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Monographs in Human Genetics 1972
Topics: Age Factors; Amino Acid Metabolism, Inborn Errors; Child; Child, Preschool; Dwarfism; Ethnicity; Female; Heterozygote; Humans; Intellectual Disability; Male; Pregnancy; Saponins; Sarcosine; Twins
PubMed: 4677036
DOI: 10.1159/000392684 -
Yi Chuan Xue Bao = Acta Genetica Sinica 1999Through the analysis of EST database, we obtained one human EST (GenBank: H28856) which showed significant similarity with the partial coding sequence of rat...
Through the analysis of EST database, we obtained one human EST (GenBank: H28856) which showed significant similarity with the partial coding sequence of rat dimethylglycine dehydrogenase gene. This EST was mapped to 9q34 due to 95.6% identity with one genomic sequence (GenBank: AC002295). A pair of primers (HRP-1/HRP-2) designed on the sequence of the EST were coupled with the primers (lambda gt10-5/lambda gt10-3) on the vector flanking cloning site respectively to amplify the 5' and 3' cDNA beyond the EST. New primers designed based on novel cDNA sequence overlapped with the sequence within EST H28856 were used for amplification with lambda gt10-5 and lambda gt10-3 by the similar way as above untill a complete ORF was obtained. Finally, a 1,970 bp sequence (termed as dimethylglycine dehydrogenase like gene isoform I, DMGDHL1a) containing a 1,428 bp complete coding sequence from the live cDNA library and 1,475 bp sequence (isoform II, termed as DMGDHL1b) containing a 1,296 bp complete coding sequence from the fetas live cDNA library were obtained. Fourteen exons were identified in isoform I and the first nine exons of isoform II which shared with isoform I could be determined too. The last 105 bp cDNA sequence of isoform II could not be found in the public database, indicating a very large intron (> 123 kb) existed between exon 9 and exon 10 of isoform II. DMGDHL1 showed highly homology on both cDNA and amino acid level with rat dimethylglycine dehydrogenase (60% identity in 135 bp and 35% identity in 436 residues respectively). It was reported that human sarcosinemia gene was mapped at 9q34. Therefore it could be a good candidate gene for the sarcosinemia.
Topics: Amino Acid Sequence; Animals; Base Sequence; Chromosomes, Human, Pair 9; Cloning, Molecular; Dimethylglycine Dehydrogenase; Exons; Humans; Mitochondrial Proteins; Molecular Sequence Data; Oxidoreductases, N-Demethylating; Rats; Sarcosine; Sarcosine Dehydrogenase
PubMed: 10876657
DOI: No ID Found -
Deutsche Medizinische Wochenschrift... Mar 2009A 46-year-old previously healthy man was incidentally found to have an elevated serum creatinine concentration of 2,7 mg/dl (250 micromol/l) in a dry chemical enzyme...
HISTORY AND PHYSICAL EXAMINATION
A 46-year-old previously healthy man was incidentally found to have an elevated serum creatinine concentration of 2,7 mg/dl (250 micromol/l) in a dry chemical enzyme test. He had no symptoms. Physical examination was unremarkable.
INVESTIGATIONS
12 days after the first laboratory test serum creatinine was to be normal (0,66 g/dl, 58 micromol/l). Urinalysis and ultrasound scan of the kidneys revealed no anomalies. But increased sarcosine levels were found in both urine and plasma.
DIAGNOSIS AND COURSE
The creatinine testing assay interfered with an elevated serum sarcosine level, which is found in an inborn error of aminoacid metabolism called sarcosinemia.
CONCLUSION
In a patient with sarcosinemia a dry chemical enzyme analysis which is often used by general practitioners can produce falsely high creatinine levels. When suspecting sarcosinemia, serum creatinine should be checked against another type of laboratory test.
