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VITAMIN B12 (METHYLCOBALAMIN) BENEFITS

KEY BENEFITS OF METHYLCOBALAMIN

        • Supports brain and nerve health
        • Supports cellular metabolism
        • Supports healthy vision

ABOUT METHYLCOBALAMIN

Cobalamin, or vitamin B12, stands out among vitamins due to its metal ion, cobalt, from which it gets its name.
 
Adenosylcobalamin is the other coenzyme form of vitamin B12 (the other is methylcobalamin). Both forms are used by the body as enzymes.
 
Methionine synthase, which makes the purines and pyrimidines needed for DNA, is the only enzyme in which methylcobalamin is used.
 
The S-adenosylmethionine cycle is also linked to the methionine synthase, which converts methyltetrahydrofolate into tetrahydrofolate. This in turn results in homocysteine being converted into methionine (thereby supporting a healthy homocysteine level).
 
The methylation process or methyl donation uses methylcobalamin as a central element.
 
Interactions between this process and metabolic function are widespread. Among the major ways, gene expression is regulated is through methylation, one of the major ways to match our genes to our environment, diet, and lifestyle.
 
It is believed that methylcobalamin is the best form of vitamin B12 for sustaining vitamin B12-dependent enzymes and that this is the most effective form of vitamin B12 for maintaining health.
 
For nerve cell function to be healthy, vitamin B12 is necessary.
 
Generally speaking, methylcobalamin is considered more of a nootropic form of vitamin B12, as it's been extensively studied for its ability to support brain, nerve, and vision functions.

METHYLCOBALAMIN FULL BENEFITS

Methionine Synthase Activity

 

  • Methylcobalamin is required as a cofactor for the activity of the cytosolic enzyme methionine synthase [2,3]
  • Methionine synthase transfers the methyl group from methyltetrahydrofolate to homocysteine to form methionine and tetrahydrofolate [2,3]
  • Methionine is required for the synthesis of S-adenosylmethionine (SAMe), a methyl group donor used in many
  • biological methylation reactions [2,3]
  • Methionine synthase is essential for the methylation of nucleic acids (DNA and RNA) for DNA synthesis and protein synthesis [2,3]

 

Cardiovascular and cerebrovascular function

 

  • Downregulates homocysteine levels (protects cardiovascular function); complementary to vitamin B6 and folic acid (vitamin B9) [4–6]

 

Vision

 

  • Supports accommodation (i.e., focusing of eyes) when using devices with screen [7,8]
  • Supports retinal circadian rhythms [9]
  • Supports healthy retinal function [10–12]
  • Supports healthy optic nerve function [10,13–21]
  • Supports retinal nerve fiber layer thickness [22,23]
  • Supports normal activity of ciliary muscles of the lens [8]
  • Supports healthy function of eye ocular surfaces and corneal nerve [24,25]

 

Gut Microbiome

 

  • Supports healthy gut microbiome flora and function [26,27]

 

Complementary ingredients

 

  • Folate - Insufficient methylcobalamin slows the regeneration of tetrahydrofolate and traps folate in a form that is not usable by the body. This can often be corrected with higher doses of folate but can mask a vitamin B12 deficiency, so vitamin B12 is almost always given when folates are supplemented.
  • Methyl Donors - Key methyl donor nutrients include trimethylglycine (betaine), folates, vitamin B6, vitamin B12, and S-adenosylmethionine: One or more of these nutrients are often given together.
  • Adenosylcobalamin (another coenzyme form of vitamin B12) [28]

VITAMIN B12 (METHYLCOBALAMIN) CAN BE FOUND IN:

