Secretory sphingomyelinase, a product of the acid sphingomyelinase gene, can hydrolyze atherogenic lipoproteins at neutral pH. Implications for atherosclerotic lesion development.

@article{Schissel1998SecretorySA,
  title={Secretory sphingomyelinase, a product of the acid sphingomyelinase gene, can hydrolyze atherogenic lipoproteins at neutral pH. Implications for atherosclerotic lesion development.},
  author={S L Schissel and Xuejun Jiang and J Tweedie-Hardman and Ts Jeong and E H Camejo and Jamila Najib and Joseph H. Rapp and Kevin J. Williams and Ira Tabas},
  journal={The Journal of biological chemistry},
  year={1998},
  volume={273 5},
  pages={2738-46}
}
The subendothelial aggregation and retention of low density lipoprotein (LDL) are key events in atherogenesis, but the mechanisms in vivo are not known. Previous studies have shown that treatment of LDL with bacterial sphingomyelinase (SMase) in vitro leads to the formation of lesion-like LDL aggregates that become retained on extracellular matrix and stimulate macrophage foam cell formation. In addition, aggregated human lesional LDL, but not unaggregated lesional LDL or plasma LDL, shows… CONTINUE READING
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