Androl. 1981, 4:372-378.
    • (1981) Int. J. Androl. , vol.4 , pp. 372-378
    • Ronnberg, L.1    Vihko, P.2    Sajanti, E.3    Vihko, R.4
  • 77
    • 0028224776 scopus 로고
    • The cellular level of prostatic acid phosphatase and the growth of human prostate carcinoma cells
    • Lin M.F., Garcia-Arenas R., Xia X.Z., Biela B., Lin F.F. The cellular level of prostatic acid phosphatase and the growth of human prostate carcinoma cells. Differentiation 1994, 57:143-149.
    • (1994) Differentiation , vol.57 , pp. 143-149
    • Lin, M.F.1    Garcia-Arenas, R.2    Xia, X.Z.3    Biela, B.4    Lin, F.F.5
  • 78
    • 0028213320 scopus 로고
    • Effect of cell density on androgen regulation of the mRNA level of human prostatic acid phosphatase
    • Lin M.F., Garcia-Arenas R. Effect of cell density on androgen regulation of the mRNA level of human prostatic acid phosphatase. Mol. Cell. Endocrinol. 1994, 99:R21-R24.
    • (1994) Mol. Cell. Endocrinol. , vol.99
    • Lin, M.F.1    Garcia-Arenas, R.2
  • 79
    • 0025141718 scopus 로고
    • Gene expression and prostate specificity of human prostatic acid phosphatase (PAP): evaluation by RNA blot analyses
    • Solin T., Kontturi M., Pohlmann R., Vihko P. Gene expression and prostate specificity of human prostatic acid phosphatase (PAP): evaluation by RNA blot analyses. Biochim. Biophys. Acta 1990, 1048:72-77.
    • (1990) Biochim. Biophys. Acta , vol.1048 , pp. 72-77
    • Solin, T.1    Kontturi, M.2    Pohlmann, R.3    Vihko, P.4
  • 80
  • 81
    • 0032489533 scopus 로고    scopus 로고
    • Expression of human prostatic acid phosphatase correlates with androgen-stimulated cell proliferation in prostate cancer cell lines
    • Lin M.F., Meng T.C., Rao P.S., Chang C., Schonthal A.H., Lin F.F. Expression of human prostatic acid phosphatase correlates with androgen-stimulated cell proliferation in prostate cancer cell lines. J. Biol. Chem. 1998, 273:5939-5947.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5939-5947
    • Lin, M.F.1    Meng, T.C.2    Rao, P.S.3    Chang, C.4    Schonthal, A.H.5    Lin, F.F.6
  • 82
    • 0034682240 scopus 로고    scopus 로고
    • Interaction between protein tyrosine phosphatase and protein tyrosine kinase is involved in androgen-promoted growth of human prostate cancer cells
    • Meng T.C., Lee M.S., Lin M.F. Interaction between protein tyrosine phosphatase and protein tyrosine kinase is involved in androgen-promoted growth of human prostate cancer cells. Oncogene 2000, 19:2664-2677.
    • (2000) Oncogene , vol.19 , pp. 2664-2677
    • Meng, T.C.1    Lee, M.S.2    Lin, M.F.3
  • 83
    • 0021846526 scopus 로고
    • Immunocytochemical demonstration of prostatic acid phosphatase: different secretion kinetics between normal, hyperplastic and neoplastic prostates
    • Mori K., Wakasugi C. Immunocytochemical demonstration of prostatic acid phosphatase: different secretion kinetics between normal, hyperplastic and neoplastic prostates. J. Urol. 1985, 133:877-883.
    • (1985) J. Urol. , vol.133 , pp. 877-883
    • Mori, K.1    Wakasugi, C.2
  • 84
    • 0023928123 scopus 로고
    • Three predominant proteins secreted by the human prostate gland
    • Lilja H., Abrahamsson P.A. Three predominant proteins secreted by the human prostate gland. Prostate 1988, 12:29-38.
    • (1988) Prostate , vol.12 , pp. 29-38
    • Lilja, H.1    Abrahamsson, P.A.2
  • 85
    • 0023733710 scopus 로고
    • Relationship of prostatic acid phosphatase localization in human prostate by a monoclonal antibody with the Gleason grading system
    • Sinha A.A., Gleason D.F., Wilson M.J., Wick M.R., Reddy P.K., Blackard C.E. Relationship of prostatic acid phosphatase localization in human prostate by a monoclonal antibody with the Gleason grading system. Prostate 1988, 13:1-15.