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REFERENCES

[1]M.H. Hill, J.E. Flatley, M.E. Barker, C.M. Garner, N.J. Manning, S.E. Olpin, S.J. Moat, J. Russell, H.J. Powers, The Journal of Nutrition 143 (2013) 142–147.
[2]F. O’Leary, S. Samman, Nutrients 2 (2010) 299–316.
[3]J.M. Berg, J.L. Tymoczko, G.J. Gatto, L. Stryer, eds., Biochemistry, 8th ed, W.H. Freeman and Company, 2015.
[4]J. Selhub, Annu. Rev. Nutr. 19 (1999) 217–246.
[5]E. Lonn, S. Yusuf, M.J. Arnold, P. Sheridan, J. Pogue, M. Micks, M.J. McQueen, J. Probstfield, G. Fodor, C. Held, J. Genest Jr, Heart Outcomes Prevention Evaluation (HOPE) 2 Investigators, N. Engl. J. Med. 354 (2006) 1567–1577.
[6]D. Serapinas, E. Boreikaite, A. Bartkeviciute, R. Bandzeviciene, M. Silkunas, D. Bartkeviciene, Reprod. Toxicol. 72 (2017) 159–163.
[7]S. Kurimoto, T. Iwasaki, T. Nomura, K. Noro, S. Yamamoto, J. UOEH 5 (1983) 101–110.
[8]T. Iwasaki, S. Kurimoto, J. UOEH 9 (1987) 127–132.
[9]N. Imamura, Y. Dake, T. Amemiya, Life Sci. 57 (1995) 1317–1323.
[10]E.M. Chester, D.P. Agamanolis, J.W. Harris, M. Victor, J.D. Hines, J.A. Kark, Acta Neurol. Scand. 61 (1980) 9–26.
[11]S.S. Reddy, Y.K. Prabhakar, C.U. Kumar, P.Y. Reddy, G.B. Reddy, Mol. Vis. 26 (2020) 311–325.
[12]J. Guo, S. Ni, Q. Li, J.-Z. Wang, Y. Yang, Neurosci. Bull. 35 (2019) 325–335.
[13]D. Stambolian, M. Behrens, Am. J. Ophthalmol. 83 (1977) 465–468.
[14]A.J. Larner, Int. J. Clin. Pract. 58 (2004) 977–978.
[15]M. Moschos, The Lancet 352 (1998) 146–147.
[16]Y. Yamazaki, F. Hayamizu, C. Tanaka, Curr. Ther. Res. Clin. Exp. 61 (2000) 443–451.
[17]X. Kong, X. Sun, J. Zhang, Yan Ke Xue Bao 20 (2004) 171–177.
[18]S.H. Chavala, G.S. Kosmorsky, M.K. Lee, M.S. Lee, Eur. J. Intern. Med. 16 (2005) 447–448.
[19]P. Enoksson, A. Norden, Acta Medica Scandinavica 167 (2009) 199–208.
[20]C. Chu, P. Scanlon, Case Reports 2011 (2011) bcr0220113823–bcr0220113823.
[21]O.P. Anand, Delhi Journal of Ophthalmology 29 (2019).
[22]S. Özkasap, K. Türkyilmaz, S. Dereci, V. Öner, T. Calapoğlu, M.C. Cüre, M. Durmuş, Childs. Nerv. Syst. 29 (2013) 2281–2286.
[23]K. Türkyılmaz, V. Öner, A.K. Türkyılmaz, A. Kırbaş, S. Kırbaş, B. Şekeryapan, Curr. Eye Res. 38 (2013) 680–684.
[24]S. Ozen, M.A. Ozer, M.O. Akdemir, Graefes Arch. Clin. Exp. Ophthalmol. 255 (2017) 1173–1177.
[25]M.R. Romano, F. Biagioni, A. Carrizzo, M. Lorusso, A. Spadaro, T. Micelli Ferrari, C. Vecchione, M. Zurria, G. Marrazzo, G. Mascio, B. Sacchetti, M. Madonna, F. Fornai, F. Nicoletti, M.D. Lograno, Exp. Eye Res. 120 (2014) 109–117.
[26]Y. Xu, S. Xiang, K. Ye, Y. Zheng, X. Feng, X. Zhu, J. Chen, Y. Chen, Front. Microbiol. 9 (2018) 2780.
[27]X. Zhu, S. Xiang, X. Feng, H. Wang, S. Tian, Y. Xu, L. Shi, L. Yang, M. Li, Y. Shen, J. Chen, Y. Chen, J. Han, J. Agric. Food Chem. 67 (2019) 916–926.
[28]E.S. Tsukerman, T.L. Korsova, A.A. Poznanskaia, Vopr. Pitan. (1992) 40–44.