Abstract
Through differential screening of established human leukaemia cell lines, we have identified and molecularly cloned lymphopain, a novel cysteine proteinase of the papain family. Lymphopain exhibits a remarkably restricted cellular pattern of expression, being predominantly expressed in cytotoxic T-lymphocytes and natural killer cells. The human lymphopain locus maps to chromosome 11q13, encodes a polypeptide of 376 amino acids and is conserved in the mouse. Both human and murine forms appear more closely related to protozoan papain-like enzymes than to other mammalian members of the papain family. The cellular distribution of lymphopain expression, together with the functional demonstration of lymphopain-associated proteinase activity in vitro, is suggestive of a role for lymphopain in immune cell-mediated, cell killing.
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Brown, J., Matutes, E., Singleton, A. et al. Lymphopain, a cytotoxic T and natural killer cell-associated cysteine proteinase. Leukemia 12, 1771–1781 (1998). https://doi.org/10.1038/sj.leu.2401164
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DOI: https://doi.org/10.1038/sj.leu.2401164
