Abnormal laminin secretion from parietal endoderm-like F9 cells in the presence of monensin.
We studied the effects of monensin on post-translational modification and intracellular transport of precursors of laminin subunits in parietal endoderm-like F9 cells. At concentrations higher than 0.1 microM, monensin inhibited the processing of high-mannose type precursors for all three subunits and caused their cytoplasmic accumulation. Furthermore, the secretion of mature subunits of laminin was inhibited. Instead, polypeptides with similar molecular weights to those of intracellular precursors were secreted. These polypeptides were immunologically related to laminin subunits and were sensitive to digestion with beta-N-acetylglucosaminidase H (Endo H). This indicated that Golgi complexes of the cells can transport the precursors of laminin subunits even with their terminal glycosylation inactivated by monensin. Tunicamycin induced the accumulation of unglycosylated precursors and strongly reduced their secretion into the medium.
D000818:Animals; D000936:Antigen-Antibody Complex; D002454:Cell Differentiation; D002460:Cell Line; D004707:Endoderm; D005663:Furans / Q000494:pharmacology*; D007106:Immune Sera; D007797:Laminin / Q000302:isolation & purification / Q000378:metabolism*; D051379:Mice; D008970:Molecular Weight; D008985:Monensin / Q000494:pharmacology*; D009363:Neoplasm Proteins / Q000302:isolation & purification / Q000378:metabolism; D013724:Teratoma / Q000378:metabolism
D000936:Antigen-Antibody Complex; D005663:Furans; D007106:Immune Sera; D007797:Laminin; D009363:Neoplasm Proteins; D008985:Monensin