JCI table of contents, Janua...( ersity of Texas examined whether caspas...)

ersity of Texas examined whether caspase-3 was capable of breaking down actomyosin the essential contractile substance of muscle. In the January 2 issue of the Journal of Clinical Investigation, the authors demonstrate that recombinant caspase-3 cleaves actomyosin resulting in a unique actin fragment and other proteins that are degraded by the ubiquitin-proteasome system. Cleaved actin fragments are present in muscles of rates with muscle atrophy from diabetes or uremia and fragment accumulation and the rate of muscle breakdown could be suppressed by a caspase-3 inhibitor. The report suggests that therapeutic strategies targeting caspase-3 activation may prevent muscle breakdown.

TITLE: Activation of caspase-3 is an initial step triggering accelerated muscle proteolysis in catabolic conditions

AUTHOR CONTACT:
William E. Mitch
University of Texas, Galveston, Texas, USA.
Phone: 409-772-9891
Fax: 409-772-8762
E-mail: wmitch@utmb.edu

View the PDF of this article at: https://www.the-jci.org/press/18330.pdf

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Tumor-suppressing ligand TRAIL may not be so selective after all

Hepatic cell death is the leading cause of fatality in patients with liver diseases, however the molecular pathways underlying this event are unknown. The tumor necrosis factorrelated apoptosis-inducing ligand (TRAIL) holds tremendous promise for cancer therapy because of its ability to selectively cause the programmed cell death (apoptosis) of tumor cells, but not most normal cells. However, some recent studies have cast doubt on this selective activity. In the January 2 issue of the Journal of Clinical Investigation, Youhai Chen and colleagues from the University of Pennsylvania investigated the role of TRAIL in hepatic cell death. Using two experimental models of hepatitis, the
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Contact: Brooke Grindlinger
science_editor@the-jci.org
212-342-9006
Journal of Clinical Investigation
2-Jan-2004

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