    • (1988) Prostate , vol.13 , pp. 1-15
    • Sinha, A.A.1    Gleason, D.F.2    Wilson, M.J.3    Wick, M.R.4    Reddy, P.K.5    Blackard, C.E.6
  • 86
    • 0022263497 scopus 로고
    • Cytochemistry and biochemistry of acid phosphatases V: electrophoretic studies on the heterogeneity of acid phosphatases from human prostate, seminal fluid, and leukocytes
    • Seitz J., Aumüller G. Cytochemistry and biochemistry of acid phosphatases V: electrophoretic studies on the heterogeneity of acid phosphatases from human prostate, seminal fluid, and leukocytes. Prostate 1985, 7:73-90.
    • (1985) Prostate , vol.7 , pp. 73-90
    • Seitz, J.1    Aumüller, G.2
  • 87
    • 0024952404 scopus 로고
    • Improved immunohistochemical detection of prostatic acid phosphatase by a monoclonal antibody
    • Lam K.W., Li C.Y., Yam L.T., Sun T., Lee G., Ziesmer S. Improved immunohistochemical detection of prostatic acid phosphatase by a monoclonal antibody. Prostate 1989, 15:13-21.
    • (1989) Prostate , vol.15 , pp. 13-21
    • Lam, K.W.1    Li, C.Y.2    Yam, L.T.3    Sun, T.4    Lee, G.5    Ziesmer, S.6
  • 89
    • 0026760922 scopus 로고
    • Expression of human prostatic acid phosphatase activity and the growth of prostate carcinoma cells
    • Lin M.F., DaVolio J., Garcia-Arenas R. Expression of human prostatic acid phosphatase activity and the growth of prostate carcinoma cells. Cancer Res. 1992, 52:4600-4607.
    • (1992) Cancer Res. , vol.52 , pp. 4600-4607
    • Lin, M.F.1    DaVolio, J.2    Garcia-Arenas, R.3
  • 90
    • 0036187849 scopus 로고    scopus 로고
    • Establishment and characterization of androgen-independent human prostate cancer LNCaP cell model
    • Igawa T., Lin F.F., Lee M.S., Karan D., Batra S.K., Lin M.F. Establishment and characterization of androgen-independent human prostate cancer LNCaP cell model. Prostate 2002, 50:222-235.
    • (2002) Prostate , vol.50 , pp. 222-235
    • Igawa, T.1    Lin, F.F.2    Lee, M.S.3    Karan, D.4    Batra, S.K.5    Lin, M.F.6
  • 91
    • 36749095145 scopus 로고    scopus 로고
    • ErbB-2 via PYK2 upregulates the adhesive ability of androgen receptor-positive human prostate cancer cells
    • Yuan T.C., Lin F.F., Veeramani S., Chen S.J., Earp H.S., Lin M.F. ErbB-2 via PYK2 upregulates the adhesive ability of androgen receptor-positive human prostate cancer cells. Oncogene 2007, 26:7552-7559.
    • (2007) Oncogene , vol.26 , pp. 7552-7559
    • Yuan, T.C.1    Lin, F.F.2    Veeramani, S.3    Chen, S.J.4    Earp, H.S.5    Lin, M.F.6
  • 92
    • 0027183359 scopus 로고
    • Cationic liposome-mediated incorporation of prostatic acid phosphatase protein into human prostate carcinoma cells
    • Lin M.F., DaVolio J., Garcia R. Cationic liposome-mediated incorporation of prostatic acid phosphatase protein into human prostate carcinoma cells. Biochem. Biophys. Res. Commun. 1993, 192:413-419.
    • (1993) Biochem. Biophys. Res. Commun. , vol.192 , pp. 413-419
    • Lin, M.F.1    DaVolio, J.2    Garcia, R.3
  • 93
    • 0030568824 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of a 185kDa Phosphoprotein (pp 185) inversely correlates with the cellular activity of human prostatic acid phosphatase
    • Lin M.F., Meng T.C. Tyrosine phosphorylation of a 185kDa Phosphoprotein (pp 185) inversely correlates with the cellular activity of human prostatic acid phosphatase. Biochem. Biophys. Res. Commun. 1996, 226:206-213.
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , pp. 206-213
    • Lin, M.F.1    Meng, T.C.2
  • 94
    • 80053130009 scopus 로고    scopus 로고
    • Histone deacetylase inhibitor valproic acid suppresses the growth and increases the androgen responsiveness of prostate cancer cells
    • Chou Y.W., Chaturvedi N.K., Ouyang S., Lin F.F., Kaushik D., Wang J., Kim I., Lin M.F. Histone deacetylase inhibitor valproic acid suppresses the growth and increases the androgen responsiveness of prostate cancer cells. Cancer Lett. 2011, 311:177-186.
