pubmed-article:1670773 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:1670773 | lifeskim:mentions | umls-concept:C0007634 | lld:lifeskim |
pubmed-article:1670773 | lifeskim:mentions | umls-concept:C0596901 | lld:lifeskim |
pubmed-article:1670773 | lifeskim:mentions | umls-concept:C0031676 | lld:lifeskim |
pubmed-article:1670773 | lifeskim:mentions | umls-concept:C0178719 | lld:lifeskim |
pubmed-article:1670773 | lifeskim:mentions | umls-concept:C0103403 | lld:lifeskim |
pubmed-article:1670773 | lifeskim:mentions | umls-concept:C1293122 | lld:lifeskim |
pubmed-article:1670773 | lifeskim:mentions | umls-concept:C1441290 | lld:lifeskim |
pubmed-article:1670773 | pubmed:issue | 2 | lld:pubmed |
pubmed-article:1670773 | pubmed:dateCreated | 1991-2-12 | lld:pubmed |
pubmed-article:1670773 | pubmed:abstractText | Covalently cross-linked multimers of lipocortin I are shown to be present in human epidermoid carcinoma A431 cells treated with epidermal growth factor or the calcium ionophore A23187. This intracellular cross-linking of lipocortin I is suggested to be mediated by the action of tissue transglutaminase, a Ca2(+)-dependent protein cross-linking enzyme. Cross-linking of lipocortin I competes with proteolytic digestion of the protein, and pretreatment of the cells with inhibitors for calpain (Ca2(+)-dependent intracellular protease) markedly enhanced the cross-linking of lipocortin I. Cross-linked lipocortin I is shown to be present in the soluble fraction of A431 cells as well as in the particulate fraction; a 34-kDa fragment of lipocortin I was solubilized successfully by plasmin digestion of the latter fraction. Immunofluorescence microscopy using specific antilipocortin-I antibody showed that cross-linked lipocortin I forms an envelope-like structure, which is not extracted with [ethylenebis(oxyethylenenitrilo)]tetraacetic acid (EGTA) or Triton X-100. In vitro incubation of purified lipocortin I with tissue transglutaminase resulted in the formation of covalently cross-linked lipocortin I dimer, tetramer, and so on. Amine incorporation and cross-linking studies using lipocortin I and its N-terminal truncated derivatives indicated that the cross-linking site is localized within the plasmin-susceptible N-terminal 29 amino acids of lipocortin I. The cross-linking of lipocortin I is shown to be accelerated more than 10 times by the addition of phosphatidylserine vesicles, on which lipocortin I molecules are most likely aligned in a conformation suitable for cross-linking. Collectively, these findings suggest that an increase of intracellular calcium concentration results in the attachment of lipocortin I onto the plasma membrane phospholipids through the C-terminal domain of the molecule where the membrane-bound lipocortin I is cross-linked by the action of tissue transglutaminase through the N-terminal domain. | lld:pubmed |
pubmed-article:1670773 | pubmed:language | eng | lld:pubmed |
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pubmed-article:1670773 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:1670773 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:1670773 | pubmed:month | Jan | lld:pubmed |
pubmed-article:1670773 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:1670773 | pubmed:author | pubmed-author:ImamuraSS | lld:pubmed |
pubmed-article:1670773 | pubmed:author | pubmed-author:AndoYY | lld:pubmed |
pubmed-article:1670773 | pubmed:author | pubmed-author:KannagiRR | lld:pubmed |
pubmed-article:1670773 | pubmed:author | pubmed-author:OwadaM KMK | lld:pubmed |
pubmed-article:1670773 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:1670773 | pubmed:day | 15 | lld:pubmed |
pubmed-article:1670773 | pubmed:volume | 266 | lld:pubmed |
pubmed-article:1670773 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:1670773 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:1670773 | pubmed:pagination | 1101-8 | lld:pubmed |
pubmed-article:1670773 | pubmed:dateRevised | 2005-11-17 | lld:pubmed |
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pubmed-article:1670773 | pubmed:year | 1991 | lld:pubmed |
pubmed-article:1670773 | pubmed:articleTitle | Calcium-induced intracellular cross-linking of lipocortin I by tissue transglutaminase in A431 cells. Augmentation by membrane phospholipids. | lld:pubmed |
pubmed-article:1670773 | pubmed:affiliation | Department of Dermatology, Faculty of Medicine, Kyoto University, Japan. | lld:pubmed |
pubmed-article:1670773 | pubmed:publicationType | Journal Article | lld:pubmed |
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