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Biology subjects

Menezes, T. N.

Publications and source records attributed to Menezes, T. N..

3 recordsLinked to original sources

Sustained loss of Pptc7 triggers variable skeletal muscle dysfunction and diminished body mass through dysregulation of BNIP3

The mitochondrial phosphatase PPTC7 is required to sustain mammalian metabolism, as its global knockout (KO) triggers hypoketotic hypoglycemia and perinatal lethality in mice. However, the extent to which the loss of Pptc7 manifests pathology beyond the perinatal transition is unknown. Furthermore, PPTC7 was recently identified as dual functional, regulating mitochondrial protein phosphorylation and receptor mediated mitophagy, rendering it unclear which function(s) may influence in vivo physiology. Here, we find that sustained, inducible Pptc7 KO decreased lean mass, compromised whole body oxygen consumption, and altered circulating metabolites in adult male mice. We hypothesized that these phenotypes stemmed from skeletal muscle dysfunction and found lower mass and fiber cross-sectional area with shifts in fiber type distribution in select muscles of the hindlimb in Pptc7 KO animals. Loss of PPTC7 increased BNIP3 protein levels and decreased mitochondrial content in skeletal muscle, suggesting elevated mitophagy may drive pathology. Consistently, KO of Bnip3 rescued the lower body weight and lean mass seen in inducible Pptc7 KO adult animals and partially rescued perinatal lethality in global Pptc7 KO mice. These data demonstrate that loss of PPTC7 incites surprisingly variable dysfunction across physiological contexts that at least partially stems from dysregulated BNIP3.

physiology↗

Impact of aldehyde dehydrogenase 2 deficiency on tissue-specific mitochondrial metabolism in aging mice

Age-related diseases arise from prolonged exposure to genetic and/or environmental factors, ultimately leading to cumulative and irreversible degeneration of tissues and the organism as a whole. We previously reported that accumulation of mitochondrially-generated aldehydes (i.e., 4-hydroxynonenal and acetaldehyde) causes mitochondrial dysfunction and accelerates the progression of age-related diseases. However, the contribution of mitochondrial aldehyde metabolism to aging (via aldehyde dehydrogenase 2, ALDH2) remains elusive. Here, we provide a comprehensive analysis of aldehyde metabolism and mitochondrial bioenergetics across different tissues in aging mice. We also address how mitochondrial function is influenced by the highly prevalent human inactivating ALDH2 E504K point mutation (ALDH2E504K) during aging. The liver metabolism was relatively resilient to aging, showing enhanced ALDH2 activity and improved mitochondrial coupling. Strikingly, aging-associated liver resilience was lost in ALDH2E504K mice. Aged hearts exhibited mixed outcomes including impaired mitochondrial basal respiration, improved ADP-driven respiration, and decreased ALDH2 detox capacity. The ALDH2E504K mutation exacerbated the already impaired cardiac ALDH2 detox capacity in aging. Strikingly, aging brain displayed pronounced vulnerability, with decreased ALDH2 activity, impaired mitochondrial bioenergetics and defective ALDH2 detox capacity. These changes were paralleled by impaired cognitive and behavioral functions in aged mice. As proof of concept, either the presence of ALDH2E504K mutation or acute ethanol challenge worsened cognitive and behavioral dysfunction in aging mice. Finally, we assessed in vitro efficacy of pharmacological ALDH2 activation in aging tissues. Collectively, these findings unravel the contribution of ALDH2E504K mutation to mitochondrial metabolism during aging; highlighting the detrimental synergy between genetic ALDH2 deficiency and aging in brain metabolism and physiology.

molecular biology↗

Ketone Body Metabolism is Not Required for Improvement of Heart Failure by Ketogenic Diet in Mice

Failing hearts increasingly metabolize ketone bodies, and enhancing ketosis improves heart failure (HF) remodeling. Circulating ketones are elevated by fasting/starvation, which is mimicked with a high-fat, low-carbohydrate "ketogenic diet" (KD). While speculated that KD improves HF through increased ketone oxidation, some evidence suggests KD paradoxically downregulates cardiac ketone oxidation despite increased ketone delivery. We sought to clarify the significance of cardiac ketone metabolism during KD in HF. Mice were subjected to transverse aortic constriction with apical myocardial infarction (TAC-MI) and fed either low-fat (LF) control or KD. Cardiac-specific mitochondrial pyruvate carrier 2 (csMPC2-/-) mice were used as a second model of heart failure. In both mice, feeding a KD improved HF, determined by echocardiography, heart weights, and gene expression analyses. Although KD increases plasma ketone bodies, gene expression for ketone metabolic genes is decreased in the hearts of KD-fed mice. Cardiac-specific {beta}-hydroxybutyrate dehydrogenase 1 (csBDH1-/-), the first enzyme in ketone catabolism, mice were also studied and crossed with the csMPC2-/-mice to create double knockout (DKO) mice. These mice were aged to 16 weeks and switched to LF or KD, and KD was able to completely normalize the hearts of both csMPC2-/- and DKO mice, suggesting that ketone metabolism is unnecessary for improving heart failure with ketogenic diet. These studies were then repeated, and mice injected with U-13C-{beta}-hydroxybutyrate to evaluate ketone metabolism. KD feeding significantly decreased the enrichment of the TCA cycle from ketone body carbons, as did the BDH1-deletion in DKO mice. Gene expression and respirometry suggests that KD instead increases cardiac fat oxidation. In conclusion, these results suggest that ketogenic diet decreases cardiac ketone metabolism and does not require ketone metabolism to improve heart failure.

physiology↗