J
Johan F. Koster
Researcher at Erasmus University Rotterdam
Publications - 128
Citations - 5415
Johan F. Koster is an academic researcher from Erasmus University Rotterdam. The author has contributed to research in topics: Pyruvate kinase & Lipid peroxidation. The author has an hindex of 38, co-authored 128 publications receiving 5349 citations.
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Iron mobilization from ferritin by superoxide derived from stimulated polymorphonuclear leukocytes. Possible mechanism in inflammation diseases.
TL;DR: It is reported that stimulated polymorphonuclear leukocytes mobilize iron from human and horse ferritin, but not from human transferrin, and it is proposed that this reaction may potentiate the formation of the OH.
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P38 Mitogen Activated Protein Kinase Regulates Endothelial VCAM-1 Expression at the Post-transcriptional Level
Anneke Pietersma,B. C. Tilly,Matthias Gaestel,N. De Jong,J C Lee,Johan F. Koster,Wim Sluiter +6 more
TL;DR: The cytokine tumor necrosis factor (TNF) alpha was found to stimulate the p38 mitogen activated protein (MAP) kinase signalling cascade in human umbilical vein endothelial cells, and VCAM-1 mRNA accumulation induced by TNFalpha was not affected by SB203580, suggesting that the p37 MAP kinase signaling cascade regulates the endothelial expression of VCam-1 at the post-transcriptional level.
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Superoxide-dependent and -independent mechanisms of iron mobilization from ferritin by xanthine oxidase. Implications for oxygen-free-radical-induced tissue destruction during ischaemia and inflammation.
TL;DR: The O2(-)-produced by xanthine oxidase, or granulocytes, will be converted by 'free' iron into much more highly toxic oxygen species such as hydroxyl radicals (OH.), exacerbating the tissue damage.
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Superoxide dependent iron release from ferritin in inflammatory diseases
TL;DR: Evidence is presented that oxygen free radicals are involved in the pathogenesis of rheumatoid arthritis (RA), and superoxide is able to release iron from ferritin, providing a suitable source of iron, for the formation of hydroxyl radicals.
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Possible involvement of the lipid-peroxidation product 4-hydroxynonenal in the formation of fluorescent chromolipids
TL;DR: The findings suggest that the fluorescent chromolipids formed by lipid peroxidation are not derived from malonaldehyde, but are formed from 4-hydroxynonenal or similar reactive aldehydes via a NADPH and/or ADP-iron-catalysed reaction with phosphatidylethanolamine and phosphatodylserine contained in the membrane.