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Molecular Cloning and Characterization of Two Novel Pro-apoptotic Isoforms of Caspase-10
Ist Teil von
The Journal of biological chemistry, 1999-04, Vol.274 (15), p.10301-10308
Ort / Verlag
United States: American Society for Biochemistry and Molecular Biology
Erscheinungsjahr
1999
Link zum Volltext
Quelle
Free E-Journal (出版社公開部分のみ)
Beschreibungen/Notizen
Caspase-10/a (Mch4) and caspase-10/b (FLICE2) are related death effector domain-containing cysteine aspartases presumed to
be at or near the apex of apoptotic signaling pathways. We report the cloning and characterization of two novel proteins that
are splice isoforms of the caspase-10 family. Caspase-10/c is a truncated protein that is essentially a prodomain-only form
of the caspase that lacks proteolytic activity in vitro but efficiently induces the formation of perinuclear filamentous structures and cell death in vivo . Caspase-10/c mRNA is specifically up-regulated upon TNF stimulation, suggesting a potential role of this isoform in amplifying
the apoptotic response to extracellular stimuli such as cytokines. Caspase-10/d is a hybrid of the known caspases Mch4 and
FLICE2, as it is identical to FLICE2 except for the small (p12) catalytic subunit, which is identical to Mch4. Caspase-10/d
is proteolytically active in vitro and also induces cell death in vivo , although it is less active than Mch4. The mRNAs for all known isoforms of caspase-10 are abundantly expressed in fetal lung,
kidney, and skeletal muscle but are very poorly expressed or absent in these tissues in the adult, implying a possible role
for the caspase-10 family in fetal development.