    • (2011) Cancer Lett. , vol.311 , pp. 177-186
    • Chou, Y.W.1    Chaturvedi, N.K.2    Ouyang, S.3    Lin, F.F.4    Kaushik, D.5    Wang, J.6    Kim, I.7    Lin, M.F.8
  • 95
    • 0017695545 scopus 로고
    • Isozymes of acid phosphatase in normal and cancerous human prostatic tissue
    • Foti A.G., Herschman H., Cooper J.F. Isozymes of acid phosphatase in normal and cancerous human prostatic tissue. Cancer Res. 1977, 37:4120-4124.
    • (1977) Cancer Res. , vol.37 , pp. 4120-4124
    • Foti, A.G.1    Herschman, H.2    Cooper, J.F.3
  • 96
    • 0019826108 scopus 로고
    • Expression of prostatic acid phosphatase in human prostate cancer
    • Loor R., Wang M.C., Valenzuela L., Chu T.M. Expression of prostatic acid phosphatase in human prostate cancer. Cancer Lett. 1981, 14:63-69.
    • (1981) Cancer Lett. , vol.14 , pp. 63-69
    • Loor, R.1    Wang, M.C.2    Valenzuela, L.3    Chu, T.M.4
  • 97
    • 54849435425 scopus 로고    scopus 로고
    • Androgen-independent prostate cancer cells acquire the complete steroidogenic potential of synthesizing testosterone from cholesterol
    • Dillard P.R., Lin M.F., Khan S.A. Androgen-independent prostate cancer cells acquire the complete steroidogenic potential of synthesizing testosterone from cholesterol. Mol. Cell. Endocrinol. 2008, 295:115-120.
    • (2008) Mol. Cell. Endocrinol. , vol.295 , pp. 115-120
    • Dillard, P.R.1    Lin, M.F.2    Khan, S.A.3
  • 99
    • 3042547296 scopus 로고    scopus 로고
    • Genetically defined mouse models that mimic natural aspects of human prostate cancer development
    • Roy-Burman P., Wu H., Powell W.C., Hagenkord J., Cohen M.B. Genetically defined mouse models that mimic natural aspects of human prostate cancer development. Endocr. Relat. Cancer 2004, 11:225-254.
    • (2004) Endocr. Relat. Cancer , vol.11 , pp. 225-254
    • Roy-Burman, P.1    Wu, H.2    Powell, W.C.3    Hagenkord, J.4    Cohen, M.B.5
  • 100
    • 53049093740 scopus 로고    scopus 로고
    • Prostatic acid phosphatase is an ectonucleotidase and suppresses pain by generating adenosine
    • Zylka M.J., Sowa N.A., Taylor-Blake B., Twomey M.A., Herrala A., Voikar V., Vihko P. Prostatic acid phosphatase is an ectonucleotidase and suppresses pain by generating adenosine. Neuron 2008, 60:111-122.
    • (2008) Neuron , vol.60 , pp. 111-122
    • Zylka, M.J.1    Sowa, N.A.2    Taylor-Blake, B.3    Twomey, M.A.4    Herrala, A.5    Voikar, V.6    Vihko, P.7
  • 102
    • 0020595221 scopus 로고
    • Phosphoprotein phosphatase activity of human prostate acid phosphatase
    • Wasylewska E., Czubak J., Ostrowski W.S. Phosphoprotein phosphatase activity of human prostate acid phosphatase. Acta Biochim. Pol. 1983, 30:175-184.
    • (1983) Acta Biochim. Pol. , vol.30 , pp. 175-184
    • Wasylewska, E.1    Czubak, J.2    Ostrowski, W.S.3
  • 103
    • 0022505776 scopus 로고
    • Human prostatic acid phosphatase has phosphotyrosyl protein phosphatase activity
    • Lin M.F., Clinton G.M. Human prostatic acid phosphatase has phosphotyrosyl protein phosphatase activity. Biochem. J. 1986, 235:351-357.
    • (1986) Biochem. J. , vol.235 , pp. 351-357
    • Lin, M.F.1    Clinton, G.M.2
  • 104
    • 0023893922 scopus 로고
    • Phosphotyrosine phosphatase activity of human and canine acid phosphatases of prostatic origin
    • Chevalier S., Landry D., Chapdelaine A. Phosphotyrosine phosphatase activity of human and canine acid phosphatases of prostatic origin. Prostate 1988, 12:209-219.
