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The coordinated and precise interaction between the ubiquitin-proteasome system (UPS), the protein chaperone system, and the autophagy-lysosome system (ALS) results in a dynamic endogenous protein quality control system that is essential to ensure the protein homeostasis 4,5,6

When tissue folate and cobalamin stores are intact, an abnormal increment of postmethionine-load homocysteinemia may also reveal a saturation of the transsulfuration pathway caused by dietary methionine excess that might be combined with transsulfuration defects (in cases with basal hyperhomocysteinemia) or with the homozygous thermolabile MTHFR defect (in cases with normal fasting homocysteine) (Cattaneo, 1999)