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Methylmalonic Acid - Crossref

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Last Updated: 23 April 2022

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Bilateral subthalamic nucleus deep brain stimulation for refractory total body dystonia secondary to metabolic autopallidotomy in a 4-year-old boy with infantile methylmalonic acidemia

The methylmalonic acidemias are a group of metabolic abnormalities that result in the accumulation of methylmalonic acid in body tissues and fluids. For 15 months, this case of total body dystonia due to MMA in a 4-year-old boy had been medically refractory. The case reveals both the safety of STN DBS in this condition and the technical difficulties in targeting a small child in a small infant.

Source link: https://doi.org/10.3171/2013.7.peds1350


Acute Lymphoblastic Leukemia in Combined Methylmalonic Acidemia and Homocysteinemia (cblC Type): A Case Report and Literature Review

Background: Methylmalonic acidemia can have many clinical manifestations, among which acute lymphoblastic leukemia has not been identified, and congenital heart disease is also unusual. Case presentation: We present an MMA lawsuit involving ALL and CHD in a 5. 5-year-old child. In physical examination, the decrease of muscle strength was also found. MMACHC c. 80A > G and c. 609G > A. Gene analysis revealed a compound heterozygous mutation in MMACHC. The MMA type CblC was identified as a blC type MMA. Both lower limbs' muscle endurance had significantly improved muscle strength, reaching nearly grade 5 in less than two months. Both the methylmalonic acid and homocysteine levels were raised. Conclusion: Metabolic disease screening and gene analysis are both highly recommended for diseases with a variety of medical signs. Synopsis: We report a case of methylmalonic acidemia in acute lymphoblastic leukemia and congenital heart disease, which revealed the importance of genetic testing and metabolic disease screening in patients with multiple systemic organ involvement.

Source link: https://doi.org/10.3389/fgene.2022.856552


Mutation eliminating mitochondrial leader sequence of methylmalonyl-CoA mutase causes muto methylmalonic acidemia.

Methylmalonyl-CoA Mutase is a mitochondrial matrix enzyme whose function is deficient in the inheritable disorder methylmalonic acidemia. A variety of biochemical phenotypes under this condition have been established by previous studies on primary fibroblast cell lines from patients with methylmalonic acidemia. One cell line with primary mutase apologetic deficiency had a particularly unusual phenotype; it contained an abnormally small and unstable immunoreactive protein that was not accessible by mitochondria; it was not inherited by mitochondria. These cells' immunoreactive protein differs from AUG codons downstream of this termination codon and, consequently, lacks a mitochondrial leader peptide.

Source link: https://doi.org/10.1073/pnas.87.8.3147


Immunochemical studies on cultured fibroblasts from patients with inherited methylmalonic acidemia.

We developed a radioimmunoase assay to measure blood from controls and 32 patients with methylmalonic acidemia due to genetic deficiencies in mutase activity. Each of the four cbl complementation groups of inherited methylmalonic acidemia, which have normal amounts of mutase activity in vitro, contained measurable CRM comparable to those of control lines. Each of seven lines from the mut-subgroup's residual mutase content indicates the presence of a structurally altered mutase protein with reduced affinity for cofactor. Several hundred percent of control were found in ranging from 20% to 100% of control. According to CRM, the 21 lines from the mut0 group, which have no detectable mutase activity in vitro, fell into two groups with respect to CRM: 9 lines had detectable CRM ranging from 3% to 40% of control; 12 others had no discernable CRM; 12 others did not have a single markable CRM.

Source link: https://doi.org/10.1073/pnas.78.12.7737


3-Hydroxypropionate: Significance of β-Oxidation of Propionate in Patients with Propionic Acidemia and Methylmalonic Acidemia

Propionyl-CoA carboxylase deficionyl-carbonate deficiate in propionyl-CoA carboxylase deficionate and 3-hydroxypropionate converts two patients with propionic acidemia in both patients and 3-hydroxypropionate. The presence of radioactive 3-hydroxypropionate in urine after these drugs' administration suggests that oxidation of propionyl-CoA by acryloyl-CoA was present in these patients. According to the conversion of vaping to 3-hydroxypropionate, the vaping of vain is oxidized in man by propionate and propionyl-CoA in man.

