CORRELATION BETWEEN VITAMIN B12 DEFICIENCY ANEMIA AND ARGININE METHYLATION IN ERYTHROCYTE BAND 3
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Abstract
Vitamin B12 deficiency is marked by megaloblastic anemia and abnormal red blood cell morphology. This study attempts to correlate B12 levels with RBC membrane proteins (especially Band 3) and arginine methylation. B12-deficient, iron-deficient and normal blood samples were analysed using SDS-PAGE and in silico using Alphafold3. SDS-PAGE revealed differences in band intensity and size, indicating altered membrane protein profiles in B12-deficient samples. AlphaFold3 modelling of known Band 3 mutations involving arginine substitutions revealed structural changes, especially in the N-terminal domain responsible for interaction with other membrane proteins. These preliminary observations suggest a possible correlation between B12 deficiency, arginine methylation, and changes in RBC membrane structure.
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References
1. Green, R. (2017). Vitamin B12 deficiency from the perspective of a practicing hematologist. Blood, 129(19), 2603–2611. https://doi.org/10.1182/blood-2016-10-569186 DOI: https://doi.org/10.1182/blood-2016-10-569186
2. Terwilliger, T. C., & Clarke, S. (1981). Methylation of proteins in intact human erythrocytes. Proceedings of the National Academy of Sciences of the United States of America, 78(1), 500–504. https://doi.org/10.1073/pnas.78.1.500
3. Kräutler, B. (2012). Vitamin B12: Chemistry and biochemistry. Biochemical Society Transactions, 40(3), 568–574. https://doi.org/10.1042/BST20120063 DOI: https://doi.org/10.1042/BST20120063
4. Vani, R., Anusha, B. A., Christina, R. M., Kavin, P., Mohammed, O., Inchara, S., Kavvyasruthi, U. J., & Sindhu, H. S. (2024). Band 3 protein: a critical component of Erythrocyte. In IntechOpen eBooks. https://doi.org/10.5772/intechopen.1005872 DOI: https://doi.org/10.5772/intechopen.1005872
5. Jarolim, P., Rubin, H. L., Brabec, V., Chrobak, L., Zolotarev, A. S., Alper, S. L., Brugnara, C., Wichterle, H., & Palek, J. (1995). Mutations of conserved arginines in the membrane domain of erythroid band 3 lead to a decrease in membrane-associated band 3 and to the phenotype of hereditary spherocytosis. Blood, 85(3), 634–640. DOI: https://doi.org/10.1182/blood.V85.3.634.bloodjournal853634
6. Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227(5259), 680–685. https://doi.org/10.1038/227680a0 DOI: https://doi.org/10.1038/227680a0
7. Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., ... & Hassabis, D. (2021). Highly accurate protein structure prediction with AlphaFold. Nature, 596, 583–589. https://doi.org/10.1038/s41586-021-03819-2 DOI: https://doi.org/10.1038/s41586-021-03819-2
8. Lux, S. E. (2015). Anatomy of the red cell membrane skeleton: unanswered questions. Blood, 127(2), 187–199. https://doi.org/10.1182/blood-2014-12-512772 DOI: https://doi.org/10.1182/blood-2014-12-512772
9. Ballas, S. K. (1978). Abnormal erythrocyte membrane protein pattern in severe megaloblastic anemia. Journal of Clinical Investigation, 61(4), 1097–1101. https://doi.org/10.1172/jci109009 DOI: https://doi.org/10.1172/JCI109009
10. Gardner, W. M., Razo, C., McHugh, T. A., Hagins, H., Vilchis-Tella, V. M., Hennessy, C., Taylor, H. J., Perumal, N., Fuller, K., Cercy, K. M., Zoeckler, L. Z., Chen, C. S., Lim, S. S., Aali, A., Abate, K. H., Abd-Elsalam, S., Abdurehman, A. M., Abebe, G., Abidi, H., Bhagavathula, A. S. (2023). Prevalence, years lived with disability, and trends in anaemia burden by severity and cause, 1990–2021: findings from the Global Burden of Disease Study 2021. The Lancet Haematology, 10(9), e713–e734. https://doi.org/10.1016/s2352-3026(23)00160-6 DOI: https://doi.org/10.1016/S2352-3026(23)00160-6
11. Reithmeier, R. A. F. (2016). Structure and function of SLC4 anion exchangers. In E. Delpire & K. L. Kirk (Eds.), Chloride Channels and Transporters in the Nervous System (pp. 223–251). Springer. https://doi.org/10.1007/978-3-319-38595-0_9
12. Jöns, T., & Drenckhahn, D. (1992). Identification of the binding interface involved in linkage of cytoskeletal protein 4.1 to the erythrocyte anion exchanger. The EMBO journal, 11(8), 2863–2867. https://doi.org/10.1002/j.1460-2075.1992.tb05354.x DOI: https://doi.org/10.1002/j.1460-2075.1992.tb05354.x