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Studies on the mechanisms of TNP-LPS-induced enhancement of MOPC-315 cell secretory differentiation

Conference · · Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
OSTI ID:7024782
The author previously reported that incubation of MOPC-315 cells in vitro for 48 hours with 0.01 ..mu..g/ml of TNP-LPS induced enhanced MOPC-315 cell secretory differentiation. He now reports that MOPC-315 cells become committed to enhanced secretory differentiation during the first 2 hours of TNP-LPS exposure. This commitment can be blocked by including the phospholipid methylation inhibitor 2-hydroxyethylhydrazine (2-HEH) in the TNP-LPS culture during the first 30 minutes. Inclusion of the serine protease inhibitor diisopropylfluorophosphate (DFP) in the TNP-LPS culture for the first 2 hours also blocks commitment to enhanced 315 cell PFC frequency. A serine protease is activated by the TNP-LPS exposure since 315 cells cultured with DFP before, but not during, TNP-LPS culture still show normal TNP-LPS enhancement. Phospholipid methylation is required for serine protease activation since incubation of the cells with 2-HEH for 30 minutes blocks the enhanced accumulation of /sup 3/H-DFP usually seen at 2 hours of TNP-LPS culture. The TNP-LPS-induced serine protease is specific for lysine since lysine analogs, but not other amino acid analogs, block TNP-LPS-induced enhancement. Protein kinase C is not required for this enhancement since inclusion of the protein kinase C inhibitor, into the TNP-LPS culture does not inhibit the enhancement of MOPC-315 PFC frequency.
Research Organization:
Univ. of South Alabama College of Medicine, Mobile
OSTI ID:
7024782
Report Number(s):
CONF-8604222-
Conference Information:
Journal Name: Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States) Journal Volume: 45:4
Country of Publication:
United States
Language:
English