Abstract
Tau is a microtubule-associated protein that causes proper role of neuron by assembling and stabilizing microtubules. The amount and post translational modification of tau can change its function as a stabilizer of microtubules. The aim of the study was to look for the expression of tau in colorectal cancer and normal cells, along with phosphorylation and microtubule binding properties of tau expressed in colorectal cancer cell. Two colorectal cancer cells (SW480 and HCT 116) expressed tau that was also phosphorylated, whereas the others (Caco-2, HT-29 and DLD1) did not. Colorectal normal cell (CCD-18Co) expressed very tiny amount of tau that was not phosphorylated. A big fraction of tau in HCT 116 did not bind to microtubule. The results suggest that some colorectal cancer cells express hyperphosphorylated tau as found in Alzheimer’s disease. So, tau in colorectal cancer cells does not look like same as tau in normal adult brain; rather it works nearly same as tau in neurodegenerative disease.
This is a preview of subscription content, log in via an institution to check access.
References
Alonso AC, Zaidi T, Grundke-Iqbal I, Iqbal K (1994) Role of abnormally phosphorylated tau in the breakdown of microtubules in Alzheimer disease. Proc Natl Acad Sci USA 91:5562–5566
Alonso AC, Grundke-Iqbal I, Iqbal K (1996) Alzheimer’s disease hyperphosphorylated tau sequesters normal tau into tangles of filaments and disassembles microtubules. Nat Med 2:783–787
Andorfer C, Acker CM, Kress Y, Hof PR, Duff K, Davies P (2005) Cell-cycle reentry and cell death in transgenic mice expressing nonmutant human tau isoforms. J Neurosci 25:5446–5454
Caceres A, Kosik KS (1990) Inhibition of neurite polarity by tau antisense oligonucleotides in primary cerebellar neurons. Nature 343:461–463
Cross DC, Munoz JP, Hernandez P, Maccioni RB (2000) Nuclear and cytoplasmic tau proteins from human nonneuronal cells share common structural and functional features with brain tau. J Cell Biochem 78:305–317
Dixit R, Ross JL, Goldman YE, Holzbaur EL (2008) Differential regulation of dynein and kinesin motor proteins by tau. Science 319:1086–1089
Gu Y, Oyama F, Ihara Y (1996) Tau is widely expressed in rat tissues. J Neurochem 67:1235–1244
Harada A, Oguchi K, Okabe S, Kuno J, Terada S, Ohshima T, Sato-Yoshitake R, Takei Y, Noda T, Hirokawa N (1994) Altered microtubule organization in small-calibre axons of mice lacking tau protein. Nature 369:488–491
Jemal A, Murray T, Samuels A, Ghafoor A, Ward E, Thun MJ (2003) Cancer statistics. CA-Cancer J Clin 53:5–26
Jimeno A, Hallur G, Chan A, Zhang X, Cusatis G, Chan F, Shah P, Chen R, Hamel E, Garrett-Mayer E, Khan S, Hidalgo M (2007) Development of two novel benzoylphenylurea sulfur analogues and evidence that the microtubule-associated protein tau is predictive of their activity in pancreatic cancer. Mol Cancer Ther 6:1509–1516
Kenner L, El-Shabrawi Y, Hutter H, Forstner M, Zatloukal K, Hoefler G, Preisegger KH, Kurzbauer R, Denk H (1994) Expression of three- and four-repeat tau isoforms in mouse liver. Hepatology 20:1086–1089
Kolarova M, Garcia-Sierra F, Bartos A, Ricny J, Ripova D (2012) Structure and pathology of tau protein in Alzheimer disease. Int J Alzheimer’s Dis 2012:731526
Kosik KS, Joachim CL, Selkoe DJ (1986) Microtubule-associated protein tau (tau) is a major antigenic component of paired helical filaments in Alzheimer disease. Proc Natl Acad Sci USA 83:4044–4048
Lee VM, Goedert M, Trojanowski JQ (2001) Neurodegenerative tauopathies. Annu Rev Neurosci 24:1121–1159
Li ZH, Xiong QY, Tu JH, Gong Y, Qiu W, Zhang HQ, Wei WS, Hou YF, Cui WQ (2013) Tau proteins expressions in advanced breast cancer and its significance in taxane-containing neoadjuvant chemotherapy. Med Oncol 30:591
Lindwall G, Cole RD (1984) Phosphorylation affects the ability of tau protein to promote microtubule assembly. J Biol Chem 259:5301–5305
