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- W2070185260 abstract "Rotavirus infection is the leading cause of severe diarrhea in infants and young children worldwide. The rotavirus nonstructural protein NSP4 acts as a viral enterotoxin to induce diarrhea and causes Ca 2+ -dependent transepithelial Cl − secretion in young mice. The cellular basis of this phenomenon was investigated in an in vitro cell line model for the human intestine. Intracellular calcium concentration ([Ca 2+ ] i ) was monitored in fura-2-loaded HT-29 cells using microscope-based fluorescence imaging. NSP4 (1 nM to 5 μM) induced both Ca 2+ release from intracellular stores and plasmalemma Ca 2+ influx. During NSP4-induced [Ca 2+ ] i mobilization, [Na + ] i homeostasis was not disrupted, demonstrating that NSP4 selectively regulated extracellular Ca 2+ entry into these cells. The ED 50 of the NSP4 effect on peak [Ca 2+ ] i mobilization was 4.6 ± 0.8 nM. Pretreatment of cells with either 2.3 × 10 −3 units/ml trypsin or 4.4 × 10 −2 units/ml chymotrypsin for 1–10 min abolished the NSP4-induced [Ca 2+ ] i mobilization. Superfusing cells with U-73122, an inhibitor of phospholipase C, ablated the NSP4 response. NSP4 induced a rapid onset and transient stimulation of inositol 1,4,5-trisphosphate (IP 3 ) production in an IP 3 -specific radioreceptor assay. Taken together, these results suggest that NSP4 mobilizes [Ca 2+ ] i in human intestinal cells through receptor-mediated phospholipase C activation and IP 3 production." @default.
- W2070185260 created "2016-06-24" @default.
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- W2070185260 date "1997-04-15" @default.
- W2070185260 modified "2023-09-26" @default.
- W2070185260 title "The rotavirus enterotoxin NSP4 mobilizes intracellular calcium in human intestinal cells by stimulating phospholipase C-mediated inositol 1,4,5-trisphosphate production" @default.
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- W2070185260 doi "https://doi.org/10.1073/pnas.94.8.3960" @default.
- W2070185260 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/20550" @default.
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