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Through this pathway, MeCbl contributes to folate metabolism, S-adenosylmethionine (SAM) generation, and a broad range of methylation reactions involving DNA, proteins, lipids, and myelin components.3 When MeCbl-dependent MS activity is reduced—whether through dietary insufficiency, malabsorption, or impaired cobalamin metabolism—biochemical consequences described in the literature include elevated homocysteine, decreased SAM, altered methylation patterns, increased uracil misincorporation, and can contribute to genomic instability.1,3 These disruptions are associated with several physiologic and neurologic findings reported in B12 insufficiency, such as myelin degeneration, axonal injury, abnormal nerve conduction, and the characteristic neuropathological features of subacute combined degeneration.1,4 Laboratory and experimental publications also describe neuronal uptake of MeCbl and report measurements involving axonal structures, myelin-supporting processes, and cellular responses to metabolic and excitatory stress, including glutamate exposure in vitro and in vivo.2 These investigations reflect the broader biologic context in which cobalamin-dependent methylation supports normal neurologic and hematologic function

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Ng and colleagues examined a synthetic hGH terminal domain in obese Zucker rats