Oxidation of cytosolic NADH formed during aerobic metabolism in mammalian cells

Dawson, Anthony G.

doi:10.1016/0968-0004(79)90417-1

Cited by 125 publications

(90 citation statements)

References 18 publications

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“…Because the inner mitochondrial membrane is impermeable to NADH (4, 5), various NADH shuttles have been described that provide pathways for reduced intermediates to enter the mitochondria for reoxidation (6). The present study found that the capacity of two of these NADH shuttles, the malatelaspartate and a-GP shuttles, are significantly increased in newborn right and left ventricular myocardium compared with adult.…”

Section: Discussionsupporting

confidence: 54%

Reducing Equivalent Shuttles in Developing Porcine Myocardium: Enhanced Capacity in the Newborn Heart

Scholz

Koppenhafer

1995

Pediatr Res

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Section: Discussionsupporting

confidence: 54%

Reducing Equivalent Shuttles in Developing Porcine Myocardium: Enhanced Capacity in the Newborn Heart

Scholz

Koppenhafer

1995

Pediatr Res

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“…He, and M. Reitman, unpublished observations. 3 The Whitehead Institute web site is http://www.genome.wi.mit. edu/, and the Stanford web site is http://www-shgc.stanford.edu/RH/.…”

Section: Resultsmentioning

confidence: 99%

“…PCR used 30 cycles of 94°C for 30 s; 56°C for 30 s; and 72°C for 30 s. Data analysis was performed using the Whitehead Institute and Stanford web sites. 3 …”

Section: Methodsmentioning

confidence: 99%

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Uncoupling Protein-3 Is a Mediator of Thermogenesis Regulated by Thyroid Hormone, β3-Adrenergic Agonists, and Leptin

Gong

Karas

et al. 1997

Journal of Biological Chemistry

739

624

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Mitochondrial uncoupling proteins (UCPs) are transporters that are important for thermogenesis. The net result of their activity is the exothermic movement of protons through the inner mitochondrial membrane, uncoupled from ATP synthesis. We have cloned a third member of the UCP family, UCP3. UCP3 is expressed at high levels in muscle and rodent brown adipose tissue. Overexpression in yeast reduced the mitochondrial membrane potential, showing that UCP3 is a functional uncoupling protein. UCP3 RNA levels are regulated by hormonal and dietary manipulations. In contrast, levels of UCP2, a widely expressed UCP family member, showed little hormonal regulation. In particular, muscle UCP3 levels were decreased 3-fold in hypothyroid rats and increased 6-fold in hyperthyroid rats. Thus UCP3 is a strong candidate to explain the effects of thyroid hormone on thermogenesis. White adipose UCP3 levels were greatly increased by treatment with the ␤3-adrenergic agonist, CL214613, suggesting another pathway for increasing thermogenesis. UCP3 mRNA levels were also regulated by dexamethasone, leptin, and starvation, albeit differently in muscle and brown adipose tissue. Starvation caused increased muscle and decreased BAT UCP3, suggesting that muscle assumes a larger role in thermoregulation during starvation. The UCP3 gene is located close to that encoding UCP2, in a chromosomal region implicated in previous linkage studies as contributing to obesity.Changes in body weight result from the difference between energy intake and energy expenditure. It is presumed that each individual has a target weight that the body tries to maintain. Since weight remains relatively constant despite large variations in energy intake, energy expenditure must be regulated. For example, people who gain weight become metabolically less efficient, whereas those who lose weight become more efficient (1).The biochemical mechanisms responsible for the regulation of energy expenditure and the efficiency of energy usage are poorly understood. Possible ways to increase energy expenditure include increasing physical activity (2) and energy dissipation as heat by futile metabolic cycles (3-5).

