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- W1968710690 abstract "Summary Objective: To assess the reactivity between dipeptidyl peptidase IV (DPP IV) and the α2,3-linked sialic acid of the plasminogen (Pg)Thr 345 O-linked carbohydrate chain as the mechanism enabling plasmin (Pm) to induce intracellular Ca 2+ via DPP IV on rheumatoid synovial fibroblasts, and identify the DPP IV region responsible for this interaction. Methods: Cytosolic Ca 2+ mobilization in rheumatoid synovial fibroblasts was assayed by Digital Imaging Microscopy (DIM). DPP IV was purified by affinity chromatography on an immobilized polysaccharide structurally analogous to the last two residues of the Pg 2 carbohydrate chain. Binding of Pg to DPP IV and identification of the DPP IV reactive site were determined by an enzyme-linked immunosorbent assay (ELISA) and inhibition of Pm-induced intracellular Ca 2+ mobilization in these cells by peptides comprising three regions of DPP IV primary structure. Results: Cytosolic Ca 2+ mobilization induced by Pm on rheumatoid synovial fibroblasts is inhibited by L-lactose, a sugar that interferes with sialic acid binding to lectins. Asialo Pg which binds and can be converted into Pm on the surface of these cells is not able to induce intracellular Ca 2+ mobilization. A peptide comprising the DPP IV primary sequence L 313 QWLRRI inhibits both Pg binding to DPP IV and Pm-induced intracellular Ca 2+ mobilization on these cells. Conclusion: The intracellular Ca 2+ mobilization resulting from the reaction between Pg/Pm and DPP IV is mediated by a lectin-like region in DPP IV. This region is structurally analogous to the sequence (QxW) 3 , previously identified as a carbohydrate-binding region in several lectin families." @default.
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- W1968710690 date "1998-11-01" @default.
- W1968710690 modified "2023-09-26" @default.
- W1968710690 title "Plasmin(ogen) carbohydrate chains mediate binding to dipeptidyl peptidase IV (CD 26) in rheumatoid arthritis human synovial fibroblasts" @default.
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- W1968710690 doi "https://doi.org/10.1016/s0268-9499(98)80395-0" @default.
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