Abstract
Receptor protein tyrosine phosphatase α (RPTPα) is transmembrane protein phosphatases, and has been proposed to be involved in the differentiation of the neuronal system. In the present study, we demonstrated the expression of RPTPα mRNA in several normal human tissues. We further investigated the regulation of expression of RPTPα mRNA in epithelial cells utilizing three commercially available human prostate cancer cell lines LNCaP, PC-3 and DU145. This is because these cells exhibit different levels of differentiation, defined by the expression of a tissue-specific differentiation antigen, prostatic acid phosphatase (PAcP), and their androgen sensitivity. LNCaP cells express PAcP and are androgen-sensitive cells, while PC-3 and DU145 cells do not express PAcP and are androgen-insensitive cells. Northern blot analyses revealed that, in LNCaP cells, fetal bovine serum (FBS) and 5α-dihydrotestosterone (DHT) down-regulates RPTPα mRNA expression, similar to the effect on PAcP. Contrarily, FBS up-regulated the RPTPα mRNA level in PC-3 and DU145 cells. In LNCaP cells, sodium butyrate inhibited cell growth and up-regulated RPTPα as well as PAcP mRNA expression. Although, sodium butyrate also inhibited the growth of PC-3 and DU145 cells, the level of RPTPα mRNA was decreased in PC-3, while increased in DU145 cells. Thus, data taken together indicate that the expression of RPTPα is apparently regulated by a similar mechanism to that of PAcP in LNCaP cells.
Similar content being viewed by others
References
Neel BG, Tonks NK: Protein tyrosine phosphatases in signal transduction. Curr Opin Cell Biol 9: 193–204, 1997
Atherton Fessler S, Hannig G, Piwnica Worms H: Reversible tyrosine phosphorylation and cell cycle control. Semin Cell Biol 4: 433–442, 1993
Chan AC, Desai DM, Weiss A: The role of protein tyrosine kinases and protein tyrosine phosphatases in T cell antigen receptor signal transduction. Annu Rev Immunol 12: 555–592, 1994
Hunter T. Oncogene products in the cytoplasm: The protein kinases. In “Oncogenes and The Molecular Origins of Cancer” Cold Spring Harbor Lab. Press, Cold Spring Harbor, 1989, pp 147–173
Hunter T, Cooper JA: Protein tyrosine kinases. Annu Rev Biochem 54: 897–930, 1985
Charbonneau H, Tonks NK: 1002 protein phosphatases. Annu Rev Cell Biol 8: 463–493, 1992
Sap J, Jiang YP, Friedlander D, Grumet M, Schlessinger J: Receptor tyrosine phosphatase R-PTP-kappa mediates homophilic binding. Mol Cell Biol 14: 1–9, 1994
Peles E, Nativ M, Campbell PL, Sakurai T, Martinez R, Lev S, Clary DO, Schilling J, Barnea G, Plowman GD, Grumet M, Schlessinger J: The carbonic anhydrase domain of receptor tyrosine phosphatase beta is a functional ligand for the axonal cell recognition molecule contactin. Cell 82: 251–260, 1995
Mauro LJ, Dixon JE: 'Zip codes' direct intracellular protein tyrosine phosphatases to the correct cellular 'address'. Trends Biochem Sci 19: 151–155, 1994
Matthews RJ, Chair ED, Thomas ML: Identification of an additional member of protein-tyrosine phosphatase familyevidence for alternative splicing in the tyrosine phosphatase domain. Proc Natl Acad Sci USA 87: 4444–4448, 1990
Sap J, Eustachio PD, Givol D, Schlessinger J: Cloning and expression of a widely expressed receptor tyrosine phosphatase. Proc Natl Acad Sci USA 87: 6112–6116, 1990
Daum G, Regenass S, Sap J, Schlessinger J, Fischer EH: Multiple forms of the human tyrosine phosphatase RPTP alpha. Isozymes and differences in glycosylation. J Biol Chem 269: 10524–10528, 1994
