| Constitutive expression and cytoplasmic compartmentalization of ATM protein in differentiated human neuron-like SH-SY5Y cells. | |
MedLine Citation:
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PMID: 17241156 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Ataxia telangiectasia (A-T) is an autosomal, recessive disorder mainly characterized by neuronal degeneration. However, the reason for neuronal degeneration in A-T patients is still unclear. ATM (A-T, mutated), the gene mutated in A-T, encodes a 370-kDa protein kinase. We measured the levels of the ATM protein found in differentiated neuron-like rat PC12 cells and differentiated neuron-like human SH-SY5Y cells. We found that, in rat PC12 cells, ATM levels decreased dramatically after differentiation, which is consistent with previous results observed in differentiated mouse neural progenitor cells. In contrast, the levels of ATM were similar before and after differentiation in human SH-SY5Y cells. Using an indirect immunofluorescence assay, we showed that ATM translocates from the nucleus to the cytoplasm in differentiated human SH-SY5Y cells. The translocation of ATM was further verified by subcellular fractionation experiments. The constitutive expression and cytoplasmic translocation of ATM in differentiated SH-SY5Y cells suggest that ATM is important for maintaining the regular function of human neuronal cells. Our results further demonstrated that, in response to insulin, ATM protects differentiated neuron-like SH-SY5Y cells from serum starvation-induced apoptosis. These data provide the first evidence that cytoplasmic ATM promotes survival of human neuronal cells in an insulin-dependent manner. |
Authors:
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Jessica K Boehrs; Jinghua He; Marie-Jo Halaby; Da-Qing Yang |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, U.S. Gov't, Non-P.H.S. |
Journal Detail:
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Title: Journal of neurochemistry Volume: 100 ISSN: 0022-3042 ISO Abbreviation: J. Neurochem. Publication Date: 2007 Jan |
Date Detail:
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Created Date: 2007-01-23 Completed Date: 2007-03-06 Revised Date: 2011-11-02 |
Medline Journal Info:
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Nlm Unique ID: 2985190R Medline TA: J Neurochem Country: England |
Other Details:
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Languages: eng Pagination: 337-45 Citation Subset: IM |
Affiliation:
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Division of Basic Biomedical Sciences, University of South Dakota, Sanford School of Medicine, Vermillion, South Dakota 57069, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Blotting, Western Cell Count Cell Cycle Proteins / metabolism* Cell Differentiation / drug effects, physiology* Cell Line Cell Nucleus / metabolism Culture Media, Serum-Free / pharmacology Cytoplasm / metabolism* DNA-Binding Proteins / metabolism* Fluorescent Antibody Technique / methods Gene Expression Regulation / drug effects, physiology Humans In Situ Nick-End Labeling / methods Nerve Growth Factor / pharmacology Neural Cell Adhesion Molecules / metabolism Neurites / physiology Neuroblastoma Neurons / metabolism*, ultrastructure* Protein-Serine-Threonine Kinases / metabolism* RNA, Messenger / metabolism Rats Reverse Transcriptase Polymerase Chain Reaction / methods Subcellular Fractions / drug effects, metabolism Transfection / methods Tretinoin / pharmacology Tumor Suppressor Proteins / metabolism* |
| Grant Support | |
ID/Acronym/Agency:
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5P20RR015567-05/RR/NCRR NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Cell Cycle Proteins; 0/Culture Media, Serum-Free; 0/DNA-Binding Proteins; 0/Neural Cell Adhesion Molecules; 0/RNA, Messenger; 0/Tumor Suppressor Proteins; 302-79-4/Tretinoin; 9061-61-4/Nerve Growth Factor; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 2.7.11.1/ataxia telangiectasia mutated protein |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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