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Class III beta-tubulin and gamma-tubulin are co-expressed and form complexes in human glioblastoma cells
Journal article   Peer reviewed

Class III beta-tubulin and gamma-tubulin are co-expressed and form complexes in human glioblastoma cells

Christos D Katsetos, Eduarda Dráberová, Barbora Smejkalová, Goutham Reddy, Louise Bertrand, Jean-Pierre de Chadarévian, Agustin Legido, Jonathan Nissanov, Peter W Baas and Pavel Dráber
Neurochemical research, v 32(8), pp 1387-1398
Aug 2007
DOI: https://doi.org/10.1007/s11064-007-9321-1
PMID: 17406983
Featured in Collection :   UN Sustainable Development Goals @ Drexel

Abstract

Paclitaxel - pharmacology Tubulin Modulators - pharmacology Humans Multiprotein Complexes Brain Neoplasms - pathology Nocodazole - pharmacology Tubulin - genetics Cell Line, Tumor - drug effects Brain Neoplasms - metabolism Tubulin - metabolism Cell Line, Tumor - cytology Glioblastoma - pathology Adult Glioblastoma - metabolism Vinblastine - pharmacology Antineoplastic Agents, Phytogenic - pharmacology Cell Line, Tumor - metabolism Child
We have previously shown that the neuronal-associated class III beta-tubulin isotype and the centrosome-associated gamma-tubulin are aberrantly expressed in astrocytic gliomas (Cell Motil Cytoskeleton 2003, 55:77-96; J Neuropathol Exp Neurol 2006, 65:455-467). Here we determined the expression, distribution and interaction of betaIII-tubulin and gamma-tubulin in diffuse-type astrocytic gliomas (grades II-IV) (n = 17) and the human glioblastoma cell line T98G. By immunohistochemistry and immunofluorescence microscopy, betaIII-tubulin and gamma-tubulin were co-distributed in anaplastic astrocytomas and glioblastomas and to a lesser extent, in low-grade diffuse astrocytomas (P < 0.05). In T98G glioblastoma cells betaIII-tubulin was associated with microtubules whereas gamma-tubulin exhibited striking diffuse cytoplasmic staining in addition to its expectant centrosome-associated pericentriolar distribution. Treatment with different anti-microtubule drugs revealed that betaIII-tubulin was not associated with insoluble gamma-tubulin aggregates. On the other hand, immunoprecipitation experiments unveiled that both tubulins formed complexes in soluble cytoplasmic pools, where substantial amounts of these proteins were located. We suggest that aberrant expression and interactions of betaIII-tubulin and gamma-tubulin may be linked to malignant changes in glial cells.

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Domestic collaboration
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Web of Science research areas
Biochemistry & Molecular Biology
Neurosciences
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