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Mch3, a Novel Human Apoptotic Cysteine Protease Highly Related to CPP32¹

Departments of Pharmacology [T. F-A., L. W., G. L., E. S. A.] and Microbiology and Immunology [Z. Y., C. M. C.], Jefferson Cancer Institute, Jefferson Medical College, Philadelphia, Pennsylvania 19107; Department of Cell Biology and Anatomy, Johns Hopkins School of Medicine, Baltimore, Maryland 21205 [A. T., W. C. E.]; Cell Biology Section, IDUN Pharmaceuticals, San Diego, California 92121 [R. A., J. K., L. F., K. J. T.]; and Department of Pathology, Duke University Medical School, Durham, North Carolina 27710 [G. S.]

Recent evidence suggests that mammalian cysteine proteases related to Caenorhabditis elegans CED-3 are key components of mammalian programmed cell death or apoptosis. We have shown recently that the CPP32 and Mch2 cysteine proteases cleave the apoptotic markers poly(ADP-ribose) polymerase (PARP) and lamins, respectively. Here we report the cloning of a new Ced-3/interleukin 1ß-converting enzyme-related gene, designated Mch3, that encodes a protein with the highest degree of homology to CPP32 compared to other family members. An alternatively spliced isoform, named Mch3ß, was also identified. Bacterially expressed recombinant Mch3 has intrinsic autocatalytic/autoactivation activity. The specific activity of Mch3 toward the peptide substrate DEVD-7-amino-4-methylcoumarin and PARP resembles that of CPP32. Like interleukin 1ß-converting enzyme and CPP32, the active Mch3 is made of two subunits derived from a precursor (proMch3). It was of interest that recombinant CPP32-p17 subunit can form an active heteromeric enzyme complex with recombinant Mch3-p12 subunit and vice versa, as determined by the ability of the heteromeric complexes to induce apoptosis in Sf9 cells. These data suggest that proMch3 and proCPP32 can interact to form an active Mch3/CPP32 heteromeric complex. We also provide evidence that CPP32 can efficiently cleave proMch3, but not the opposite, suggesting that Mch3 activation in vivo may depend in part on CPP32 activity. The high degree of conservation in structure and specific activity and the coexistence of Mch3 and CPP32 in the same cell suggests that the PARP cleavage activity observed during apoptosis cannot solely be attributed to CPP32 but could also be an activity of Mch3.

¹ This work was supported in part by a grant from IDUN Pharmaceuticals to (E. S. A.), by Grant AI 35035-01 from NIH (to G. L.), and by Grant CA69008 from NIH (to W. C. E.).

² To whom requests for reprints should be addressed, at Department of Pharmacology, Jefferson Medical College, Bluemle Life Sciences Building, 233 South 10th Street, Philadelphia, PA 19107. Phone: (215) 955-4632; Fax: (215) 923-1098; E-mail: E_Alnemri@lac.jci.tju.edu.

Received 9/29/95. Accepted 10/27/95.

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