scholarly journals Sex differences in mitochondrial respiratory function in human skeletal muscle

2018 ◽  
Vol 314 (6) ◽  
pp. R909-R915 ◽  
Author(s):  
Paula M. Miotto ◽  
Chris McGlory ◽  
Tanya M. Holloway ◽  
Stuart M. Phillips ◽  
Graham P. Holloway
Keyword(s):  
Skeletal Muscle ◽  
Sex Differences ◽  
Human Skeletal Muscle ◽  
Muscle Metabolism ◽  
Adenosine Diphosphate ◽  
Men And Women ◽  
Respiration Rates ◽  
Malonyl Coa ◽  
Carnitine Palmitoyl Transferase I ◽  
Mitochondrial Respiratory

Mitochondrial bioenergetic contributions to sex differences in human skeletal muscle metabolism remain poorly defined. The primary aim of this study was to determine whether mitochondrial respiratory kinetics differed between healthy young men and women in permeabilized skeletal muscle fibers. While men and women displayed similar ( P > 0.05) maximal respiration rates and abundance of mitochondrial/adenosine diphosphate (ADP) transport proteins, women had lower ( P < 0.05) mitochondrial ADP sensitivity (+30% apparent Km) and absolute respiration rates at a physiologically relevant ADP concentration (100 μM). Moreover, although men and women exhibited similar carnitine palmitoyl transferase-I protein content- and palmitoyl-CoA-supported respiration, women displayed greater sensitivity to malonyl-CoA-mediated respiratory inhibition. These data establish baseline sex differences in mitochondrial bioenergetics and provide the foundation for studying mitochondrial function within the context of metabolic perturbations and diseases that affect men and women differently.

scholarly journals Sex Differences in Global mRNA Content of Human Skeletal Muscle

PLoS ONE ◽  
2009 ◽  
Vol 4 (7) ◽  
pp. e6335 ◽  
Author(s):  
Amy C. Maher ◽  
Minghua H. Fu ◽  
Robert J. Isfort ◽  
Alex R. Varbanov ◽  
Xiaoyan A. Qu ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Sex Differences ◽  
Human Skeletal Muscle ◽  
Mrna Content

Human skeletal muscle malonyl-CoA at rest and during prolonged submaximal exercise

1996 ◽  
Vol 270 (3) ◽  
pp. E541-E544 ◽  
Author(s):  
L. M. Odland ◽  
G. J. Heigenhauser ◽  
G. D. Lopaschuk ◽  
L. L. Spriet
Keyword(s):  
Skeletal Muscle ◽  
Fatty Acid ◽  
Fatty Acid Oxidation ◽  
High Performance ◽  
Human Skeletal Muscle ◽  
Vastus Lateralis ◽  
Submaximal Exercise ◽  
Acid Oxidation ◽  
Vastus Lateralis Muscle ◽  
Malonyl Coa

Previous literature has indicated that contraction-induced decreases in malonyl-CoA are instrumental in the regulation of fatty acid oxidation during prolonged submaximal exercise. This study was designed to measure malonyl-CoA in human vastus lateralis muscle at rest and during submaximal exercise. Eight males and one female cycled for 70 min (10 min at 40% and 60 min at 65% maximal O2 uptake). Needle biopsies were obtained at rest and at 10 min, 20 min, and 70 min of exercise. Malonyl-CoA content in preexercise biopsy samples determined by high-performance liquid chromatography (HPLC) was 1.53 +/- 0.18 micromol/kg dry mass (dm). Malonyl-CoA content did not change significantly during exercise (1.39 +/- 0.21 at 10 min, 1.46 +/- 0.14 at 20 min, and 1.22 +/- 0.15 micromol/kg dm at 70 min). In contrast, malonyl-CoA content determined by HPLC in perfused rat red gastrocnemius muscle decreased significantly during 20 min of stimulation at 0.7 Hz [3.44 +/- 0.54 to 1.64 +/- 0.23 nmol/g dm, (n=9)]. We conclude that human skeletal muscle malonyl-CoA content 1) is less than reported in rat skeletal muscle at rest, 2) does not decrease with prolonged submaximal exercise, and 3) is not predictive of increased fatty acid oxidation during exercise.

