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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2001-3-22
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pubmed:abstractText |
S100 proteins are a family of 10-14 kDa EF-hand-containing calcium binding proteins that function to transmit calcium-dependent cell regulatory signals. S100 proteins have no intrinsic enzyme activity but bind in a calcium-dependent manner to target proteins to modulate target protein function. Transglutaminases are enzymes that catalyze the formation of covalent epsilon-(gamma-glutamyl)lysine bonds between protein-bound glutamine and lysine residues. In the present study we show that transglutaminase-dependent covalent modification is a property shared by several S100 proteins and that both type I and type II transglutaminases can modify S100 proteins. We further show that the reactive regions are at the solvent-exposed amino- and carboxyl-terminal ends of the protein, regions that specify S100 protein function. We suggest that transglutaminase-dependent modification is a general mechanism designed to regulate S100 protein function.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Annexins,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamine,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Putrescine,
http://linkedlifedata.com/resource/pubmed/chemical/S100 Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/S100A11 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/S100A7 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Transglutaminases,
http://linkedlifedata.com/resource/pubmed/chemical/transglutaminase 2
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pubmed:status |
MEDLINE
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pubmed:month |
Mar
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pubmed:issn |
0006-2960
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
13
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pubmed:volume |
40
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3167-73
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:11258932-3T3 Cells,
pubmed-meshheading:11258932-Animals,
pubmed-meshheading:11258932-Annexins,
pubmed-meshheading:11258932-Calcium,
pubmed-meshheading:11258932-Calcium-Binding Proteins,
pubmed-meshheading:11258932-Cells, Cultured,
pubmed-meshheading:11258932-Epidermis,
pubmed-meshheading:11258932-GTP-Binding Proteins,
pubmed-meshheading:11258932-Glutamine,
pubmed-meshheading:11258932-Humans,
pubmed-meshheading:11258932-Keratinocytes,
pubmed-meshheading:11258932-Lysine,
pubmed-meshheading:11258932-Mice,
pubmed-meshheading:11258932-Psoriasis,
pubmed-meshheading:11258932-Putrescine,
pubmed-meshheading:11258932-S100 Proteins,
pubmed-meshheading:11258932-Substrate Specificity,
pubmed-meshheading:11258932-Swine,
pubmed-meshheading:11258932-Transglutaminases
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pubmed:year |
2001
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pubmed:articleTitle |
S100A7, S100A10, and S100A11 are transglutaminase substrates.
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pubmed:affiliation |
Department of Physiology and Biophysics, Case Western Reserve University School of Medicine, 2109 Adelbert Road, Cleveland, Ohio 44106-4970, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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