Topics: Amino Acid Metabolism, Inborn Errors; Choline; Creatinine; Diagnosis, Differential; Humans; Kidney; Kidney Diseases; Male; Middle Aged; Sarcosine; Ultrasonography; Urinalysis
PubMed: 19294604
DOI: 10.1055/s-0029-1208096 -
Revista Clinica Espanola Apr 1951
Topics: Amino Acid Metabolism, Inborn Errors; Humans; Leukemia; Mitochondrial Diseases; Sarcosine Dehydrogenase
PubMed: 14865064
DOI: No ID Found -
Zhonghua Er Ke Za Zhi = Chinese Journal... Feb 2016
Topics: Amino Acid Metabolism, Inborn Errors; Humans; Mitochondrial Diseases; Sarcosine Dehydrogenase
PubMed: 26875469
DOI: 10.3760/cma.j.issn.0578-1310.2016.02.018 -
Molecular Neurobiology Aug 2017Sarcosine is an N-methyl derivative of the amino acid glycine, and its elevation in tissues and physiological fluids of patients with sarcosinemia could reflect a...
Sarcosine is an N-methyl derivative of the amino acid glycine, and its elevation in tissues and physiological fluids of patients with sarcosinemia could reflect a deficient pool size of activated 1-carbon units. Sarcosinemia is a rare inherited metabolic condition associated with mental retardation. In the present study, we investigated the acute effect of sarcosine and/or creatine plus pyruvate on some parameters of oxidative stress and energy metabolism in cerebral cortex homogenates of 21-day-old Wistar rats. Acute administration of sarcosine induced oxidative stress and diminished the activities of adenylate kinase, GAPDH, complex IV, and mitochondrial and cytosolic creatine kinase. On the other hand, succinate dehydrogenase activity was enhanced in cerebral cortex of rats. Moreover, total sulfhydryl content was significantly diminished, while DCFH oxidation, TBARS content, and activities of SOD and GPx were significantly enhanced by acute administration of sarcosine. Co-administration of creatine plus pyruvate was effective in the prevention of alterations provoked by sarcosine administration on the oxidative stress and the enzymes of phosphoryltransfer network. These results indicate that acute administration of sarcosine may stimulate oxidative stress and alter the energy metabolism in cerebral cortex of rats. In case these effects also occur in humans, they may contribute, along with other mechanisms, to the neurological dysfunction of sarcosinemia, and creatine and pyruvate supplementation could be beneficial to the patients.
Topics: Adenylate Kinase; Animals; Cerebral Cortex; Creatine Kinase; Energy Metabolism; Fluoresceins; Glutathione Peroxidase; Models, Biological; Oxidation-Reduction; Oxidative Stress; Rats, Wistar; Sarcosine; Superoxide Dismutase
PubMed: 27356917
DOI: 10.1007/s12035-016-9984-1 -
The mouse mutation sarcosinemia (sar) maps to chromosome 2 in a region homologous to human 9q33-q34.Genomics Aug 1996The autosomal recessive mouse mutation sarcosinemia (sar), which was discovered segregating in the progeny of a male whose premeiotic germ cells had been treated with...
The autosomal recessive mouse mutation sarcosinemia (sar), which was discovered segregating in the progeny of a male whose premeiotic germ cells had been treated with the mutagen ethylnitrosourea, is characterized by a deficiency in sarcosine dehydrogenase activity. Using an intersubspecific cross, we mapped the sar locus to mouse chromosome 2, approximately 15-18 cM from the centromere. The genetic localization of this locus in the mouse allows the identification of a candidate region in human (9q33-q34) where the homologous disease should map.
Topics: Amino Acid Metabolism, Inborn Errors; Animals; Centromere; Chromosome Mapping; Chromosomes, Human, Pair 9; Female; Genes, Recessive; Humans; Male; Mice; Mice, Mutant Strains; Microsatellite Repeats; Mutation; Polymorphism, Genetic; Sarcosine
PubMed: 8812433
DOI: 10.1006/geno.1996.0442 -
European Journal of Biochemistry Nov 1998Sarcosine dehydrogenase (SarDH) is a mitochondrial flavoenzyme involved in the oxidative degradation of choline to glycine. The absence of SarDH activity in humans is...