    • (1988) Prostate , vol.12 , pp. 209-219
    • Chevalier, S.1    Landry, D.2    Chapdelaine, A.3
  • 105
    • 0000776021 scopus 로고
    • Human prostatic acid phosphatase and its phosphotyrosylprotein phosphatase activity
    • Lin M.F., Clinton G.M. Human prostatic acid phosphatase and its phosphotyrosylprotein phosphatase activity. Adv. Protein Phosphatases 1987, 4:199-228.
    • (1987) Adv. Protein Phosphatases , vol.4 , pp. 199-228
    • Lin, M.F.1    Clinton, G.M.2
  • 106
    • 0023811151 scopus 로고
    • Molecular cloning and sequence analysis of cDNA encoding human prostatic acid phosphatase
    • Vihko P., Virkkunen P., Henttu P., Roiko K., Solin T., Huhtala M.L. Molecular cloning and sequence analysis of cDNA encoding human prostatic acid phosphatase. FEBS Lett. 1988, 236:275-281.
    • (1988) FEBS Lett. , vol.236 , pp. 275-281
    • Vihko, P.1    Virkkunen, P.2    Henttu, P.3    Roiko, K.4    Solin, T.5    Huhtala, M.L.6
  • 107
    • 0025285698 scopus 로고
    • Primary structure of rat secretory acid phosphatase and comparison to other acid phosphatases
    • Roiko K., Janne O.A., Vihko P. Primary structure of rat secretory acid phosphatase and comparison to other acid phosphatases. Gene 1990, 89:223-229.
    • (1990) Gene , vol.89 , pp. 223-229
    • Roiko, K.1    Janne, O.A.2    Vihko, P.3
  • 108
    • 0035413604 scopus 로고    scopus 로고
    • Molecular reactions of protein phosphatases-insights from structure and chemistry
    • Jackson M.D., Denu J.M. Molecular reactions of protein phosphatases-insights from structure and chemistry. Chem. Rev. 2001, 101:2313-2340.
    • (2001) Chem. Rev. , vol.101 , pp. 2313-2340
    • Jackson, M.D.1    Denu, J.M.2
  • 109
    • 0021349470 scopus 로고
    • A phosphotyrosyl-protein phosphatase activity associated with acid phosphatase from human prostate gland
    • Li H.C., Chernoff J., Chen L.B., Kirschonbaum A. A phosphotyrosyl-protein phosphatase activity associated with acid phosphatase from human prostate gland. Eur. J. Biochem. 1984, 138:45-51.
    • (1984) Eur. J. Biochem. , vol.138 , pp. 45-51
    • Li, H.C.1    Chernoff, J.2    Chen, L.B.3    Kirschonbaum, A.4
  • 110
    • 0027395746 scopus 로고
    • Rat acid phosphatase: overexpression of active, secreted enzyme by recombinant baculovirus-infected insect cells, molecular properties, and crystallization
    • Vihko P., Kurkela R., Porvari K., Herrala A., Lindfors A., Lindqvist Y., Schneider G. Rat acid phosphatase: overexpression of active, secreted enzyme by recombinant baculovirus-infected insect cells, molecular properties, and crystallization. Proc. Natl. Acad. Sci. U. S. A. 1993, 90:799-803.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 799-803
    • Vihko, P.1    Kurkela, R.2    Porvari, K.3    Herrala, A.4    Lindfors, A.5    Lindqvist, Y.6    Schneider, G.7
  • 111
    • 0033022342 scopus 로고    scopus 로고
    • Mechanism for hormone-independent prostate cancer through modulation of androgen receptor signaling by the HER-2/neu tyrosine kinase
    • Craft N., Shostak Y., Carey M., Sawyers C.L. Mechanism for hormone-independent prostate cancer through modulation of androgen receptor signaling by the HER-2/neu tyrosine kinase. Nat. Med. 1999, 5:280-285.
