F
Fritz Märki
Researcher at Novartis
Publications - 23
Citations - 1088
Fritz Märki is an academic researcher from Novartis. The author has contributed to research in topics: Phospholipase A2 & Mesangial cell. The author has an hindex of 16, co-authored 23 publications receiving 1071 citations.
Papers
More filters
Journal ArticleDOI
Interleukin 1 and tumor necrosis factor synergistically stimulate prostaglandin synthesis and phospholipase A2 release from rat renal mesangial cells.
TL;DR: Rat glomerular mesangial cells with recombinant human interleukin 1 alpha, rIL-1 alpha or rTNF induces prostaglandin E2 (PGE2) synthesis and the release of a phospholipase A2 (PLA2) activity, which is calcium-dependent and contributes to PGE2 synthesis and PLA2 release.
Journal ArticleDOI
Duramycins B and C, two new lanthionine containing antibiotics as inhibitors of phospholipase A2. Structural revision of duramycin and cinnamycin.
Andreas Fredenhagen,Gabriele Fendrich,Fritz Märki,Walter Märki,Johannes Gruner,Fritz Raschdorf,Heinrich Peter +6 more
TL;DR: Physico-chemical data of these compounds provide evidence for a similar structure for all duramycin antibiotics, and Leucopeptin has been shown to be identical to Duramycin.
Journal ArticleDOI
Interleukin-1β, tumor necrosis factor and forskolin stimulate the synthesis and secretion of group II phospholipase A2 in rat mesangial cells
TL;DR: The results indicate that the increased phospholipase A2 activity upon treatment of mesangial cells with these stimulators is due to increased synthesis of group II phosphate A2, over 85 % of which appears to be secreted from the cells.
Journal ArticleDOI
Endogenous suppression of neutral-active and calcium-dependent phospholipase A2 in human polymorphonuclear leukocytes.
Fritz Märki,Richard C. Franson +1 more
TL;DR: In vitro data indicate that neutral-active and calcium-dependent phospholipase A2 in human polymorphonuclear leukocytes is largely suppressed by endogenous inhibitors and suggest that unsaturated fatty acids and some of their metabolites may partly account for this suppressor activity.
Journal ArticleDOI
Studies on the acyl-chain selectivity of cellular phospholipases A2
TL;DR: Results with human platelet cytosol were highly suggestive for the presence of an arachidonoyl-selective phospholipase A2 when separate phosphatidylcholine species were assayed, but this apparent selectivity was progressively lost when the substrates were mixed or embedded in a membrane of 1-palmitoysl-2-linoleoylphosphatidolcholine.