J. Kamens, M. Paskind, M. Hugunin, R.V. Talanian, H. Allen, D. Banach, N. Bump, M. Hackett, C.G. Johnston, P. Li, J.A. Mankovich, M. Terranova, T. Ghayur, "Identification and characterization of ICH-2, a novel member of the interleukin-1b-converting enzyme family of cysteine proteases," Journal of Biological Chemistry, 270:15250-6, 1995. (Cited in nearly 100 publications through June 1997)
Comments by Joanne Kamens, BASF Bioresearch Corp., Worcester, Mass.
HIGH INTEREST: Joanne Kamens' paper reporting on the ICH-2 gene attracted attention because of caspases' role in cell death. Interleukin-1ß converting enzyme (ICE) was once thought to be a unique enzyme with a single, straightforward function-cleaving the cytokine interleukin-1b into its active form. All that changed in 1993, when a gene in C. elegans involved in apoptosis, called Ced-3, was cloned and found to share extensive homology with ICE. Assigning two separate functions-cytokine processing and apoptosis induction-to these two homologs suggested that ICE was probably ...