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“…In conjunction with the cytosolic glycerol-3-phosphate dehydrogenase, this shuttle uses the interconversion of glycerol-3-phosphate to dihydroxyacetone phosphate to oxidize cytosolic NADH by transferring reduction equivalents from the cytosol to the mitochondrion (1,2). The expression of human and rat mGPDH is regulated by two somatic promoters in a tissue-specific manner (3)(4)(5)(6)(7), but rat mGPDH is additionally regulated by a third testis-specific promoter (8).…”

mentioning

confidence: 99%

Germ Cell Nuclear Factor Relieves cAMP-response Element Modulator τ-mediated Activation of the Testis-specific Promoter of Human Mitochondrial Glycerol-3-phosphate Dehydrogenase

Rajković¹,

Middendorff

Wetzel³

et al. 2004

Journal of Biological Chemistry

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Mitochondrial glycerol-3-phosphate dehydrogenase (mGPDH) is an essential component of the glycerol phosphate shuttle that transfers reduction equivalents from the cytosol into the mitochondrion. Within the testis, immunohistological analysis localized human mG-PDH to late spermatids and to the midpiece of spermatozoa. The expression of human mGPDH is regulated by two somatic promoters, and here, we describe a third testis-specific promoter of human mGPDH. The usage of this testis-specific promoter correlates with the expression of a shortened mGPDH transcript of ϳ2.4 kb in length, which is solely detectable from testicular RNA. Within the testis-specific promoter, we detected a cAMPresponse element (CRE) site at ؊51, which binds the testis-specific transcriptional activator CRE modulator (CREM ) in electrophoretic mobility shift assays. This recognition site overlaps with a nuclear receptor binding half-site at ؊49, which binds the testis-specific transcriptional repressor germ cell nuclear factor (GCNF). Both factors compete for binding to the same DNA response element. Ectopic expression of CREM in HepG2 cells activated a promoter-driven luciferase construct in transient transfection experiments. Additional cotransfection of GCNF relieved this activity, suggesting a down-regulation of CREM -mediated activation by GCNF. This effect was preserved by introducing the CRE/nuclear receptor-binding element into a heterologous promoter context. Our data suggest a down-regulation of CREM -mediated gene expression by GCNF, which might be a general regulation mechanism for several postmeiotically expressed genes with a temporal expression peak during early spermatid development.Mitochondrial glycerol-3-phosphate dehydrogenase (mG-PDH) 1 is an essential component of the glycerol phosphate shuttle. In conjunction with the cytosolic glycerol-3-phosphate dehydrogenase, this shuttle uses the interconversion of glycerol-3-phosphate to dihydroxyacetone phosphate to oxidize cytosolic NADH by transferring reduction equivalents from the cytosol to the mitochondrion (1, 2). The expression of human and rat mGPDH is regulated by two somatic promoters in a tissue-specific manner (3-7), but rat mGPDH is additionally regulated by a third testis-specific promoter (8). The usage of the testis-specific promoter of mGPDH results in a shortened transcript length of ϳ2.4 kb containing an alternate first exon at its 5Ј end and a shortened 3Ј-untranslated region; however, the open reading frame remains unaffected (3,8). In rat testis, mGPDH transcripts have been detected in postmeiotic germ cells during early spermatid development, whereas mGPDH proteins have been detected during late spermatid development (8). The knockout of mGPDH in transgenic mice leads to reduced fertility (9, 10).Within the testis, spermatogenesis is a complex developmental process that includes the mitotic proliferation of spermatogonial stem cells, meiotic prophase, division of spermatocytes, and morphological changes of haploid spermatids to highly specialized spermato...

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Oxidation of cytosolic NADH formed during aerobic metabolism in mammalian cells

Cited by 125 publications

References 18 publications

Reducing Equivalent Shuttles in Developing Porcine Myocardium: Enhanced Capacity in the Newborn Heart

Reducing Equivalent Shuttles in Developing Porcine Myocardium: Enhanced Capacity in the Newborn Heart

Uncoupling Protein-3 Is a Mediator of Thermogenesis Regulated by Thyroid Hormone, β3-Adrenergic Agonists, and Leptin

Germ Cell Nuclear Factor Relieves cAMP-response Element Modulator τ-mediated Activation of the Testis-specific Promoter of Human Mitochondrial Glycerol-3-phosphate Dehydrogenase

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