scholarly journals Observations on the affinity for carnitine, and malonyl-CoA sensitivity, of carnitine palmitoyltransferase I in animal and human tissues. Demonstration of the presence of malonyl-CoA in non-hepatic tissues of the rat

1983 ◽  
Vol 214 (1) ◽  
pp. 21-28 ◽  
Author(s):  
J D McGarry ◽  
S E Mills ◽  
C S Long ◽  
D W Foster
Keyword(s):  
Skeletal Muscle ◽  
Carnitine Palmitoyltransferase ◽  
Acid Oxidation ◽  
Long Chain Fatty Acid ◽  
Intracellular Location ◽  
Adult Rat ◽  
Malonyl Coa ◽  
Carnitine Palmitoyltransferase I ◽  
20 Nm ◽  
Carnitine Palmitoyl Transferase I

The requirement for carnitine and the malonyl-CoA sensitivity of carnitine palmitoyl-transferase I (EC 2.3.1.21) were measured in isolated mitochondria from eight tissues of animal or human origin using fixed concentrations of palmitoyl-CoA (50 microM) and albumin (147 microM). The Km for carnitine spanned a 20-fold range, rising from about 35 microM in adult rat and human foetal liver to 700 microM in dog heart. Intermediate values of increasing magnitude were found for rat heart, guinea pig liver and skeletal muscle of rat, dog and man. Conversely, the concentration of malonyl-CoA required for 50% suppression of enzyme activity fell from the region of 2-3 microM in human and rat liver to only 20 nM in tissues displaying the highest Km for carnitine. Thus, the requirement for carnitine and sensitivity to malonyl-CoA appeared to be inversely related. The Km of carnitine palmitoyltransferase I for palmitoyl-CoA was similar in tissues showing large differences in requirement for carnitine. Other experiments established that, in addition to liver, heart and skeletal muscle of fed rats contain significant quantities of malonyl-CoA and that in all three tissues the level falls with starvation. Although its intracellular location in heart and skeletal muscle is not known, the possibility is raised that malonyl-CoA (or a related compound) could, under certain circumstances, interact with carnitine palmitoyltransferase I in non-hepatic tissues and thereby exert control over long chain fatty acid oxidation.

Human Skeletal Muscle Metabolism in Iron Deficiency

1993 ◽  
Vol 84 (s28) ◽  
pp. 38P-38P ◽  
Author(s):  
CH Thompson ◽  
GJ Kemp ◽  
DJ Taylor ◽  
GK Radda ◽  
B Rajagopalan
Keyword(s):  
Skeletal Muscle ◽  
Iron Deficiency ◽  
Human Skeletal Muscle ◽  
Muscle Metabolism ◽  
Skeletal Muscle Metabolism

CPT I ACTIVITY AND MALONYL-COA SENSITIVITY IN AEROBICALLY TRAINED AND UNTRAINED HUMAN SKELETAL MUSCLE.

1998 ◽  
Vol 30 (Supplement) ◽  
pp. 137 ◽  
Author(s):  
E C Starritt ◽  
R A Howlett ◽  
G JF Heigenhauser ◽  
M Hargreaves ◽  
L L Spriet
Keyword(s):  
Skeletal Muscle ◽  
Human Skeletal Muscle ◽  
Malonyl Coa ◽  
Cpt I ◽  
Aerobically Trained

Effects of 7 wk of endurance training on human skeletal muscle metabolism during submaximal exercise

2004 ◽  
Vol 97 (6) ◽  
pp. 2148-2153 ◽  
Author(s):  
Paul J. LeBlanc ◽  
Krista R. Howarth ◽  
Martin J. Gibala ◽  
George J. F. Heigenhauser
Keyword(s):  
Skeletal Muscle ◽  
Endurance Training ◽  
Glycogen Phosphorylase ◽  
Human Skeletal Muscle ◽  
Vastus Lateralis ◽  
Muscle Metabolism ◽  
Allosteric Modulators ◽  
Before And After ◽  
First Time ◽  
Muscle Biopsies

