| Posttranslational nitrotyrosination of alpha-tubulin induces cell cycle arrest and inhibits proliferation of vascular smooth muscle cells. | |
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MedLine Citation:
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PMID: 17118269 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Hyperproliferation of vascular smooth muscle cells is a hallmark of atherosclerosis and related vascular complications. Microtubules are important for many aspects of mammalian cell responses including growth, migration and signaling. alpha-Tubulin, a component of the microtubule cytoskeleton, is unique amongst cellular proteins in that it undergoes a reversible posttranslational modification whereby the C-terminal tyrosine residue is removed (Glu-tubulin) and re-added (Tyr-tubulin). Whereas the reversible detyrosination/tyrosination cycle of alpha-tubulin has been implicated in regulating various aspects of cell biology, the precise function of this posttranslational modification has remained poorly characterized. Herein, we provide evidence suggesting that alpha-tubulin detyrosination is a required event in the proliferation of vascular smooth muscle cells. Proliferation of rat aortic smooth muscle cells in response to serum was temporally associated with the detyrosination of alpha-tubulin, but not acetylation of alpha-tubulin; Glu-tubulin reached maximal levels between 12 and 18h following cell cycle initiation. Inclusion of 3-nitro-l-tyrosine (NO(2)Tyr) in the culture medium resulted in the selective nitrotyrosination of alpha-tubulin, that was paralleled by decreased elaboration of Glu-tubulin, decreased expression of cyclins A and E, decreased association of the microtubule plus-end binding protein EB1, and inhibited cell proliferation. Nitrotyrosination of alpha-tubulin did not induce necrotic or apoptotic death of rat aortic smooth muscle cells, but instead led to cell cycle arrest at the G(1)/S boundary coincident with decreased DNA synthesis. Collectively, these results suggest that the C-terminus of alpha-tubulin and its detyrosination are functionally important as a molecular switch that regulates cell cycle progression in vascular smooth muscle cells. |
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Authors:
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Anh D Phung; Karel Soucek; Lukás Kubala; Richart W Harper; J Chloë Bulinski; Jason P Eiserich |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S. |
Journal Detail:
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Title: European journal of cell biology Volume: 85 ISSN: 0171-9335 ISO Abbreviation: Eur. J. Cell Biol. Publication Date: 2006 Dec |
Date Detail:
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Created Date: 2006-11-22 Completed Date: 2007-02-06 Revised Date: 2007-12-03 |
Medline Journal Info:
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Nlm Unique ID: 7906240 Medline TA: Eur J Cell Biol Country: Germany |
Other Details:
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Languages: eng Pagination: 1241-52 Citation Subset: IM |
Affiliation:
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Department of Internal Medicine, University of California, Davis, CA 95616, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Apoptosis / physiology Cell Cycle / physiology* Cell Proliferation* Cells, Cultured Glutamic Acid / metabolism Microtubules / physiology Muscle, Smooth, Vascular / cytology*, physiology Protein Processing, Post-Translational / physiology* Rats Tubulin / metabolism* Tyrosine / analogs & derivatives*, metabolism |
| Grant Support | |
ID/Acronym/Agency:
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HL07013/HL/NHLBI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Tubulin; 3604-79-3/3-nitrotyrosine; 55520-40-6/Tyrosine; 56-86-0/Glutamic Acid |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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