| pubmed-article:15038793 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:15038793 | lifeskim:mentions | umls-concept:C0028630 | lld:lifeskim |
| pubmed-article:15038793 | lifeskim:mentions | umls-concept:C0963455 | lld:lifeskim |
| pubmed-article:15038793 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:15038793 | pubmed:issue | Pt 1 | lld:pubmed |
| pubmed-article:15038793 | pubmed:dateCreated | 2004-6-21 | lld:pubmed |
| pubmed-article:15038793 | pubmed:abstractText | Transglutaminases (TGases) are Ca2+-dependent enzymes capable of catalysing transamidation of glutamine residues to form intermolecular isopeptide bonds. Nine distinct TGases have been described in mammals, and two of them (types 2 and 3) are regulated by GTP/ATP. TGase2 hydrolyses GTP and is therefore a bifunctional enzyme. In the present study, we report that TGase5 is also regulated by nucleotides. We have identified the putative TGase5 GTP-binding pocket by comparative amino acid sequence alignment and homology-derived three-dimensional modelling. GTP and ATP inhibit TGase5 cross-linking activity in vitro, and Ca2+ is capable of completely reversing this inhibition. In addition, TGase5 mRNA is not restricted to epidermal tissue, but is also present in different adult and foetal tissues, suggesting a role for TGase5 outside the epidermis. These results reveal the reciprocal actions of Ca2+ and nucleotides with respect to TGase5 activity. Taken together, these results indicate that TGases are a complex family of enzymes regulated by calcium, with at least three of them, namely TGase2, TGase3 and TGase5, also being regulated by ATP and GTP. | lld:pubmed |
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| pubmed-article:15038793 | pubmed:language | eng | lld:pubmed |
| pubmed-article:15038793 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:15038793 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15038793 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15038793 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:15038793 | pubmed:issn | 1470-8728 | lld:pubmed |
| pubmed-article:15038793 | pubmed:author | pubmed-author:MelinoGerryG | lld:pubmed |
| pubmed-article:15038793 | pubmed:author | pubmed-author:ClardyJonJ | lld:pubmed |
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| pubmed-article:15038793 | pubmed:author | pubmed-author:TerrinoniAles... | lld:pubmed |
| pubmed-article:15038793 | pubmed:author | pubmed-author:CandiEleonora... | lld:pubmed |
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| pubmed-article:15038793 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:15038793 | pubmed:day | 1 | lld:pubmed |
| pubmed-article:15038793 | pubmed:volume | 381 | lld:pubmed |
| pubmed-article:15038793 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15038793 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15038793 | pubmed:pagination | 313-9 | lld:pubmed |
| pubmed-article:15038793 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:15038793 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15038793 | pubmed:articleTitle | Transglutaminase 5 is regulated by guanine-adenine nucleotides. | lld:pubmed |
| pubmed-article:15038793 | pubmed:affiliation | Department of Experimental Medicine and Biochemical Sciences, Biochemistry LAb IDI-IRCCS, University of Rome Tor Vergata, via Montpellier 1, 00133 Rome, Italy. | lld:pubmed |
| pubmed-article:15038793 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15038793 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:15038793 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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