Neutral sphingomyelinase increases the binding, internalization, and degradation of low density lipoproteins and synthesis of cholesteryl ester in cultured human fibroblasts.

@article{Chatterjee1993NeutralSI,
  title={Neutral sphingomyelinase increases the binding, internalization, and degradation of low density lipoproteins and synthesis of cholesteryl ester in cultured human fibroblasts.},
  author={Subroto Chatterjee},
  journal={The Journal of biological chemistry},
  year={1993},
  volume={268 5},
  pages={3401-6}
}
I have investigated the effects of human urinary neutral sphingomyelinase (N-SMase) (Chatterjee, S., and Ghosh, N. (1989) J. Biol. Chem. 264, 12554-12561) on the cell-surface binding, internalization, and degradation of 125I-low density lipoprotein (LDL) and on cholesteryl ester synthesis in cultured human fibroblasts. N-SMase exerted a concentration-dependent continuous stimulation of 125I-LDL cell-surface binding, internalization, and degradation in normal human fibroblasts. A 3-fold increase… CONTINUE READING