ArticleBMB reports2013
C-terminal truncation of a bovine B(12) trafficking chaperone enhances the sensitivity of the glutathione-regulated thermostability.
Article in BMB reports, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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Who cites it
4 citing papers in PubMed, 5 citations in OpenAlex.
- The cobalamin processing enzyme of Trichoplax adhaerens.The Journal of biological chemistry · 2025Article
- Regulation of GlutathioneInternational journal of molecular sciences · 2024Article
- Inhibition of glutathione S-transferase omega 1-catalyzed protein deglutathionylation suppresses adipocyte differentiation.BMB reports · 2023Article
- Identification of anti-adipogenic proteins in adult bovine serum suppressing 3T3-L1 preadipocyte differentiation.BMB reports · 2013Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
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Abstract
The human B(12) trafficking chaperone hCblC is well conserved in mammals and non-mammalian eukaryotes. However, the C-terminal ~40 amino acids of hCblC vary significantly and are predicted to be deleted by alternative splicing of the encoding gene. In this study, we examined the thermostability of the bovine CblC truncated at the C-terminal variable region (t-bCblC) and its regulation by glutathione. t-bCblC is highly thermolabile (T(m) = ~42(o)C) similar to the full-length protein (f-bCblC). However, t-bCblC is stabilized to a greater extent than f-bCblC by binding of reduced glutathione (GSH) with increased sensitivity to GSH. In addition, binding of oxidized glutathione (GSSG) destabilizes t-bCblC to a greater extent and with increased sensitivity as compared to f-bCblC. These results indicate that t-bCblC is a more sensitive form to be regulated by glutathione than the full-length form of the protein.
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