Journal
JOURNAL OF CELLULAR BIOCHEMISTRY
Volume 108, Issue 3, Pages 555-564Publisher
WILEY
DOI: 10.1002/jcb.22287
Keywords
TAU; PROSTATE CANCER CELLS; MICROTUBULE BINDING; PHOSPHORYLATION; PHOSPHATIDYLINOSITOL 3-KINASE
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Funding
- National Cancer Institute (NCI) [CA103672]
- University of Iowa and Aging Program Research Development Funding Initiative
- NIH [P20]
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Tau is a microtubule-associated protein whose function has been investigated primarily in neurons. Recently, tau expression has been correlated with increased drug resistance in various cancers of non-neuronal tissues. In this report, we investigate the tau expressed in cancerous prostate lines ALVA-31, DU 145, and PC-3. Prostate cancer tau is heat-stable and highly phosphorylated, containing many of the modifications identified in Alzheimer's disease brain tau. RT-PCR and phosphatase treatment indicated that all six alternatively spliced adult brain tau isoforms are expressed in ALVA-31 cells, and isoforms containing exon 6 as well as high molecular weight tau isoforms containing either exon 4A or a larger splice variant of exon 4A are also present. Consistent with its hyperphosphorylated state, a large proportion of ALVA-31 tau does not bind to microtubules, as detected by confocal microscopy and biochemical tests. Finally, endogenous ALVA-31 tau can interact with the p85 subunit of phosphatidylinositol 3-kinase, as demonstrated by co-immunoprecipitations and in vitro protein-binding assays. Our results suggest that tau in prostate cancer cells does not resemble that front normal adult brain and support the hypothesis that tau is a multifunctional protein. J. Cell. Biochem. 108: 555-564, 2009. (C) 2009 Wiley-Liss, Inc.
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