![Sample our Medicine, Dentistry, Nursing & Allied Health journals, sign in here to start your FREE access for 14 days]({"type":"image" , "src" : "/sda/5944/TOC-Subject-Sample-2021-Medicine-Dentistry-Nursing-Allied-Health.jpg"})
Abstract
Kald B, Boll R-M, Gustafson-Svärd C, Sjödahl R, Tagesson C. Phospholipase C from Clostridium perfringens stimulates acetyltransferase-dependent formation of platelet-activating factor in cultured intestinal epithelial cells (INT 407). Scand J Gastroenterol 1994;29:243-247.
The mechanisms by which phospholipase C from Clostridium perfringens stimulates the formation of platelet-activating factor (PAF-acether) in cultured intestinal epithelial cells (INT 407) were investigated. Although stimulation with phospholipase C caused a significant formation of PAF-acether, there was no significant increase in the cellular levels of lysoPAF-acether after stimulation. Moreover, when cells prelabeled with 3H-l-0-alkyl-2-acyl-sn-glycerophosphocholine were stimulated with phospholipase C, the 3H-lysoPAF-acether content was not increased in stimulated cells as compared with unstimulated cells. When cells were preincubated with the calmodulin inhibitor trifluoperazine (TFPA), the protein kinase C inhibitor l-(5-isoquinolinylsulfonyl)-2-methylpiperazine (H-7), or the combined phospholipase A2-inhibitor and lipoxygenase inhibitor nordihydroguaiaretic acid (NDGA) before stimulation with phospholipase C, the PAF-acether formation was significantly decreased. The phospholipase A2 inhibitor 4-bromophenacyl bromide (BPB), on the other hand, had no significant effect on the PAF-acether formation. Preincubation with NDGA also decreased the levels of lysoPAF-acether, whereas BPB. H7, or TFPA had no such effect. These findings indicate that stimulation of acetyltransferase activity with increased acetylation of lysoPAF-acether may be one way by which phospholipase C from C. perfringens stimulates formation of PAF-acether in INT 407 cells.