B12 deficiency or defective enzyme activity?

[lizw118]

I am researching some of my metametrix test results now for my methylation protocol. One thing that came up on my test is high methylmalonate, which is a marker for low B12. However I just came across this interesting information, which indicates that high urine methylmalonate could indicate a dysfunction in B12 transport:
"The research of Miller et al., have recently shown that methylmalonate is a reliable index of defective enzyme activity, namely transcobalamin II (TCII), responsible for transporting B12 from the ileum to the tissues. Apparently, variant enzyme activity in TCII is due to a single nucleotide polymorphism (SNP) at base position 776 in the DNA sequence in which a G-to-C substitution results in the synthesis of this enzyme carrying an arginine residue in place of proline at codon position 259. This common polymorphism results in a decreased binding affinity of the enzyme for B12 with consequent compromised delivery of B12 to tissues, and overall decrease in B12 functional status.3"
Does anyone know what could be done to remedy that situation, if it was the case? Is the methylation protocol with high doses of B12 better for this type of problem?

I read this from the following site:
http://www.usbiotek.com/Downloads/information/MarkOATLArticle-V6.pdf

 

[Freddd]

I am researching some of my metametrix test results now for my methylation protocol. One thing that came up on my test is high methylmalonate, which is a marker for low B12. However I just came across this interesting information, which indicates that high urine methylmalonate could indicate a dysfunction in B12 transport:
"The research of Miller et al., have recently shown that methylmalonate is a reliable index of defective enzyme activity, namely transcobalamin II (TCII), responsible for transporting B12 from the ileum to the tissues. Apparently, variant enzyme activity in TCII is due to a single nucleotide polymorphism (SNP) at base position 776 in the DNA sequence in which a G-to-C substitution results in the synthesis of this enzyme carrying an arginine residue in place of proline at codon position 259. This common polymorphism results in a decreased binding affinity of the enzyme for B12 with consequent compromised delivery of B12 to tissues, and overall decrease in B12 functional status.3"
Does anyone know what could be done to remedy that situation, if it was the case? Is the methylation protocol with high doses of B12 better for this type of problem?

I read this from the following site:
http://www.usbiotek.com/Downloads/information/MarkOATLArticle-V6.pdf

Hi Liz,

This is a total non-issue when using the sublingual active forms of the vitamins. When you put an adb12 under lip or tongue in 10 minutes it will be entering the mitochondria via diffusion. This issue only comes up in terms of inactive cobalamins. It is not relevant for mb12 or adb12 taken in mg quantity. This is one of the reasons I suggest bypassing all of this very complicated absorption and transportation issues of b12 that are typically "assumed" to work by using the multi-mg quantities of adb12 and mb12, both forms. They often don't.