    • (1999) Nat. Med. , vol.5 , pp. 280-285
    • Craft, N.1    Shostak, Y.2    Carey, M.3    Sawyers, C.L.4
  • 112
    • 0033545848 scopus 로고    scopus 로고
    • From HER2/Neu signal cascade to androgen receptor and its coactivators: a novel pathway by induction of androgen target genes through MAP kinase in prostate cancer cells
    • Yeh S., Lin H.K., Kang H.Y., Thin T.H., Lin M.F., Chang C. From HER2/Neu signal cascade to androgen receptor and its coactivators: a novel pathway by induction of androgen target genes through MAP kinase in prostate cancer cells. Proc. Natl. Acad. Sci. U. S. A. 1999, 96:5458-5463.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 5458-5463
    • Yeh, S.1    Lin, H.K.2    Kang, H.Y.3    Thin, T.H.4    Lin, M.F.5    Chang, C.6
  • 113
    • 0023774990 scopus 로고
    • The epidermal growth factor receptor from prostate cells is dephosphorylated by a prostate-specific phosphotyrosyl phosphatase
    • Lin M.F., Clinton G.M. The epidermal growth factor receptor from prostate cells is dephosphorylated by a prostate-specific phosphotyrosyl phosphatase. Mol. Cell. Biol. 1988, 8:5477-5485.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 5477-5485
    • Lin, M.F.1    Clinton, G.M.2
  • 114
    • 0032555565 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of c-ErbB-2 is regulated by the cellular form of prostatic acid phosphatase in human prostate cancer cells
    • Meng T.C., Lin M.F. Tyrosine phosphorylation of c-ErbB-2 is regulated by the cellular form of prostatic acid phosphatase in human prostate cancer cells. J. Biol. Chem. 1998, 273:22096-22104.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22096-22104
    • Meng, T.C.1    Lin, M.F.2
  • 116
    • 0037421969 scopus 로고    scopus 로고
    • ErbB-2 signaling is involved in regulating PSA secretion in androgen-independent human prostate cancer LNCaP C-81 cells
    • Lee M.S., Igawa T., Yuan T.C., Zhang X.Q., Lin F.F., Lin M.F. ErbB-2 signaling is involved in regulating PSA secretion in androgen-independent human prostate cancer LNCaP C-81 cells. Oncogene 2003, 22:781-796.
    • (2003) Oncogene , vol.22 , pp. 781-796
    • Lee, M.S.1    Igawa, T.2    Yuan, T.C.3    Zhang, X.Q.4    Lin, F.F.5    Lin, M.F.6
  • 117
    • 45349108158 scopus 로고    scopus 로고
    • Elevated levels of HER-2/neu and androgen receptor in clinically localized prostate cancer identifies metastatic potential
    • Ricciardelli C., Jackson M.W., Choong C.S., Stahl J., Marshall V.R., Horsfall D.J., Tilley W.D. Elevated levels of HER-2/neu and androgen receptor in clinically localized prostate cancer identifies metastatic potential. Prostate 2008, 68:830-838.
    • (2008) Prostate , vol.68 , pp. 830-838
    • Ricciardelli, C.1    Jackson, M.W.2    Choong, C.S.3    Stahl, J.4    Marshall, V.R.5    Horsfall, D.J.6    Tilley, W.D.7
  • 119
    • 84861608177 scopus 로고    scopus 로고
    • Reactive oxygen species induced by p66Shc longevity protein mediate nongenomic androgen action via tyrosine phosphorylation signaling to enhance tumorigenicity of prostate cancer cells
    • Veeramani S., Chou Y.W., Lin F.C., Muniyan S., Lin F.F., Kumar S., Xie Y., Lele S.M., Tu Y., Lin M.F. Reactive oxygen species induced by p66Shc longevity protein mediate nongenomic androgen action via tyrosine phosphorylation signaling to enhance tumorigenicity of prostate cancer cells. Free Radic. Biol. Med. 2012, 53:95-108.
    • (2012) Free Radic. Biol. Med. , vol.53 , pp. 95-108
    • Veeramani, S.1    Chou, Y.W.2    Lin, F.C.3    Muniyan, S.4    Lin, F.F.5    Kumar, S.6    Xie, Y.7    Lele, S.M.8    Tu, Y.9    Lin, M.F.10
  • 121
    • 34047209514 scopus 로고    scopus 로고
    • Prostate-derived factor as a paracrine and autocrine factor for the proliferation of androgen receptor-positive human prostate cancer cells
    • Chen S.J., Karan D., Johansson S.L., Lin F.F., Zeckser J., Singh A.P., Batra S.K., Lin M.F. Prostate-derived factor as a paracrine and autocrine factor for the proliferation of androgen receptor-positive human prostate cancer cells. Prostate 2007, 67:557-571.
