| pubmed-article:14630574 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14630574 | lifeskim:mentions | umls-concept:C0086418 | lld:lifeskim |
| pubmed-article:14630574 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
| pubmed-article:14630574 | lifeskim:mentions | umls-concept:C0027950 | lld:lifeskim |
| pubmed-article:14630574 | lifeskim:mentions | umls-concept:C0031308 | lld:lifeskim |
| pubmed-article:14630574 | lifeskim:mentions | umls-concept:C0013878 | lld:lifeskim |
| pubmed-article:14630574 | lifeskim:mentions | umls-concept:C0021027 | lld:lifeskim |
| pubmed-article:14630574 | lifeskim:mentions | umls-concept:C0205307 | lld:lifeskim |
| pubmed-article:14630574 | lifeskim:mentions | umls-concept:C1155437 | lld:lifeskim |
| pubmed-article:14630574 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:14630574 | pubmed:dateCreated | 2003-11-21 | lld:pubmed |
| pubmed-article:14630574 | pubmed:abstractText | The aim of this study was to investigate the effects of elevated glucose concentrations on complement receptor- and Fcgamma receptor-mediated phagocytosis in normal human neutrophils. D-Glucose at 15 or 25 mM dose-dependently inhibited both complement receptor- and Fcgamma receptor-mediated phagocytosis, as compared to that at a normal physiological glucose concentration. The protein kinase C (PKC) inhibitors GF109203X and Go6976 both dose-dependently and completely reversed the inhibitory effect of 25 mM D-glucose on phagocytosis. Complement receptor-mediated phagocytosis was dose-dependently inhibited by the cell permeable diacylglycerol analogue 1,2-dioctanoyl-sn-glycerol (DAG), an effect that was abolished by PKC inhibitors. Furthermore, suboptimal inhibitory concentrations of DAG and glucose showed an additive inhibitory effect on complement receptor-mediated phagocytosis. The authors conclude that elevated glucose concentrations can inhibit complement receptor and Fcgamma receptor-mediated phagocytosis in normal human neutrophils by activating PKCalpha and/or PKCbeta, an effect possibly mediated by DAG. | lld:pubmed |
| pubmed-article:14630574 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14630574 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14630574 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14630574 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14630574 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14630574 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14630574 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14630574 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14630574 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14630574 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14630574 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14630574 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14630574 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14630574 | pubmed:issn | 1543-8600 | lld:pubmed |
| pubmed-article:14630574 | pubmed:author | pubmed-author:OldenborgPer-... | lld:pubmed |
| pubmed-article:14630574 | pubmed:author | pubmed-author:SehlinJanoveJ | lld:pubmed |
| pubmed-article:14630574 | pubmed:author | pubmed-author:SaiepourDanie... | lld:pubmed |
| pubmed-article:14630574 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14630574 | pubmed:volume | 4 | lld:pubmed |
| pubmed-article:14630574 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14630574 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14630574 | pubmed:pagination | 125-32 | lld:pubmed |
| pubmed-article:14630574 | pubmed:dateRevised | 2008-11-20 | lld:pubmed |
| pubmed-article:14630574 | pubmed:meshHeading | pubmed-meshheading:14630574... | lld:pubmed |
| pubmed-article:14630574 | pubmed:meshHeading | pubmed-meshheading:14630574... | lld:pubmed |
| pubmed-article:14630574 | pubmed:meshHeading | pubmed-meshheading:14630574... | lld:pubmed |
| pubmed-article:14630574 | pubmed:meshHeading | pubmed-meshheading:14630574... | lld:pubmed |
| pubmed-article:14630574 | pubmed:meshHeading | pubmed-meshheading:14630574... | lld:pubmed |
| pubmed-article:14630574 | pubmed:meshHeading | pubmed-meshheading:14630574... | lld:pubmed |
| pubmed-article:14630574 | pubmed:meshHeading | pubmed-meshheading:14630574... | lld:pubmed |
| pubmed-article:14630574 | pubmed:meshHeading | pubmed-meshheading:14630574... | lld:pubmed |
| pubmed-article:14630574 | pubmed:meshHeading | pubmed-meshheading:14630574... | lld:pubmed |
| pubmed-article:14630574 | pubmed:meshHeading | pubmed-meshheading:14630574... | lld:pubmed |
| pubmed-article:14630574 | pubmed:meshHeading | pubmed-meshheading:14630574... | lld:pubmed |
| pubmed-article:14630574 | pubmed:meshHeading | pubmed-meshheading:14630574... | lld:pubmed |
| pubmed-article:14630574 | pubmed:articleTitle | Hyperglycemia-induced protein kinase C activation inhibits phagocytosis of C3b- and immunoglobulin g-opsonized yeast particles in normal human neutrophils. | lld:pubmed |
| pubmed-article:14630574 | pubmed:affiliation | Department of Integrative Medical Biology, Section for Histology and Cell Biology, Umeå University, Umeå, Sweden. | lld:pubmed |
| pubmed-article:14630574 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14630574 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
