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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Relationship between soluble intracellular endothelin-converting enzyme and endothelin-1 synthesis: effect of inhibitors of the secretory pathway.

The relationship between soluble and membrane-bound endothelin-converting enzyme ( ECE) activity with the level of endothelin-1 (ET-1) synthesis was investigated in cultured endothelial cells. Escherichia coli lipopolysaccharide (LPS) was used to stimulate ET-1 synthesis, and brefeldin A, monensin, colchicine or cytochalasin B, which disrupt peptide biosynthetic pathways in a variety of ways, were tested for their ability to modify changes in ET-1 synthesis and ECE levels. LPS increased ET-1 secretion by more than twofold. Levels of soluble ECE activity, but not those of membrane-bound ECE activity, correlated with ET-1 synthesis. These results suggest the soluble ECE activity is likely to play a role in ET-1 biosynthesis.[1]

References

  1. Relationship between soluble intracellular endothelin-converting enzyme and endothelin-1 synthesis: effect of inhibitors of the secretory pathway. Corder, R., Khan, N.Q., Harrison, V.J., Wood, E.G., Lees, D.M., Barker, S. J. Cardiovasc. Pharmacol. (2000) [Pubmed]
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