This is the first study to examine the effects of endurance training on the activation state of glycogen phosphorylase (Phos) and pyruvate dehydrogenase (PDH) in human skeletal muscle during exercise. We hypothesized that 7 wk of endurance training (Tr) would result in a posttransformationally regulated decrease in flux through Phos and an attenuated activation of PDH during exercise due to alterations in key allosteric modulators of these important enzymes. Eight healthy men (22 ± 1 yr) cycled to exhaustion at the same absolute workload (206 ± 5 W; ∼80% of initial maximal oxygen uptake) before and after Tr. Muscle biopsies (vastus lateralis) were obtained at rest and after 5 and 15 min of exercise. Fifteen minutes of exercise post-Tr resulted in an attenuated activation of PDH (pre-Tr: 3.75 ± 0.48 vs. post-Tr: 2.65 ± 0.38 mmol·min−1·kg wet wt−1), possibly due in part to lower pyruvate content (pre-Tr: 0.94 ± 0.14 vs. post-Tr: 0.46 ± 0.03 mmol/kg dry wt). The decreased pyruvate availability during exercise post-Tr may be due to a decreased muscle glycogenolytic rate (pre-Tr: 13.22 ± 1.01 vs. post-Tr: 7.36 ± 1.26 mmol·min−1·kg dry wt−1). Decreased glycogenolysis was likely mediated, in part, by posttransformational regulation of Phos, as evidenced by smaller net increases in calculated muscle free ADP (pre-Tr: 111 ± 16 vs. post-Tr: 84 ± 10 μmol/kg dry wt) and Pi (pre-Tr: 57.1 ± 7.9 vs. post-Tr: 28.6 ± 5.6 mmol/kg dry wt). We have demonstrated for the first time that several signals act to coordinately regulate Phos and PDH, and thus carbohydrate metabolism, in human skeletal muscle after 7 wk of endurance training.

scholarly journals Genome-wide DNA methylation and transcriptome integration reveal distinct sex differences in skeletal muscle.

2021 ◽  
Author(s):  
Shanie Landen ◽  
Macsue Jacques ◽  
Danielle Hiam ◽  
Javier Alvarez Romero ◽  
Nicholas R Harvey ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Dna Methylation ◽  
Sex Differences ◽  
Complex Traits ◽  
Human Skeletal Muscle ◽  
Gene Set Enrichment Analysis ◽  
P Value ◽  
Transcriptional Level ◽  
Differentially Methylated Genes ◽  
Males And Females

Nearly all human complex traits and diseases exhibit some degree of sex differences, and epigenetics contributes to these differences as DNA methylation shows sex differences in various tissues. However, skeletal muscle epigenetic sex differences remain largely unexplored, yet skeletal muscle displays distinct sex differences at the transcriptome level. We conducted a large-scale meta-analysis of autosomal DNA methylation sex differences in human skeletal muscle in three separate cohorts (Gene SMART, FUSION, and GSE38291), totalling n = 369 human muscle samples (n = 222 males, n = 147 females). We found 10,240 differentially methylated regions (DMRs) at FDR < 0.005, 94% of which were hypomethylated in males, and gene set enrichment analysis revealed that differentially methylated genes were involved in muscle contraction and metabolism. We then integrated our epigenetic results with transcriptomic data from the GTEx database and the FUSION cohort. Altogether, we identified 326 autosomal genes that display sex differences at both the DNA methylation, and transcriptome levels. Importantly, sex-biased genes at the transcriptional level were overrepresented among the sex-biased genes at the epigenetic level (p-value = 4.6e-13), which suggests differential DNA methylation and gene expression between males and females in muscle are functionally linked. In conclusion, we uncovered thousands of genes that exhibit DNA methylation differences between the males and females in human skeletal muscle that may modulate mechanisms controlling muscle metabolism and health.

scholarly journals Resting skeletal muscle PNPLA2 (ATGL) and CPT1B are associated with peak fat oxidation rates in men and women but do not explain observed sex differences

2021 ◽  
Vol 106 (5) ◽  
pp. 1208-1223 ◽  
Author(s):  
Oliver J. Chrzanowski‐Smith ◽  
Robert M. Edinburgh ◽  
Eleanor Smith ◽  
Mark P. Thomas ◽  
Jean‐Philippe Walhin ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Sex Differences ◽  
Fat Oxidation ◽  
Men And Women ◽  
Oxidation Rates
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