    • (2007) Prostate , vol.67 , pp. 557-571
    • Chen, S.J.1    Karan, D.2    Johansson, S.L.3    Lin, F.F.4    Zeckser, J.5    Singh, A.P.6    Batra, S.K.7    Lin, M.F.8
  • 122
    • 80955179558 scopus 로고    scopus 로고
    • TNFα enhances the motility and invasiveness of prostatic cancer cells by stimulating the expression of selective glycosyl- and sulfotransferase genes involved in the synthesis of selectin ligands
    • Radhakrishnan P., Chachadi V., Lin M.F., Singh R., Kannagi R., Cheng P.W. TNFα enhances the motility and invasiveness of prostatic cancer cells by stimulating the expression of selective glycosyl- and sulfotransferase genes involved in the synthesis of selectin ligands. Biochem. Biophys. Res. Commun. 2011, 409:436-441.
    • (2011) Biochem. Biophys. Res. Commun. , vol.409 , pp. 436-441
    • Radhakrishnan, P.1    Chachadi, V.2    Lin, M.F.3    Singh, R.4    Kannagi, R.5    Cheng, P.W.6
  • 124
    • 84884772860 scopus 로고    scopus 로고
    • PTPs emerge as PIPs: protein tyrosine phosphatases with lipid-phosphatase activities in human disease
    • Pulido R., Stoker A.W., Hendriks W.J. PTPs emerge as PIPs: protein tyrosine phosphatases with lipid-phosphatase activities in human disease. Hum. Mol. Genet. 2013, 22:R66-R76.
    • (2013) Hum. Mol. Genet. , vol.22
    • Pulido, R.1    Stoker, A.W.2    Hendriks, W.J.3
  • 125
    • 0347696003 scopus 로고    scopus 로고
    • Suppression versus induction of androgen receptor functions by the phosphatidylinositol 3-kinase/Akt pathway in prostate cancer LNCaP cells with different passage numbers
    • Lin H.K., Hu Y.C., Yang L., Altuwaijri S., Chen Y.T., Kang H.Y., Chang C. Suppression versus induction of androgen receptor functions by the phosphatidylinositol 3-kinase/Akt pathway in prostate cancer LNCaP cells with different passage numbers. J. Biol. Chem. 2003, 278:50902-50907.
    • (2003) J. Biol. Chem. , vol.278 , pp. 50902-50907
    • Lin, H.K.1    Hu, Y.C.2    Yang, L.3    Altuwaijri, S.4    Chen, Y.T.5    Kang, H.Y.6    Chang, C.7
  • 126
    • 84860217431 scopus 로고    scopus 로고
    • The functions and regulation of the PTEN tumour suppressor
    • Song M.S., Salmena L., Pandolfi P.P. The functions and regulation of the PTEN tumour suppressor. Nat. Rev. Mol. Cell Biol. 2012, 13:283-296.
    • (2012) Nat. Rev. Mol. Cell Biol. , vol.13 , pp. 283-296
    • Song, M.S.1    Salmena, L.2    Pandolfi, P.P.3
  • 127
    • 11144310076 scopus 로고    scopus 로고
    • The complexity of PTEN: mutation, marker and potential target for therapeutic intervention
    • Steelman L.S., Bertrand F.E., McCubrey J.A. The complexity of PTEN: mutation, marker and potential target for therapeutic intervention. Expert Opin. Ther. Targets 2004, 8:537-550.
    • (2004) Expert Opin. Ther. Targets , vol.8 , pp. 537-550
    • Steelman, L.S.1    Bertrand, F.E.2    McCubrey, J.A.3
  • 128
    • 36849018402 scopus 로고    scopus 로고
    • Why is PTEN an important tumor suppressor?
    • Li L., Ross A.H. Why is PTEN an important tumor suppressor?. J. Cell. Biochem. 2007, 102:1368-1374.
    • (2007) J. Cell. Biochem. , vol.102 , pp. 1368-1374
    • Li, L.1    Ross, A.H.2
  • 129
    • 33646705667 scopus 로고    scopus 로고
    • Regulation of the PTEN phosphatase
    • Gericke A., Munson M., Ross A.H. Regulation of the PTEN phosphatase. Gene 2006, 374:1-9.
    • (2006) Gene , vol.374 , pp. 1-9
    • Gericke, A.1    Munson, M.2    Ross, A.H.3
  • 130
    • 66149141021 scopus 로고    scopus 로고
    • PTEN and the PI3-kinase pathway in cancer
    • Chalhoub N., Baker S.J. PTEN and the PI3-kinase pathway in cancer. Annu. Rev. Pathol. 2009, 4:127-150.
    • (2009) Annu. Rev. Pathol. , vol.4 , pp. 127-150
    • Chalhoub, N.1    Baker, S.J.2
  • 131
    • 0035252894 scopus 로고    scopus 로고
    • Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling
    • Janssens V., Goris J. Protein phosphatase 2A: a highly regulated family of serine/threonine phosphatases implicated in cell growth and signalling. Biochem. J. 2001, 353:417-439.
