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Results: 8

1.
Fig. 5.

Fig. 5. From: Successful adaptation to ketosis by mice with tissue-specific deficiency of ketone body oxidation.

Circulating metabolites in neonatal tissue-specific SCOT-KO strains. A: blood glucose (mg/dl) in P1 mice. B: serum AcAc and d-βOHB (mM) in P1 mice; n = 5–8/group. ***P < 0.001 and **P < 0.01 for serum ketone concentration ([ketone]) vs. flox/flox by 1-way ANOVA. ††P < 0.01 for serum [ketone] vs. flox/rec by 1-way ANOVA.

David G. Cotter, et al. Am J Physiol Endocrinol Metab. 2013 February 15;304(4):E363-E374.
2.
Fig. 4.

Fig. 4. From: Successful adaptation to ketosis by mice with tissue-specific deficiency of ketone body oxidation.

Preservation of CoA transferase protein in nontargeted tissues of tissue-specific SCOT-KO mouse models. Immunoblot for CoA transferase (SCOT) and actin in brain, muscle, and myocardial protein lysates derived from P0 SCOT-Heart-KO (A), SCOT-Muscle-KO (B), SCOT-Neuron-KO (C), and control mice.

David G. Cotter, et al. Am J Physiol Endocrinol Metab. 2013 February 15;304(4):E363-E374.
3.
Fig. 7.

Fig. 7. From: Successful adaptation to ketosis by mice with tissue-specific deficiency of ketone body oxidation.

Adult tissue-specific SCOT-KO mice tolerate starvation. Serum glucose (mg/dl; A), serum total ketone bodies (TKB, mM; B), and body weight (g; C) were measured in fasting SCOT-Heart-KO, Muscle-KO, Neuron-KO, and control adult mice after the indicated durations of nutrient withdrawal. ***P < 0.001, **P < 0.01, and *P < 0.05 by 2-way ANOVA compared with the same genotype at 4 h. †††P < 0.001 and ††P < 0.01 by 2-way ANOVA compared with flox/flox at the same time point. ‡‡‡P < 0.001 by 2-way ANOVA compared with flox/rec control; n ≥ 6/group for each measurement at all time points and for each genotype.

David G. Cotter, et al. Am J Physiol Endocrinol Metab. 2013 February 15;304(4):E363-E374.
4.
Fig. 6.

Fig. 6. From: Successful adaptation to ketosis by mice with tissue-specific deficiency of ketone body oxidation.

Increased glucose consumption by brains of neonatal SCOT-Neuron-KO mice. A: [1-13C]glucose labeling of lactate, a surrogate for glycolysis in brains of SCOT-Neuron-KO (on the flox/rec germline background) and control mice, 30 min after ip injection of [1-13C]glucose into P2 animals. B: 13C labeling of glutamate (surrogate for terminal oxidation in the tricarboxylic acid cycle) in these same cerebral extracts; n = 4/group. *P < 0.05 by Student's t-test. C: relative mRNA abundance of gluconeogenic [phosphoenolpyruvate carboxykinase (Pck1)] and ketogenic [hydroxymethylglutaryl-CoA synthase (Hmgcs2) and d-β-hydroxybutyrate-dehydrogenase (Bdh1)] genes in livers of P2 SCOT-Neuron-KO and control mice; n = 5/group.

David G. Cotter, et al. Am J Physiol Endocrinol Metab. 2013 February 15;304(4):E363-E374.
5.
Fig. 3.

Fig. 3. From: Successful adaptation to ketosis by mice with tissue-specific deficiency of ketone body oxidation.

Absence of CoA transferase protein and enzymatic activity in tissue-specific SCOT-KO mouse strains. CoA transferase activity was measured spectrophotometrically (left) in tissue lysates derived from heart (A), skeletal muscle (quadriceps/hamstrings) (B), and brains (C) of P0 mice; n = 3–6/group. ***P < 0.001 by linear regression t-test. Brains of SCOT-Neuron-KO mice on both flox/flox and flox/rec genetic backgrounds were analyzed (depicted as flox/x). Immunoblots for CoA transferase (SCOT) and actin (right). D: immunoblot (left) and densitometric quantification (right) of CoA transferase protein abundance, normalized to actin in isolated hippocampi from adult SCOT-Neuron-KO mice; n = 5 for flox/flox mice; n = 2 for flox/rec mice; n = 2 for flox/flox:SCOT-Neuron-KO mice; n = 5 for flox/rec:SCOT-Neuron-KO mice. ***P < 0.001, **P < 0.01, and *P < 0.05 by 1-way ANOVA. ns, Not significant.

David G. Cotter, et al. Am J Physiol Endocrinol Metab. 2013 February 15;304(4):E363-E374.
6.
Fig. 8.

Fig. 8. From: Successful adaptation to ketosis by mice with tissue-specific deficiency of ketone body oxidation.

