| http://purl.uniprot.org/citations/18436303 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/18436303 | http://www.w3.org/2000/01/rdf-schema#comment | "Ca(2+) influx has been shown to be essential for NADPH oxidase activity which is involved in the inflammatory process. Ca(2+) conditions underlying the oxidative response are clearly delineated. Here, we show that store-operated Ca(2+) entry (SOCE) is required at the beginning of NADPH oxidase activation in response to fMLF (N-formyl-L-methionyl-L-leucyl-L-phenylalanine) in neutrophil-like HL-60 cells. When extracellular Ca(2+) is initially removed, early addition of Ca(2+) after stimulation causes a complete restoration of Ca(2+) entry and H(2)O(2) production. Both Ca(2+) entry and H(2)O(2) production are decreased by purported SOCE blockers, 2-aminoethoxydiphenyl borane (2-APB) and SK&F 96365. Endogenously expressed TRPC (transient receptor potential canonical) homologues and Orai1 were investigated for their role in supporting store-operated Ca(2+) channels activity. TRPC1, TRPC6 and Orai1 knock-out by siRNA resulted in the inhibition of Ca(2+) influx and H(2)O(2) production in response to fMLF and thapsigargin while suppression of TRPC3 had no effect on thapsigargin induced-SOCE. 2-APB and SK&F 96365 were able to amplify the reduction of fMLF-stimulated Ca(2+) entry and H(2)O(2) production observed in cells transfected by TRPC3 siRNA. In summary, Ca(2+) influx in HL-60 cells relies on different membrane TRPC channels and Orai1 for allowing NADPH oxidase activation. TRPC3 primarily mediates SOCE-independent pathways and TRPC1, TRPC6 and Orai1 exclusively contribute to SOCE."xsd:string |
| http://purl.uniprot.org/citations/18436303 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.ceca.2008.03.002"xsd:string |
| http://purl.uniprot.org/citations/18436303 | http://purl.uniprot.org/core/author | "Melchior C."xsd:string |
| http://purl.uniprot.org/citations/18436303 | http://purl.uniprot.org/core/author | "Schenten V."xsd:string |
| http://purl.uniprot.org/citations/18436303 | http://purl.uniprot.org/core/author | "Plancon S."xsd:string |
| http://purl.uniprot.org/citations/18436303 | http://purl.uniprot.org/core/author | "Brechard S."xsd:string |
| http://purl.uniprot.org/citations/18436303 | http://purl.uniprot.org/core/author | "Tschirhart E.J."xsd:string |
| http://purl.uniprot.org/citations/18436303 | http://purl.uniprot.org/core/date | "2008"xsd:gYear |
| http://purl.uniprot.org/citations/18436303 | http://purl.uniprot.org/core/name | "Cell Calcium"xsd:string |
| http://purl.uniprot.org/citations/18436303 | http://purl.uniprot.org/core/pages | "492-506"xsd:string |
| http://purl.uniprot.org/citations/18436303 | http://purl.uniprot.org/core/title | "Store-operated Ca2+ channels formed by TRPC1, TRPC6 and Orai1 and non-store-operated channels formed by TRPC3 are involved in the regulation of NADPH oxidase in HL-60 granulocytes."xsd:string |
| http://purl.uniprot.org/citations/18436303 | http://purl.uniprot.org/core/volume | "44"xsd:string |
| http://purl.uniprot.org/citations/18436303 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/18436303 |
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