    • (2001) Biochem. J. , vol.353 , pp. 417-439
    • Janssens, V.1    Goris, J.2
  • 132
  • 133
    • 0028021165 scopus 로고
    • Comparison of heterotrimeric protein phosphatase 2A containing different B subunits
    • Kamibayashi C., Estes R., Lickteig R.L., Yang S.I., Craft C., Mumby M.C. Comparison of heterotrimeric protein phosphatase 2A containing different B subunits. J. Biol. Chem. 1994, 269:20139-20148.
    • (1994) J. Biol. Chem. , vol.269 , pp. 20139-20148
    • Kamibayashi, C.1    Estes, R.2    Lickteig, R.L.3    Yang, S.I.4    Craft, C.5    Mumby, M.C.6
  • 134
    • 0030790128 scopus 로고    scopus 로고
    • Novel protein serine/threonine phosphatases: variety is the spice of life
    • Cohen P.T. Novel protein serine/threonine phosphatases: variety is the spice of life. Trends Biochem. Sci. 1997, 22:245-251.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 245-251
    • Cohen, P.T.1
  • 135
    • 33645232372 scopus 로고    scopus 로고
    • Protein phosphatase 2A regulatory subunit B56alpha associates with c-myc and negatively regulates c-myc accumulation
    • Arnold H.K., Sears R.C. Protein phosphatase 2A regulatory subunit B56alpha associates with c-myc and negatively regulates c-myc accumulation. Mol. Cell. Biol. 2006, 26:2832-2844.
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 2832-2844
    • Arnold, H.K.1    Sears, R.C.2
  • 137
    • 38349190654 scopus 로고    scopus 로고
    • Regulation of phosphorylation of Thr-308 of Akt, cell proliferation, and survival by the B55alpha regulatory subunit targeting of the protein phosphatase 2A holoenzyme to Akt
    • Kuo Y.C., Huang K.Y., Yang C.H., Yang Y.S., Lee W.Y., Chiang C.W. Regulation of phosphorylation of Thr-308 of Akt, cell proliferation, and survival by the B55alpha regulatory subunit targeting of the protein phosphatase 2A holoenzyme to Akt. J. Biol. Chem. 2008, 283:1882-1892.
    • (2008) J. Biol. Chem. , vol.283 , pp. 1882-1892
    • Kuo, Y.C.1    Huang, K.Y.2    Yang, C.H.3    Yang, Y.S.4    Lee, W.Y.5    Chiang, C.W.6
  • 138
    • 80054801896 scopus 로고    scopus 로고
    • Evaluation of PPP2R2A as a prostate cancer susceptibility gene: a comprehensive germline and somatic study
    • Cheng Y., Liu W., Kim S.T., Sun J., Lu L., Sun J., Zheng S.L., Isaacs W.B., Xu J. Evaluation of PPP2R2A as a prostate cancer susceptibility gene: a comprehensive germline and somatic study. Cancer Genet. 2011, 204:375-381.
    • (2011) Cancer Genet. , vol.204 , pp. 375-381
    • Cheng, Y.1    Liu, W.2    Kim, S.T.3    Sun, J.4    Lu, L.5    Sun, J.6    Zheng, S.L.7    Isaacs, W.B.8    Xu, J.9
  • 139
    • 84856741945 scopus 로고    scopus 로고
    • Pleckstrin homology domain leucine-rich repeat protein phosphatase (PHLPP): a new player in cell signaling
    • Warfel N.A., Newton A.C. Pleckstrin homology domain leucine-rich repeat protein phosphatase (PHLPP): a new player in cell signaling. J. Biol. Chem. 2012, 287:3610-3616.
    • (2012) J. Biol. Chem. , vol.287 , pp. 3610-3616
    • Warfel, N.A.1    Newton, A.C.2
  • 140
    • 33947203621 scopus 로고    scopus 로고
    • PHLPP and a second isoform, PHLPP2, differentially attenuate the amplitude of Akt signaling by regulating distinct Akt isoforms
    • Brognard J., Sierecki E., Gao T., Newton A.C. PHLPP and a second isoform, PHLPP2, differentially attenuate the amplitude of Akt signaling by regulating distinct Akt isoforms. Mol. Cell 2007, 25:917-931.
