Source:http://linkedlifedata.com/resource/pubmed/id/16763214
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
6
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| pubmed:dateCreated |
2006-9-7
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| pubmed:abstractText |
Promyelocytic NB4 leukemia cells undergo differentiation to granulocytes following retinoic acid treatment. Here we report that tissue transglutaminase (TG2), a protein cross-linking enzyme, was induced, then partially translocated into the nucleus, and became strongly associated with the chromatin during the differentiation process. The transglutaminase-catalyzed cross-link content of both the cytosolic and the nuclear protein fractions increased while NB4 cells underwent cellular maturation. Inhibition of cross-linking activity of TG2 by monodansylcadaverin in these cells led to diminished nitroblue tetrazolium (NBT) positivity, production of less superoxide anion, and decreased expression of GP91PHOX, the membrane-associated subunit of NADPH oxidase. Neutrophils isolated from TG2(-/-) mice showed diminished NBT reduction capacity, reduced superoxide anion formation, and down-regulation of the gp91phox subunit of NADPH oxidase, compared with wild-type cells. It was also observed that TG2(-/-) mice exhibited increased neutrophil phagocytic activity, but had attenuated neutrophil chemotaxis and impaired neutrophil extravasation with higher neutrophil counts in their circulation during yeast extract-induced peritonitis. These results clearly suggest that TG2 may modulate the expression of genes related to neutrophil functions and is involved in several intracellular and extracellular functions of extravasating neutrophil.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
AIM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cadaverine,
http://linkedlifedata.com/resource/pubmed/chemical/Cybb protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/DNA,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/NADPH Oxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxides,
http://linkedlifedata.com/resource/pubmed/chemical/Transglutaminases,
http://linkedlifedata.com/resource/pubmed/chemical/monodansylcadaverine,
http://linkedlifedata.com/resource/pubmed/chemical/transglutaminase 2
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| pubmed:status |
MEDLINE
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| pubmed:month |
Sep
|
| pubmed:issn |
0006-4971
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:day |
15
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| pubmed:volume |
108
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
2045-54
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| pubmed:dateRevised |
2006-11-15
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| pubmed:meshHeading |
pubmed-meshheading:16763214-Active Transport, Cell Nucleus,
pubmed-meshheading:16763214-Animals,
pubmed-meshheading:16763214-Base Sequence,
pubmed-meshheading:16763214-Cadaverine,
pubmed-meshheading:16763214-Cell Differentiation,
pubmed-meshheading:16763214-Cell Line, Tumor,
pubmed-meshheading:16763214-Chemotaxis, Leukocyte,
pubmed-meshheading:16763214-DNA,
pubmed-meshheading:16763214-Escherichia coli,
pubmed-meshheading:16763214-GTP-Binding Proteins,
pubmed-meshheading:16763214-Gene Expression Regulation,
pubmed-meshheading:16763214-Granulocytes,
pubmed-meshheading:16763214-Membrane Glycoproteins,
pubmed-meshheading:16763214-Mice,
pubmed-meshheading:16763214-Mice, Knockout,
pubmed-meshheading:16763214-NADPH Oxidase,
pubmed-meshheading:16763214-Neutrophils,
pubmed-meshheading:16763214-Phagocytosis,
pubmed-meshheading:16763214-Superoxides,
pubmed-meshheading:16763214-Transglutaminases
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| pubmed:year |
2006
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| pubmed:articleTitle |
Tissue-transglutaminase contributes to neutrophil granulocyte differentiation and functions.
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| pubmed:affiliation |
Department of Biochemistry and Molecular Biology, University of Debrecen, Medical and Health Science Center, H-4012 Debrecen, Nagyerdei krt. 98, Hungary. zoli@indi.biochem.dote.hu
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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