Source link: https://doi.org/10.1073/pnas.69.10.2807


CONGENITAL METHYLMALONIC ACIDEMIA: ENZYMATIC EVIDENCE FOR TWO FORMS OF THE DISEASE

Vitamin B 12 therapy in one of these clinical studies will either correct or prevent these clinical findings, while in a second variant vitamin B 12 therapy is of no use. The livers of patients with the second version of the disease exhibit normal enzymatic activity in the presence of vitamin B12's coenzyme form of vitamin B12, but not in the absence of the added coenzyme component.

Source link: https://doi.org/10.1073/pnas.63.1.191


Identification of the gene responsible for the cblA complementation group of vitamin B 12 -responsive methylmalonic acidemia based on analysis of prokaryotic gene arrangements

Vitamin B 12 is an important cofactor in two enzymes, methionine synthase, and methylmalonyl-CoA mutationase. Potential candidates were found in a bacterial operons with genes in close proximity to the gene for methylmalonyl-CoA mutase gene and searching for orthologous sequences in the human genome. The A candidate gene in cblA patient cell lines was tested for deleterious mutations, which resulted in a 4-bp deletion in three cell lines, as well as an 8-bp deletion, leading to a stop codon and an amino acid substitution, as well as an 8-bp deletion and point mutations. The deduced amino acid sequence reveals a domain structure that belongs to the AAA ATPase superfamily that includes a large number of proteins, including ATP-binding cassette transporter accessory proteins that bind ATP and GTP. We suspect we have identified a component of a transporter or an accessory protein that is involved in vitamin B12 translocation into mitochondria.

Source link: https://doi.org/10.1073/pnas.242614799


Targeting proximal tubule mitochondrial dysfunction attenuates the renal disease of methylmalonic acidemia

Isolated methylmalonic acidemia, caused by a lack of the mitochondrial enzyme methylmalonyl-CoA mutase, is often complicated by end-stage renal disease that is resistant to standard treatments, such as liver transplantation. Mut was expressed in the liver of Mut / mice as a stable transgene under the custody of an albumin promoter. To establish a viable model of MMA renal disease, Mut was expressed in the liver of Mut // mice as a stable transgene under the care of an albumin promoter. Tg INS-Alb- Mut mice as a unique model of MMA renal disease from a large and diverse patient cohort precisely replicated the results in the animals, leading to Mut INS-Alb-mut mice as a unique model of MMA renal disease. Our studies show that antioxidants can attenuate MMA-associated kidney disease, proximal tubular mitochondrial dysfunction is a key pathogenic mechanism of MMA-associated kidney disease, identify lipocalin-2 as a biomarker of increased oxidative stress in the renal tubule, and that antioxidants can attenuate renal disease of MMA.

Source link: https://doi.org/10.1073/pnas.1302764110


A G-protein editor gates coenzyme B 12 loading and is corrupted in methylmalonic aciduria

This conversion of coenzyme B 12 or 5'-deoxyadenosylcobalamin by adenosyltransferase to methylmalonyl-CoA mutase is limited by a small G protein, MeaB. For gating cofactor transfer, the GTP-binding energy is required for the editing job; that is, to distinguish between active and inactive cofactor forms. During turnover, the G protein chaperone also serves its editing function by using the GTP's binding energy to elicit the release of an inactive cofactor that is occasionally present during MCM's catalytic cycle.

Source link: https://doi.org/10.1073/pnas.0908106106


In vitamin B 12 deficiency, higher serum folate is associated with increased total homocysteine and methylmalonic acid concentrations

We found that a combination of elevated serum folate and low vitamin B 12 status was more indicative of cognitive decline and anemia in older participants in the 1999-2002 National Health and Nutrition Examination Survey, suggesting a higher risk of cognitive decline and anemia than other combinations of vitamin B 12 and folate status. The NHANES III and the NHANES 2002-2002 cohorts sought to determine the combined effect of serum folate and vitamin B 12 concentrations on two key measures of vitamin B 12 status, total homocysteine, and methylmalonic acid. Concentrations of both metabolites decreased dramatically in B12 > 148 pmol/liter in rats with serum vitamin B12> 148 pmol/liter, as serum folate increased. These results point to an escalating of vitamin B 12's enzymatic functions as folate status rises in people who are vitamin B12-deficient.

Source link: https://doi.org/10.1073/pnas.0709487104

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions