Human mitochondrial NADP-dependent isocitrate dehydrogenase in man-mouse somatic cell hybrids

Bruns, G. A. P.; Eisenman, Robert; Gerald, Park S.

doi:10.1159/000130713

Cited by 10 publications

(7 citation statements)

References 7 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…et al, 1975), sor bitol dehydrogenase, SORD (Donald et al, 1979), pyruvate kinase-3, PKM2 (van Hi yningen et al, 1975), and mitochondrial iso citrate dehydrogenase, IDH2 (Bruns et al, 1976;Shimizu et al, 1977). One of these enzymes, MAN A, is also a neutral glycosidase.…”

Section: Discussionmentioning

confidence: 99%

Assignment of the gene for human neutral alpha-glucosidase C to chromosome 15

Martiniuk¹,

Hirschhorn²,

Smith³

1980

Cytogenet Genome Res

View full text Add to dashboard Cite

Human neutral α-glucosidase C (GANC) can be separated from the homologous mouse isozyme by starch gel electrophoresis at pH 6.5. A total of 40 clones (13 primary and 27 secondary) were derived from eight separate hybridization experiments between the mouse HPRT deficient RAG cell line and eight different human long term lymphoid cell lines or fetal cells. The thirteen primary clones showed 100% concordance between the expression of the human enzyme and the presence or absence of human chromosome 15. Analysis of the 27 secondary clones showed only two subclones discordant for segregation of human GANC and enzyme markers for 15. The two apparently discordant clones for human GANC were both derived from the same RAG × human fetal lung primary clone, and both lacked GANC activity, while retaining a 15. Since human GANC is polymorphic with a null allele at high frequency (Martiniuk and Hirschhorn, 1980), it is possible that these subclones carried one chromosome with a null allele for GANC. Alternatively there could been an undetected chromosome break between the GANC locus and the loci of the marker enzymes. Whatever the reason for the two apparently discordant subclones, combined data from all 40 clones show 95% concordant segregation for human GANC and No. 15.

show abstract

Section: Discussionmentioning

confidence: 99%

Assignment of the gene for human neutral alpha-glucosidase C to chromosome 15

Martiniuk¹,

Hirschhorn²,

Smith³

1980

Cytogenet Genome Res

View full text Add to dashboard Cite

show abstract

“…Isocitrate dehydrogenase (IDH) 1 and 2, which act in the cytoplasm and mitochondrion, respectively, are NADPH-dependent enzymes that metabolize isocitrate to α-ketoglutarate (α-KG), an intermediary product in the TCA cycle that is involved in various metabolic pathways ( 22 – 25 ). In particular, α-KG functions as an electron donor to PHDs for prolyl hydroxylation, which is important for hydroxylation and degradation of HIF1α ( 26 ).…”

mentioning

confidence: 99%

LncRNA IDH1-AS1 links the functions of c-Myc and HIF1α via IDH1 to regulate the Warburg effect

Xiang

Jin

et al. 2018

Proc. Natl. Acad. Sci. U.S.A.

View full text Add to dashboard Cite

SignificanceWe report in this article that c-Myc-mediated repression of lncRNA IDH1-AS1 sustains activation of the Warburg effect by HIF1α under normoxic conditions. IDH1-AS1 would otherwise enhance IDH1 enzymatic activity through promoting its homodimerization, leading to increased production of α-KG, which, along with decreases in ROS levels similarly resulting from increased IDH1 activity, causes down-regulation of HIF1a and a reduction in glycolysis. Collectively, our results have identified a signaling axis c-Myc-(IDH1-AS1)-IDH1-αKG/ROS-HIF1α that is important for activation of the Warburg effect under normoxia. Moreover, the results reveal IDH1 as a member of c-Myc-responsive metabolic enzymes and demonstrate that c-Myc plays an important part in balancing mitochondrial respiration and glycolysis to ensure glycolysis be executed efficiently in cancer cells under normoxia.

show abstract

“…IDH2 encodes a key enzyme in the tricarboxylic acid cycle [39] and was found to have a parallel amino acid replacement at position 186 of valine (V) to alanine (A) on three mammalian lineages. Dolphins, in addition to having large brains, adapted to the aquatic lifestyle through ancestors that had a long history of a semi-aquatic lifestyle, a lifestyle which incurs energy costs that are higher than running [40].…”

Section: Resultsmentioning

confidence: 99%

Parallel evolution of IDH2 gene in cetaceans, primates and bats

Chen

et al. 2013

FEBS Letters

View full text Add to dashboard Cite

a b s t r a c tCetaceans and primates both have large brains that require large amounts of aerobic energy metabolism. In bats, the cost of flight makes locomotion energetically demanding. These mammalian groups may represent three independent evolutionary origins of an energy-demanding lifestyle in mammals. IDH2 encodes an enzyme in the tricarboxylic acid cycle in the mitochondrion, which plays a key role in aerobic energy metabolism. In this study, we cloned and sequenced this gene in two cetaceans, and 19 bat species, and compared the data with available primate sequences to test its evolution. We found significant signals of parallel evolution in this gene among these three groups. Parallel evolution of this gene may reflect their parallel evolution towards a higher demand for energy.

show abstract

Human mitochondrial NADP-dependent isocitrate dehydrogenase in man-mouse somatic cell hybrids

Cited by 10 publications

References 7 publications

Assignment of the gene for human neutral alpha-glucosidase C to chromosome 15

Assignment of the gene for human neutral alpha-glucosidase C to chromosome 15

LncRNA IDH1-AS1 links the functions of c-Myc and HIF1α via IDH1 to regulate the Warburg effect

Parallel evolution of IDH2 gene in cetaceans, primates and bats

Contact Info

Product

Resources

About