Chromosome 1 open reading frame 41 Function

Small Heat Shock Protein
    Based on BLAST result, our protein target (human 1tvg) showed the best similarity and homology with heat shock protein family B-small (human hspf; NP_057210.2), thus they may have a similar function.  Some articles about HSPB11 suggest that small heat shock protein play in the role of cancer development. Hsp functionally has anti apoptotic activity, which if over expressed lead to tumor growth and resistance to chemo or radiotherapy ( Bellyei et al., 2006; Pozsgai et al., 2007).  The anti apoptotic effect of hsp is mediated by the activation of Hsp90 (which Hsp16.2 binds with) and by the activation of PI-3 kinase-Akt pathway. Pozsgai et al. (2007) research data suggest that there is correlation between the progressive cytoplasmic expressions of small Hsp and brain tumor malignancy.
    Note from Bellyei et al, 2006 about sHsp. Small hsps known to has chaperone function to prevent protein aggregation induced by thermal and chemical stress. sHsp family is characterized as conserved C-terminal domain of about 90 amino acids, the α crystalline domain, and a variable N terminal domain. Small hsp is considered as ATP-independent chaperones, it not involves in regulating protein folding. However, under cellular stress it will prevent aggregation and precipitation of protein by interact with and stabilize that targeted protein. sHsp monomer mass between 12-43 kDa and create oligomeric structures of 12-24 subunits (some even up to 50 units).