Identification by mass spectrometry of a new alpha-tubulin isotype expressed in human breast and lung carcinoma cell lines

Biochemistry
S RaoGeorge A Orr

Abstract

The extensive C-terminal molecular heterogeneity of alpha- and beta-tubulin is a consequence of multiple isotypes, the products of distinct genes, that undergo several posttranslational modifications. These include polyglutamylation and polyglycylation of both subunits, reversible tyrosination and removal of the penultimate glutamate from alpha-tubulin, and phosphorylation of the beta III isotype. A mass spectrometry-based method has been developed for the analysis of the C-terminal diversity of tubulin from human cell lines. Total cell extracts are resolved by SDS--PAGE and transferred to nitrocellulose, and the region of the blot corresponding to tubulin (approximately 50 kDa) was excised and digested with CNBr to release the highly divergent C-terminal tubulin fragments. The masses of the human alpha- and beta-tubulin CNBr-derived C-terminal peptides are all in the 1500--4000 Da mass range and can be analyzed directly by MALDI-TOF mass spectrometry in the negative ion mode without significant interference from other released peptides. In this study, the tubulin isotype diversity in MDA-MB-231, a human breast carcinoma cell line, and A549, a human non-small lung cancer cell line, is reported. The major tubulin isotypes presen...Continue Reading

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Citations

Jan 28, 2004·Cancer Letters·Alessia BiscaGiuseppe Damante
Jan 22, 2008·Journal of the American Society for Mass Spectrometry·Matthew T OlsonAlfred L Yergey
Feb 14, 2002·Chemical Reviews·Yehia Mechref, Milos V Novotny
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Mar 21, 2008·The Journal of Immunology : Official Journal of the American Association of Immunologists·Trudie A GoersThalachallour Mohanakumar

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