| pubmed-article:16763214 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:16763214 | lifeskim:mentions | umls-concept:C0027950 | lld:lifeskim |
| pubmed-article:16763214 | lifeskim:mentions | umls-concept:C0542341 | lld:lifeskim |
| pubmed-article:16763214 | lifeskim:mentions | umls-concept:C1326082 | lld:lifeskim |
| pubmed-article:16763214 | lifeskim:mentions | umls-concept:C1880177 | lld:lifeskim |
| pubmed-article:16763214 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:16763214 | pubmed:dateCreated | 2006-9-7 | lld:pubmed |
| pubmed-article:16763214 | 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. | lld:pubmed |
| pubmed-article:16763214 | pubmed:language | eng | lld:pubmed |
| pubmed-article:16763214 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16763214 | pubmed:citationSubset | AIM | lld:pubmed |
| pubmed-article:16763214 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16763214 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16763214 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16763214 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16763214 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16763214 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16763214 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16763214 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16763214 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16763214 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:16763214 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:16763214 | pubmed:month | Sep | lld:pubmed |
| pubmed-article:16763214 | pubmed:issn | 0006-4971 | lld:pubmed |
| pubmed-article:16763214 | pubmed:author | pubmed-author:LanotteMichel... | lld:pubmed |
| pubmed-article:16763214 | pubmed:author | pubmed-author:VámosiGyörgyG | lld:pubmed |
| pubmed-article:16763214 | pubmed:author | pubmed-author:FésüsLászlóL | lld:pubmed |
| pubmed-article:16763214 | pubmed:author | pubmed-author:SzántóAttilaA | lld:pubmed |
| pubmed-article:16763214 | pubmed:author | pubmed-author:BalajthyZoltá... | lld:pubmed |
| pubmed-article:16763214 | pubmed:author | pubmed-author:CsomósKriszti... | lld:pubmed |
| pubmed-article:16763214 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:16763214 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:16763214 | pubmed:volume | 108 | lld:pubmed |
| pubmed-article:16763214 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:16763214 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:16763214 | pubmed:pagination | 2045-54 | lld:pubmed |
| pubmed-article:16763214 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
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| pubmed-article:16763214 | pubmed:year | 2006 | lld:pubmed |
| pubmed-article:16763214 | pubmed:articleTitle | Tissue-transglutaminase contributes to neutrophil granulocyte differentiation and functions. | lld:pubmed |
| pubmed-article:16763214 | 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 | lld:pubmed |
| pubmed-article:16763214 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:16763214 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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