Wang Y, Pallen CJ: The receptor-like protein tyrosine phosphatase HPTP alpha has two active catalytic domains with distinct substrate specificities. EMBO J 10: 3231–3237, 1991
den Hertog J, Tracy S, Hunter T: Phosphorylation of receptor protein-tyrosine phosphatase alpha on Tyr789, a binding site for the SH3-SH2-SH3 adaptor protein GRB-2 in vivo. EMBO J 13: 3020–3032, 1994
den Hertog J, Hunter T: Tight association of GRB2 with receptor protein-tyrosine phosphatase alpha is mediated by the SH2 and C-terminal SH3 domains. EMBO J 15: 3016–3027, 1996
Su J, Yang LT, Sap J: Association between receptor protein-tyrosine phosphatase RPTPalpha and the Grb2 adaptor. Dual Src homology (SH) 2/SH3 domain requirement and functional consequences. J Biol Chem 271: 28086–28096, 1996
Zheng XM, Pallen CJ: Expression of receptor-like protein tyrosine phosphatase alpha in rat embryo fibroblasts activates mitogenactivated protein kinase and c-Jun. J Biol Chem 269: 23302–23309, 1994
Zheng XM, Wang Y, Pallen CJ: Cell transformation and activation of pp60c-src by overexpression of a protein tyrosine phosphatase. Nature 359: 336–339, 1992
den Hertog J, Pals CE, Peppelenbosch MP, Tertoolen LG, de Laat SW, Kruijer W: Receptor protein tyrosine phosphatase alpha activates pp60c-src and is involved in neuronal differentiation. EMBO J 12: 3789–3798, 1993
Bjelfman C, Meyerson G, Cartwright CA, Mellstrom K, Hammerling U, Pahlman S: Early activation of endogenous pp60src kinase activity during neuronal differentiation of cultured human neuroblastoma cells. Mol Cell Biol 10: 361–370, 1990
Lynch SA, Brugge JS, Levine JM: Induction of altered c-src product during neural differentiation of embryonal carcinoma cells. Science 234: 873–876, 1986
van Inzen WG, Peppelenbosch MP, van den Brand MW, Tertoolen LG, de Laat S: The role of receptor protein tyrosine phosphatase alpha in neuronal differentiation of embryonic stem cells. Brain Res Dev Brain Res. 91: 304–307, 1996
Yang XH, Seow KT, Bahri SM, Oon SH, Chia W: Two Drosophila receptor-like tyrosine phosphatase genes are expressed in a subset of developing axons and pioneer neurons in the embryonic CNS. Cell 67: 661–673, 1991
Lin MF, DaVolio J, Garcia-Arenas R: Expression of human prostatic acid phosphatase activity and the growth of prostate carcinoma cells. Cancer Res 52: 4600–4607, 1992
Lin MF, Meng TC, Rao PS, Chang C, Schonthal AH, Lin FF: Expression of human prostatic acid phosphatase correlates with androgen-stimulated cell proliferation in prostate cancer cell lines. J Biol Chem 273: 5939–5947, 1998
Shen R, Dorai T, Szaboles M, Katz AE, Olsson CA, Buttyan R: Transdifferenciation of cultured human prostate cancer cells to a neuroendocrine cell phenotype in a hormone-depleted medium. Urol Oncol 3: 67–75, 1997
Qiu Y, Robinson D, Pretlow TG, Kung H: JEtk/Bmx, a tyrosine kinase with a pleckstrin-homology domain, is an effector of phosphatidylinositol 3′-kinase and is involved in interleukin 6-induced neuroendocrine differentiation of prostate cancer cells. Proc Natl Acad Sci USA 95: 3644–3649, 1998
Bonkhoff H, Wernert N, Dhom G, Remberger K: Relation of endocrine-paracrine cells to cell proliferation in normal, hyperplastic, and neoplastic human prostate. Prostate 19: 91–98, 1991
di Sant'Agnese PA: Neuroendocrine differentiation in carcinoma of the prostate. Diagnostic, prognostic, and therapeutic implications. Cancer 70: 254–268, 1992
