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Identification of differentially expressed proteins in vitamin B 12
- Source :
- Journal of the Practice of Cardiovascular Sciences, Vol 1, Iss 1, Pp 45-53 (2015)
- Publication Year :
- 2015
- Publisher :
- Wolters Kluwer Medknow Publications, 2015.
-
Abstract
- Background: Vitamin B 12 (cobalamin) is a water-soluble vitamin generally synthesized by microorganisms. Mammals cannot synthesize this vitamin but have evolved processes for absorption, transport and cellular uptake of this vitamin. Only about 30% of vitamin B 12 , which is bound to the protein transcobalamin (TC) (Holo-TC [HoloTC]) enters into the cell and hence is referred to as the biologically active form of vitamin B 12 . Vitamin B 12 deficiency leads to several complex disorders, including neurological disorders and anemia. We had earlier shown that vitamin B 12 deficiency is associated with coronary artery disease (CAD) in Indian population. In the current study, using a proteomics approach we identified proteins that are differentially expressed in the plasma of individuals with low HoloTC levels. Materials and Methods: We used isobaric-tagging method of relative and absolute quantitation to identify proteins that are differently expressed in individuals with low HoloTC levels when compared to those with normal HoloTC level. Results: In two replicate isobaric tags for relative and absolute quantitation experiments several proteins involved in lipid metabolism, blood coagulation, cholesterol metabolic process, and lipoprotein metabolic process were found to be altered in individuals having low HoloTC levels. Conclusions: Our study indicates that low HoloTc levels could be a risk factor in the development of CAD.
Details
- Language :
- English
- ISSN :
- 23955414 and 24542830
- Volume :
- 1
- Issue :
- 1
- Database :
- Directory of Open Access Journals
- Journal :
- Journal of the Practice of Cardiovascular Sciences
- Publication Type :
- Academic Journal
- Accession number :
- edsdoj.0d86c91fc8f941308691898b1b1b0448
- Document Type :
- article
- Full Text :
- https://doi.org/10.4103/2395-5414.157568