Sarcosine dehydrogenase (SarDH) is a mitochondrial flavoenzyme involved in the oxidative degradation of choline to glycine. The absence of SarDH activity in humans is genetically transmitted and is the cause of an amino acid metabolism disorder called sarcosinemia. Tryptic fragments of the purified enzyme from rat liver were subjected to Edman degradation and the sequences obtained were used to clone the cDNA encoding the full length protein. The deduced amino acid sequence of SarDH shares an overall similarity of 47% with dimethylglycine dehydrogenase (Me2GlyDH), another flavoenzyme involved in the mitochondrial choline catabolism with a similar FAD-binding domain. Covalent binding of FAD to SarDH was demonstrated by the observation of strong fluorescence at 530 nm under excitation at 450 nm of the enzyme immunoprecipitated under denaturing conditions from liver extracts. The localization of SarDH immunoreactivity in the mitochondrial matrix was confirmed by Western-blot analysis of purified mitochondrial fractions. Finally, the tissue distribution of SarDH was investigated by Northern-blot analysis of total RNA and Western-blot analysis of total protein from several rat tissues. A strong expression in the liver, but also in the lung, pancreas, kidney, thymus, and oviduct was observed. We therefore suggest that the enzymes of the choline catabolism pathway are important also for metabolism in nonhepatic tissues.
Topics: Amino Acid Sequence; Animals; Base Sequence; Blotting, Western; Cell Line; Cloning, Molecular; DNA Primers; DNA, Complementary; Humans; Male; Mitochondria, Liver; Molecular Sequence Data; Oxidoreductases, N-Demethylating; RNA, Messenger; Rats; Rats, Wistar; Sarcosine Dehydrogenase; Sequence Homology, Amino Acid
PubMed: 9839943
DOI: 10.1046/j.1432-1327.1998.2570556.x -
Scientific Reports Feb 2023Suppressor of mek1 (Dictyostelium) homolog 2 (Smek2), was identified as one of the responsible genes for diet-induced hypercholesterolemia (DIHC) of exogenously...
Suppressor of mek1 (Dictyostelium) homolog 2 (Smek2), was identified as one of the responsible genes for diet-induced hypercholesterolemia (DIHC) of exogenously hypercholesterolemic (ExHC) rats. A deletion mutation in Smek2 leads to DIHC via impaired glycolysis in the livers of ExHC rats. The intracellular role of Smek2 remains obscure. We used microarrays to investigate Smek2 functions with ExHC and ExHC.BN-Dihc2 congenic rats that harbor a non-pathological Smek2 allele from Brown-Norway rats on an ExHC background. Microarray analysis revealed that Smek2 dysfunction leads to extremely low sarcosine dehydrogenase (Sardh) expression in the liver of ExHC rats. Sarcosine dehydrogenase demethylates sarcosine, a byproduct of homocysteine metabolism. The ExHC rats with dysfunctional Sardh developed hypersarcosinemia and homocysteinemia, a risk factor for atherosclerosis, with or without dietary cholesterol. The mRNA expression of Bhmt, a homocysteine metabolic enzyme and the hepatic content of betaine (trimethylglycine), a methyl donor for homocysteine methylation were low in ExHC rats. Results suggest that homocysteine metabolism rendered fragile by a shortage of betaine results in homocysteinemia, and that Smek2 dysfunction causes abnormalities in sarcosine and homocysteine metabolism.
Topics: Animals; Rats; Betaine; Glucose; Homocysteine; Hypercholesterolemia; Hyperhomocysteinemia; Liver; Mutation; Rats, Inbred BN; Sarcosine; Sarcosine Dehydrogenase; Amino Acid Metabolism, Inborn Errors; Phosphoprotein Phosphatases
PubMed: 36810603
DOI: 10.1038/s41598-022-26115-z -
The American Journal of Medicine Oct 1961
Topics: Amino Acid Metabolism, Inborn Errors; Esophageal Neoplasms; Humans; Intestinal Neoplasms; Intestines; Leiomyoma; Leiomyosarcoma; Mitochondrial Diseases; Sarcosine Dehydrogenase; Stomach Neoplasms
PubMed: 13901886
DOI: 10.1016/0002-9343(61)90143-7