| Methylglyoxal induces apoptosis in Jurkat leukemia T cells by activating c-Jun N-terminal kinase. | |
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MedLine Citation:
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PMID: 10723098 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Methylglyoxal (MG) is a physiological metabolite, but it is known to be toxic, inducing stress in cells and causing apoptosis. This study examines molecular mechanisms in the MG-induced signal transduction leading to apoptosis, focusing particularly on the role of JNK activation. We first confirmed that MG caused apoptosis in Jurkat cells and that it was cell type dependent because it failed to induce apoptosis in MOLT-4, HeLa, or COS-7 cells. A caspase inhibitor, Z-DEVD-fmk, completely blocked MG-induced poly(ADP-ribose)polymerase (PARP) cleavage and apoptosis, showing the critical role of caspase activation. Inhibition of JNK activity by a JNK inhibitor, curcumin, remarkably reduced MG-induced caspase-3 activation, PARP cleavage, and apoptosis. Stable expression of the dominant negative mutant of JNK also protected cells against apoptosis notably, although not completely. Correspondingly, loss of the mitochondrial membrane potential induced by MG was decreased by the dominant negative JNK. These results confirmed a crucial role of JNK working upstream of caspases, as well as an involvement of JNK in affecting the mitochondrial membrane potential. |
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Authors:
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J Du; H Suzuki; F Nagase; A A Akhand; T Yokoyama; T Miyata; K Kurokawa; I Nakashima |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Journal of cellular biochemistry Volume: 77 ISSN: 0730-2312 ISO Abbreviation: J. Cell. Biochem. Publication Date: 2000 Mar |
Date Detail:
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Created Date: 2000-05-31 Completed Date: 2000-05-31 Revised Date: 2009-11-19 |
Medline Journal Info:
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Nlm Unique ID: 8205768 Medline TA: J Cell Biochem Country: UNITED STATES |
Other Details:
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Languages: eng Pagination: 333-44 Citation Subset: IM |
Copyright Information:
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Copyright 2000 Wiley-Liss, Inc. |
Affiliation:
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Department of Immunology, Nagoya University School of Medicine, Aichi 466-8550, Japan. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Apoptosis / drug effects* COS Cells Caspase 3 Caspases / antagonists & inhibitors Cell Line Cysteine Proteinase Inhibitors / pharmacology Enzyme Activation / drug effects Hela Cells Humans Intracellular Membranes / drug effects, metabolism JNK Mitogen-Activated Protein Kinases Jurkat Cells Membrane Potentials / drug effects Mitochondria / drug effects, metabolism Mitogen-Activated Protein Kinases / genetics, metabolism* Mutation Oligopeptides / pharmacology Poly(ADP-ribose) Polymerases / metabolism Pyruvaldehyde / toxicity* Transfection |
| Chemical | |
Reg. No./Substance:
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0/Cysteine Proteinase Inhibitors; 0/Oligopeptides; 0/benzoylcarbonyl-aspartyl-glutamyl-valyl-aspartyl-fluoromethyl ketone; 78-98-8/Pyruvaldehyde; EC 2.4.2.30/Poly(ADP-ribose) Polymerases; EC 2.7.11.24/JNK Mitogen-Activated Protein Kinases; EC 2.7.11.24/Mitogen-Activated Protein Kinases; EC 3.4.22.-/CASP3 protein, human; EC 3.4.22.-/Caspase 3; EC 3.4.22.-/Caspases |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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