| pubmed-article:8104938 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8104938 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
| pubmed-article:8104938 | lifeskim:mentions | umls-concept:C0524637 | lld:lifeskim |
| pubmed-article:8104938 | lifeskim:mentions | umls-concept:C0030956 | lld:lifeskim |
| pubmed-article:8104938 | lifeskim:mentions | umls-concept:C1521761 | lld:lifeskim |
| pubmed-article:8104938 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
| pubmed-article:8104938 | lifeskim:mentions | umls-concept:C1149592 | lld:lifeskim |
| pubmed-article:8104938 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:8104938 | pubmed:issue | 28 | lld:pubmed |
| pubmed-article:8104938 | pubmed:dateCreated | 1993-11-24 | lld:pubmed |
| pubmed-article:8104938 | pubmed:abstractText | Factor XIIIa is a transglutaminase that catalyzes intermolecular gamma-glutamyl-epsilon-lysyl bonds between fibrin and other proteins involved in hemostasis. We synthesized 25 peptides from various regions of factor XIIIa and studied their effects on cross-linking fibrin, N,N'-dimethylcasein, or fibronectin. We found that two peptides, Asn72-Asp97 (peptide-4) and Asp190-Phe230 (peptide-7), inhibited factor XIIIa cross-linking of these substrates. The other peptides did not inhibit factor XIIIa activity. The inhibition of cross-linking was reversed by excess substrate, indicating that the peptides were interacting with fibrin and not factor XIIIa. The peptides were not pseudosubstrates since they were not cross-linked to fibrin. The peptides did not modify the primary amine binding site as increasing the primary amine concentration did not reverse inhibition. Peptides-4 and -7 also had no effect on exposure of the active site of factor XIIIa and no synergistic inhibitory effects were detected. Peptides-4 and -7 had no effect on factor XIIIa binding to fibrin suggesting that the binding sites and the substrate recognition sites were distinct. Synthetic peptides containing shorter amino acid sequences of peptide-4 were inactive. In contrast, the amino-terminal (Asp190-Lys199, Tyr194-Tyr204) and the carboxyl-terminal (Lys221-Phe230) portions of peptide-7 were 20-60-fold less inhibitory compared to intact peptide-7. Peptides-4 and -7 also inhibited guinea pig liver tissue transglutaminase from cross-linking fibrinogen, N,N'-dimethylcasein, and fibronectin. In conclusion, we have identified two regions outside the active site pocket which are important for substrate recognition in factor XIIIa and tissue transglutaminase. | lld:pubmed |
| pubmed-article:8104938 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8104938 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8104938 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8104938 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8104938 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8104938 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8104938 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8104938 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8104938 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8104938 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8104938 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8104938 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8104938 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8104938 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8104938 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8104938 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8104938 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8104938 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:8104938 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:8104938 | pubmed:author | pubmed-author:GreenbergC... | lld:pubmed |
| pubmed-article:8104938 | pubmed:author | pubmed-author:AchyuthanK... | lld:pubmed |
| pubmed-article:8104938 | pubmed:author | pubmed-author:SlaughterT... | lld:pubmed |
| pubmed-article:8104938 | pubmed:author | pubmed-author:EnghildJ JJJ | lld:pubmed |
| pubmed-article:8104938 | pubmed:author | pubmed-author:SantiagoM AMA | lld:pubmed |
| pubmed-article:8104938 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8104938 | pubmed:day | 5 | lld:pubmed |
| pubmed-article:8104938 | pubmed:volume | 268 | lld:pubmed |
| pubmed-article:8104938 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8104938 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8104938 | pubmed:pagination | 21284-92 | lld:pubmed |
| pubmed-article:8104938 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:8104938 | pubmed:meshHeading | pubmed-meshheading:8104938-... | lld:pubmed |
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| pubmed-article:8104938 | pubmed:meshHeading | pubmed-meshheading:8104938-... | lld:pubmed |
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| pubmed-article:8104938 | pubmed:meshHeading | pubmed-meshheading:8104938-... | lld:pubmed |
| pubmed-article:8104938 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8104938 | pubmed:articleTitle | Factor XIIIa-derived peptides inhibit transglutaminase activity. Localization of substrate recognition sites. | lld:pubmed |
| pubmed-article:8104938 | pubmed:affiliation | Department of Medicine, Duke University Medical Center, Durham, North Carolina 27710. | lld:pubmed |
| pubmed-article:8104938 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8104938 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8104938 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8104938 | lld:pubmed |
