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- W2313630186 abstract "The stimulation of human epidermoid carcinoma A431 cells with the calcium ionophore A23187 resulted in the formation of high-molecular-weight lipocortins I, having apparent molecular weights of 75 kDa and 160 kDa as detected with specific anti-lipocortin I antibody. These immunoreactive proteins were identified to be covalently cross-linked multimers of lipocortin I, since essentially the same cross-linked multimers were observed when purified lipocortin I was incubated with tissue transglutaminase (TGase)in vitro. Classical amine substrates for TGase, such as dansylcadaverine and putrescine, were also incorporated stoichiometrically into lipocortin I. Cross-linking or amine incorporation was not observed with lipocortin II. Des 1–26 lipocortin I did not serve as a substrate for TGase, indicating that the N-terminal region of lipocortin I plays an important role in the formation of lipocortin I multimers. The cross-linking of lipocortin I by TGase resulted in a remarkable enhancement of calcium sensitivity for phospholipid binding;i.e., the free calcium concentration required for the cross-linked lipocortin I to attain 50% maximal binding to phosphatidylserine vesicles was as little as 3 μM, while that required for intact monomeric lipocortin I was 20 μM." @default.
- W2313630186 created "2016-06-24" @default.
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- W2313630186 date "1992-04-01" @default.
- W2313630186 modified "2023-10-18" @default.
- W2313630186 title "Detection of lipocortin I in osteoblastic cells" @default.
- W2313630186 doi "https://doi.org/10.1016/0169-6009(92)92128-d" @default.
- W2313630186 hasPublicationYear "1992" @default.
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