Liu F, Iqbal K, Grundke-Iqbal I, Rossie S, Gong CX (2005) Dephosphorylation of tau by protein phosphatase 5: impairment in Alzheimer’s disease. J Biol Chem 280:1790–1796
Mandelkow EM, Biernat J, Drewes G, Gustke N, Trinczek B, Mandelkow E (1995) Tau domains, phosphorylation, and interactions with microtubules. Neurobiol Aging 16:355–362
Mimori K, Sadanaga N, Yoshikawa Y, Ishikawa K, Hashimoto M, Tanaka F, Sasaki A, Inoue H, Sugimachi K, Mori M (2006) Reduced tau expression in gastric cancer can identify candidates for successful Paclitaxel treatment. Brit J Cancer 94:1894–1897
Pusztai L, Jeong JH, Gong Y, Ross JS, Kim C, Paik S, Rouzier R, Andre F, Hortobagyi GN, Wolmark N, Symmans WF (2009) Evaluation of microtubule-associated protein-tau expression as a prognostic and predictive marker in the NSABP-B 28 randomized clinical trial. J Clin Oncol 27:4287–4292
Rouzier R, Rajan R, Wagner P, Hess KR, Gold DL, Stec J, Ayers M, Ross JS, Zhang P, Buchholz TA, Kuerer H, Green M, Arun B, Hortobagyi GN, Symmans WF, Pusztai L (2005) Microtubule-associated protein tau: a marker of paclitaxel sensitivity in breast cancer. Proc Natl Acad Sci USA 102:8315–8320
Sangrajrang S, Denoulet P, Millot G, Tatoud R, Podgorniak MP, Tew KD, Calvo F, Fellous A (1998) Estramustine resistance correlates with tau over-expression in human prostatic carcinoma cells. Int J Cancer 77:626–631
Smith CJ, Anderton BH, Davis DR, Gallo JM (1995) Tau isoform expression and phosphorylation state during differentiation of cultured neuronal cells. FEBS Lett 375:243–248
Smoter M, Bodnar L, Grala B, Stec R, Zieniuk K, Kozlowski W, Szczylik C (2013) Tau protein as a potential predictive marker in epithelial ovarian cancer patients treated with paclitaxel/platinum first-line chemotherapy. J Exp Clin Canc Res 32:25
Souter S, Lee G (2009) Microtubule-associated protein tau in human prostate cancer cells: isoforms, phosphorylation, and interactions. J Cell Biochem 108:555–564
Wagner P, Wang B, Clark E, Lee H, Rouzier R, Pusztai L (2005) Microtubule associated protein (MAP)-tau: a novel mediator of paclitaxel sensitivity in vitro and in vivo. Cell Cycle 4:1149–1152
Wang Q, Wang N, Shao G, Qian J, Shen D, Fei Y, Mao W, Wu D (2013) Relationship between gastric cancer tau protein expression and paclitaxel sensitivity. Pathol Oncol Res 19:429–435
Weingarten MD, Lockwood AH, Hwo SY, Kirschner MW (1975) A protein factor essential for microtubule assembly. Proc Natl Acad Sci USA 72:1858–1862
Witman GB, Cleveland DW, Weingarten MD, Kirschner MW (1976) Tubulin requires tau for growth onto microtubule initiating sites. Proc Natl Acad Sci USA 73:4070–4074
Wood JG, Mirra SS, Pollock NJ, Binder LI (1986) Neurofibrillary tangles of Alzheimer disease share antigenic determinants with the axonal microtubule-associated protein tau (tau). Proc Natl Acad Sci USA 83:4040–4043
Zhang X, Zhang YW, Liu S, Bulloj A, Tong GG, Zhang Z, Liao FF, Xu H (2006) Tumor suppressor PTEN affects tau phosphorylation: deficiency in the phosphatase activity of PTEN increases aggregation of an FTDP-17 mutant tau. Mol Neurodegener 1:7
Acknowledgments
This research was performed as part of the project titled ‘Development and industrialization of high value cosmetic raw materials from marine microalgae,’ funded by the Ministry of Oceans and Fisheries, Korea and was supported by an intramural Grant (2Z04690) from the KIST Gangneung Institute of Natural Products.
Author information
Authors and Affiliations
Corresponding author
Rights and permissions
About this article
Cite this article
Huda, M.N., Kim, D.H., Erdene-Ochir, E. et al. Expression, phosphorylation, localization, and microtubule binding of tau in colorectal cell lines. Appl Biol Chem 59, 807–812 (2016). https://doi.org/10.1007/s13765-016-0228-x
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s13765-016-0228-x