Diminished total body ketone body oxidative capacity impairs adaptation to ketotic nutrient states. Metabolic parameters were measured in 6-wk-old Oxct1+/− and Oxct1+/+ (wild-type littermate control) male mice subjected to ketotic nutrient states. Total body weight (g; A), serum total ketone bodies (mM; B), serum glucose (mg/dl; C), and serum free fatty acids (FFA, mM; D) were measured in fasting mice. Total serum ketone bodies (mM; E) and serum glucose (mg/dl; F) were also measured in 8-wk-old male Oxct1+/− and littermate Oxct1+/+ (wild-type) mice maintained either on a standard polysaccharide-rich (Chow) diet or low-protein, low-carbohydrate, high-fat ketogenic diet (KD) for 2 wk; n = 7/group. ***P < 0.001, **P < 0.01, and *P < 0.05 by 2-way ANOVA.

David G. Cotter, et al. Am J Physiol Endocrinol Metab. 2013 February 15;304(4):E363-E374.
7.
Fig. 2.

Fig. 2. From: Successful adaptation to ketosis by mice with tissue-specific deficiency of ketone body oxidation.

Restoration of ketone body oxidative capacity selectively within cardiomyocytes of germline SCOT-KO mice. A: immunoblot for CoA transferase (SCOT) and actin in brain, muscle, and myocardial protein lysates derived from the first postnatal day (P0) SCOT-KO mice with transgene-mediated restoration of cardiomyocyte CoA transferase (SCOT-Heart-OVEX:SCOT-KO mice). B: immunoblot for CoA transferase (SCOT) and actin in myocardial protein lysates derived from P0 hearts of wild-type mice, SCOT-Heart-OVEX:SCOT-KO mice, and SCOT-KO mice. C: CoA transferase activity was measured spectrophotometrically in tissue lysates derived from hearts of P0 wild-type and SCOT-KO mice and hearts and brains of P0 SCOT-Heart-OVEX:SCOT-KO mice; n = 3/group. ***P < 0.001 by linear regression t-test vs. SCOT-Heart-OVEX:SCOT-KO heart. †††P < 0.001 by linear regression t-test vs. wild-type heart. D: serum ketone bodies (mM) in P1 wild-type, SCOT-KO, SCOT-Heart-OVEX, and SCOT-Heart-OVEX:SCOT-KO mice; n = 5–6/group. ***P < 0.001 and *P < 0.05 for d-β-hydroxybutyrate (βOHB); †††P < 0.001 for acetoacetate (AcAc); ‡‡‡P < 0.001 for the AcAc-to-d-βOHB ratio by 2-way ANOVA compared with genotype control on the Oxct1+/+ (wild-type) background. E: blood glucose (mg/dl) in P1 mice; n = 4–6/group. ***P < 0.001 and *P < 0.05 by 2-way ANOVA.

David G. Cotter, et al. Am J Physiol Endocrinol Metab. 2013 February 15;304(4):E363-E374.
8.
Fig. 1.

Fig. 1. From: Successful adaptation to ketosis by mice with tissue-specific deficiency of ketone body oxidation.

Strategy for the generation of transgenic overexpresser and tissue-specific succinyl-CoA:3-oxoacid CoA transferase (SCOT)-knockout (KO) mice. A: transgenic mice that overexpress coenzyme A (CoA) transferase in cardiomyocytes (SCOT-Heart-OVEX mice). Mouse Oxct1 cDNA was subcloned downstream of the α-myosin heavy chain (MHC) promoter to generate mice overexpressing CoA transferase specifically within cardiomyocytes. ATG, initiator methionine codon; TGA, stop codon; kb, kilobase; UTR, untranslated region. B: schematics depict the endogenous Oxct1 mouse gene (wild type); targeted Null allele (the germline knockout allele); Flox allele, which encodes normal CoA transferase protein; and the recombined Rec (also a null) allele. Polyadenylation (pA) signals in the Null locus terminate transcription after exon 5, and a splice acceptor (SA)/internal ribosomal entry sequence (IRES) results in a truncated and catalytically inactive product from residual message. Flp recombinase recognition target (FRT) sites flank the β-gal and neomycin resistance cassettes and the pA signals. Thus, Flp recombinase mediates removal of the pA transcriptional stop signals and lacZ/neomycin cassette, restoring an active Oxct1 Flox allele in the germline. Exon 6 is flanked by loxP recognition sequences in the Flox allele for cell type-specific Cre recombinase-mediated recombination and inactivation. Genotyping primers for each allele are indicated as horizontal arrows (see Table 1 for sequences). β-gal, β-galactosidase-encoding lacZ gene; β-act:neo, neomycin resistance gene driven by the β-actin promoter.

David G. Cotter, et al. Am J Physiol Endocrinol Metab. 2013 February 15;304(4):E363-E374.

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