    • (2007) Mol. Cell , vol.25 , pp. 917-931
    • Brognard, J.1    Sierecki, E.2    Gao, T.3    Newton, A.C.4
  • 143
    • 77950239573 scopus 로고    scopus 로고
    • HER kinase axis receptor dimer partner switching occurs in response to EGFR tyrosine kinase inhibition despite failure to block cellular proliferation
    • Jain A., Penuel E., Mink S., Schmidt J., Hodge A., Favero K., Tindell C., Agus D.B. HER kinase axis receptor dimer partner switching occurs in response to EGFR tyrosine kinase inhibition despite failure to block cellular proliferation. Cancer Res. 2010, 70:1989-1999.
    • (2010) Cancer Res. , vol.70 , pp. 1989-1999
    • Jain, A.1    Penuel, E.2    Mink, S.3    Schmidt, J.4    Hodge, A.5    Favero, K.6    Tindell, C.7    Agus, D.B.8
  • 144
    • 0032903767 scopus 로고    scopus 로고
    • Reduced expression of protein tyrosine phosphatase gamma in lung and ovarian tumors
    • van Niekerk C.C., Poels L.G. Reduced expression of protein tyrosine phosphatase gamma in lung and ovarian tumors. Cancer Lett. 1999, 137:61-73.
    • (1999) Cancer Lett. , vol.137 , pp. 61-73
    • van Niekerk, C.C.1    Poels, L.G.2
  • 145
    • 0027520197 scopus 로고
    • Leukocyte common antigen-related receptor-linked tyrosine phosphatase. Regulation of mRNA expression
    • Longo F.M., Martignetti J.A., Le Beau J.M., Zhang J.S., Barnes J.P., Brosius J. Leukocyte common antigen-related receptor-linked tyrosine phosphatase. Regulation of mRNA expression. J. Biol. Chem. 1993, 268:26503-26511.
    • (1993) J. Biol. Chem. , vol.268 , pp. 26503-26511
    • Longo, F.M.1    Martignetti, J.A.2    Le Beau, J.M.3    Zhang, J.S.4    Barnes, J.P.5    Brosius, J.6
  • 147
    • 35649021332 scopus 로고    scopus 로고
    • NADPH oxidase promotes pancreatic cancer cell survival via inhibiting JAK2 dephosphorylation by tyrosine phosphatases
    • Lee J.K., Edderkaoui M., Truong P., Ohno I., Jang K.T., Berti A., Pandol S.J., Gukovskaya A.S. NADPH oxidase promotes pancreatic cancer cell survival via inhibiting JAK2 dephosphorylation by tyrosine phosphatases. Gastroenterology 2007, 133:1637-1648.
    • (2007) Gastroenterology , vol.133 , pp. 1637-1648
    • Lee, J.K.1    Edderkaoui, M.2    Truong, P.3    Ohno, I.4    Jang, K.T.5    Berti, A.6    Pandol, S.J.7    Gukovskaya, A.S.8
  • 148
    • 33646135276 scopus 로고    scopus 로고
    • Tyrosine kinase-role and significance in cancer
    • Paul M.K., Mukhopadhyay A.K. Tyrosine kinase-role and significance in cancer. Int. J. Med. Sci. 2004, 1:101-115.
    • (2004) Int. J. Med. Sci. , vol.1 , pp. 101-115
    • Paul, M.K.1    Mukhopadhyay, A.K.2
  • 150
    • 79960050610 scopus 로고    scopus 로고
    • PTEN tumor suppressor network in PI3K-Akt pathway control
    • Georgescu M.M. PTEN tumor suppressor network in PI3K-Akt pathway control. Genes Cancer 2010, 1:1170-1177.
    • (2010) Genes Cancer , vol.1 , pp. 1170-1177
    • Georgescu, M.M.1
  • 151
    • 84868528894 scopus 로고    scopus 로고
    • The PI3K/AKT/mTOR pathway as a therapeutic target in endometrial cancer
    • Slomovitz B.M., Coleman R.L. The PI3K/AKT/mTOR pathway as a therapeutic target in endometrial cancer. Clin. Cancer Res. 2012, 18:5856-5864.
    • (2012) Clin. Cancer Res. , vol.18 , pp. 5856-5864
    • Slomovitz, B.M.1    Coleman, R.L.2
  • 154
    • 84893003451 scopus 로고    scopus 로고
    • Therapeutic targeting of cancers with loss of PTEN function
    • Dillon L.M., Miller T.W. Therapeutic targeting of cancers with loss of PTEN function. Curr. Drug Targets 2014, 15:65-79.
    • (2014) Curr. Drug Targets , vol.15 , pp. 65-79
    • Dillon, L.M.1    Miller, T.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.