Apaf-1, a human protein homologous to C. elegans CED-4, participates in cytochrome c-dependent activation of caspase-3

Article Abstract:

Research work has been undertaken into the purification, cDNA cloning and characterization of Apaf-1, a 130 kd protein from HeLa cell cytosol. This protein plays a role in the cytochrome c-dependent activation of caspase-3. Activated caspase-3 will cleave and activate the 45 kd subunit of DNA fragmentation factor, which subsequently prompts the degradation of DNA in nucleosomal fragments. There is evidence to suggest that Apaf-1 may be the mammalian homolog of CED-4. It does not appear to be a caspase itself.

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Hibernation proteins: Preparing for life in the freezer

Article Abstract:

Hibernation is an extreme response to a seasonal environment, yet nothing about how it is timed or how vital cellular functions are sustained in the face of plummeting body temperature is known. A liver-derived protein complex is identified as an essential coordinator of this adaptation to the depredations of winter.

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Life, Sex, and WT1 isoforms--three amino acids can make all the difference

Article Abstract:

Results point out that the Wilms' tumor suppresor gene, WT1, encodes upto 24 protein isoforms through a combination of alternative splicing, translational start sites, and RNA editing. Two alternative splice products with only three amino acid difference between them exhibit different biologcal functions.

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