Garcia-Arenas R, Lin FF, Lin D, Jin LP, Shih CC, Chang C, Lin MF: The expression of prostatic acid phosphatase is transcriptionally regulated in human prostate carcinoma cells. Mol Cell Endocrinol 111: 29–37, 1995
Kaighn ME, Kirk D, Szalay M, Lechner JF: Growth control of prostatic carcinoma cells in serum-free media: interrelationship of hormone response, cell density, and nutrient media. Proc Natl Acad Sci USA 78: 5673–5676, 1981
Chomczynski P: A reagent for the single-step simultaneous isolation of RNA, DNA and proteins from cell and tissue samples. Biotechniques 15: 532–534, 536–537, 1993
Zelivianski S, Comeau D, Lin MF: Cloning and analysis of the promoter activity of the human prostatic acid phosphatase gene. Biochem Biophys Res Commun 245: 108–112, 1998
Lin MF, Garcia-Arenas R, Kawachi M, Lin FF: Regulation of the expression of prostatic acid phosphatase in LNCaP human prostate carcinoma cells. Cell Mol Biol Res 39: 739–750, 1993
Tian SS, Tsoulfas P, Zinn K: Three receptor-linked protein-tyrosine phosphatases are selectively expressed on central nervous system axons in the Drosophila embryo. Cell 67: 675–680, 1991
Halgunset J, Lamvik T, Espevik T: Butyrate effects on growth, morphology, and fibronectin production in PC-3 prostatic carcinoma cells. Prostate 12: 65–77, 1988
Hathcock KS, Hirano H, Hodes RJ: CD45 expression by murine B cells and T cells: alteration of CD45 isoforms in subpopulations of activated B cells. Immunol Res 12: 21–36, 1993
Buzzi M, Lu L, Lombardi AJJr, Posner MR, Brautigan DL, Fast LD, Frackelton ARJr: Differentiation-induced changes in proteintyrosine phosphatase activity and commensurate expression of CD45 in human leukemia cell lines. Cancer Res 52: 4027–4035, 1992
Watanabe TKT, Oishi M: Alteration of phosphotyrosinecontaining proteins at the early stage of erythroid differentiation of mouse erythroleukemia (MEL) cells. J Biol Chem 267: 17116–17120, 1992
den Hertog J, Pals CE, Jonk LJ, Kruijer W: Differential expression of a novel murine non-receptor protein tyrosine phosphatase during differentiation of P19 embryonal carcinoma cells. Biochem Biophys Res Commun 184: 1241–1249, 1992
Seimiya H, Tsuruo T: Differential expression of protein tyrosine phosphatase genes during phorbol ester-induced differentiation of human leukemia U937 cells. Cell Growth Differ 4: 1033–1039, 1993
Henttu P, Vihko P: The protein kinase C activator, phorbol ester, elicits disparate functional responses in androgen-sensitive and androgen-independent human prostatic cancer cells. Biochem Biophys Res Commun 244: 167–171, 1998
Tsai W, Morielli AD, Cachero TG, Peralta EG: Receptor protein tyrosine phosphatase alpha participates in the m1 muscarinic acetylcholine receptor-dependent regulation of Kv1.2 channel activity. EMBO J 18: 109–118, 1999
Camby I, Etievant C, Petein M, Dedecker R, van Velthoven R, Danguy A, Pasteels JL, Kiss R: Influence of culture media on the morphological differentiation of the PC-3 and DU145 prostatic neoplastic cell lines. Prostate 24: 187–196, 1994
Timar J, Raso E, Fazakas ZS, Silletti S, Raz A, Honn KV: Multiple use of a signal transduction pathway in tumor cell invasion. Anticancer Res 16: 3299–3306, 1996
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Zelivianski, S., Dean, J., Madhavan, D. et al. Expression of receptor protein tyrosine phosphatase agr; mRNA in human prostate cancer cell lines. Mol Cell Biochem 208, 11–18 (2000). https://doi.org/10.1023/A:1007010304194
Issue Date:
DOI: https://doi.org/10.1023/A:1007010304194