Purification of cachectin, a lipoprotein lipase-suppressing hormone secreted by endotoxin-induced RAW 264.7 cells

@article{Beutler1985PurificationOC,
  title={Purification of cachectin, a lipoprotein lipase-suppressing hormone secreted by endotoxin-induced RAW 264.7 cells},
  author={Bruce Beutler and John R. Mahoney and N Le Trang and Phillip H. Pekala and Anthony Cerami},
  journal={The Journal of Experimental Medicine},
  year={1985},
  volume={161},
  pages={984 - 995}
}
Previous studies have indicated that endotoxin and other bacterial and protozoal products can stimulate macrophages to produce a factor that can suppress the activity of the enzyme lipoprotein lipase (LPL), in vivo and in vitro. In the present report we describe the purification of this factor, cachectin, to apparent homogeneity from the conditioned medium of endotoxin-stimulated RAW 264.7 cells. The isolated protein has an isoelectric point of 4.7 and a subunit molecular weight of 17,000… CONTINUE READING

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Lipopolysaccharide - treated RAW 264 . 7 cells produce a mediator which inhibits lipoprotein lipase in 3 T 3L 1 cells

  • A. Cerami
  • 1985

Lipopolysaccharide-treated RAW 264.7 cells produce a mediator which inhibits lipoprotein lipase in 3T3-L1 cells.J, lmmunol

  • J. R. Mahoney, B. A. Beutler, +4 authors BEUTLER
  • 1985
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