scholarly journals Proteomic and Structural Manifestations of Cardiomyopathy in Rat Models of Obesity and Weight Loss

2021 ◽  
Vol 12 ◽  
Author(s):  
Arkadiusz D. Liśkiewicz ◽  
Łukasz Marczak ◽  
Katarzyna Bogus ◽  
Daniela Liśkiewicz ◽  
Marta Przybyła ◽  
...  
Keyword(s):  
Weight Loss ◽  
Glucose Transporter ◽  
Cardiac Tissue ◽  
After Effects ◽  
Glut 1 ◽  
Metabolic Substrates ◽  
Cardiac Phenotype ◽  
Obese Rats ◽  
Key Enzyme ◽  
Obesity Cardiomyopathy

Obesity cardiomyopathy increases the risk of heart failure and death. Obesity is curable, leading to the restoration of the heart phenotype, but it is not clear if there are any after-effects of obesity present after weight loss. We characterize the proteomic landscape of obesity cardiomyopathy with an evaluation of whether the cardiac phenotype is still shaped after weight loss. Cardiomyopathy was validated by cardiac hypertrophy, fibrosis, oversized myocytes, and mTOR upregulation in a rat model of cafeteria diet-induced developmental obesity. By global proteomic techniques (LC-MS/MS) a plethora of molecular changes was observed in the heart and circulation of obese animals, suggesting abnormal utilization of metabolic substrates. This was confirmed by increased levels of cardiac ACSL-1, a key enzyme for fatty acid degradation and decreased GLUT-1, a glucose transporter in obese rats. Calorie restriction and weight loss led to the normalization of the heart’s size, but fibrosis was still excessive. The proteomic compositions of cardiac tissue and plasma were different after weight loss as compared to control. In addition to morphological consequences, obesity cardiomyopathy involves many proteomic changes. Weight loss provides for a partial repair of the heart’s architecture, but the trace of fibrotic deposition and proteomic alterations may occur.

scholarly journals Proteomic and structural heart changes in obese rats are incompletely restored after weight loss

2020 ◽  
Author(s):  
Arkadiusz Liśkiewicz ◽  
Łukasz Marczak ◽  
Katarzyna Bogus ◽  
Daniela Liśkiewicz ◽  
Marta Przybyła ◽  
...  
Keyword(s):  
Weight Loss ◽  
Connective Tissue ◽  
Cardiac Fibrosis ◽  
Glucose Transporter ◽  
Cardiac Tissue ◽  
Proteomic Profiling ◽  
After Effects ◽  
Metabolic Substrates ◽  
Key Enzyme ◽  
Obesity Cardiomyopathy

Abstract Background As a systemic disorder, obesity strongly affects the cardiovascular system, inducing cardiac overgrowth, which increases the risk of heart failure and death. Moreover, obesity is potentially curable, leading to the restoration of the heart phenotype, but it is not clear if all of the after-effects are reversed after weight loss. of the heart phenotype, but it is not clear if all of the after-effects are reversed after weight loss. Here we describe the proteomic and morphologic phenotype of the heart in a rat model of developmental obesity with an evaluation of whether the observed effects are persistent in spite of weight loss. Methods Developmental obesity with hyperlipidemia and insulin resistance was induced in young rats by exposure to a Western diet composed of human snacks. An histologic evaluation of the heart was performed to measure the size of the cardiomyocytes and amount of connective tissue discriminating the phenotype of obesity cardiomyopathy. The cardiac tissue and plasma were analyzed by global proteomic profiling. Based on these data, we targeted proteins for evaluation with the western blot. The histological and proteomic measurements were performed after weight loss to validate which features of obesity cardiomyopathy were persistent. Results Obesity cardiomyopathy was determined as cardiac hypertrophy associated with fibrosis, oversized myocytes, and mTOR upregulation. A plethora of molecular changes were observed, suggesting an effect on the utilization of metabolic substrates in the hearts of obese animals. This was confirmed by increased levels of ACSL-1, a key enzyme for fatty acid degradation and decreased GLUT-1, a glucose transporter. Immunological processes and lipid metabolism were also affected in the cardiac tissue and plasma. Weight loss led to the normalization of the heart’s size, but some after-effects of obesity such as connective tissue abundance and abnormal proteomic composition were still persistent. Conclusion In addition to morphological consequences, obesity cardiomyopathy involves many proteomic changes. Obesity treatment and weight loss provides for a partial repair of the heart’s architecture, but cardiac fibrosis and some proteomic alterations persist.

Immunolocalization of GLUT-1 glucose transporter in rat skeletal muscle and in normal and hypoxic cardiac tissue

1993 ◽  
Vol 265 (3) ◽  
pp. E454-E464 ◽  
Author(s):  
C. L. Doria-Medina ◽  
D. D. Lund ◽  
A. Pasley ◽  
A. Sandra ◽  
W. I. Sivitz
Keyword(s):  
Skeletal Muscle ◽  
Cellular Localization ◽  
Glucose Transporter ◽  
Cardiac Tissue ◽  
Heart Tissue ◽  
Nerve Fibers ◽  
Cell Type ◽  
Cardiac Tissues ◽  
Type Distribution ◽  
Glut 1

We compared the expression and cell-type localization of GLUT-1 mRNA and protein between cardiac and skeletal muscle of normal rats. Also, since we recently showed that cardiac GLUT-1 is upregulated in rats exposed to hypobaric hypoxia, we examined the cellular localization of GLUT-1 in cardiac tissue of normal and hypoxic rats. Confocal light microscopy and double immunofluorescent labeling revealed intense localization of GLUT-1 around neurofilament immunoreactivity within gastrocnemius muscle consistent with the previously described localization of large amounts of GLUT-1 in perineurial sheaths of skeletal muscle. However, using the same methods, we were unable to visualize GLUT-1 adjacent to nerve fibers in numerous sections of right or left ventricles or atria. Compared with skeletal myoctes, however, GLUT-1 immunofluorescence among cardiomyocytes was much more intense, particularly along the plasma membrane and especially intercalated discs. GLUT-1 immunofluorescence was also seen within the walls of arterioles within the heart. The predominant localization of GLUT-1 expression to cardiomyocytes in heart tissue was confirmed by in situ mRNA hybridization to digoxigenin-conjugated GLUT-1 cDNA. Northern blot analysis demonstrated that GLUT-1 mRNA was increased severalfold in the cardiac tissues compared with skeletal muscle. Although we detected GLUT-1 protein by immunoblotting of detergent extracts of the heart, we could not detect GLUT-1 in similar extracts of skeletal muscle. The cell type distribution of GLUT-1 in hearts of hypoxic rats was not different by immunohistochemistry from normals. These data indicate that 1) the cell-type distribution of GLUT-1 in the heart differs markedly from that in skeletal muscle. GLUT-1 in cardiac tissue, unlike skeletal muscle, is predominantly expressed within myocytes. 2) Cardiac GLUT-1 is not located along nerve fibers. 3) GLUT-1 mRNA and protein levels in cardiac tissue are considerably greater than in skeletal muscle. 4) The hypoxia-induced increase in cardiac GLUT-1 that we previously reported must occur within cardiomyocytes.

Differential glycolytic and glycogenogenic transduction pathways in male and female bovine embryos produced in vitro

2012 ◽  
Vol 24 (2) ◽  
pp. 344 ◽  
Author(s):  
M. Garcia-Herreros ◽  
I. M. Aparicio ◽  
D. Rath ◽  
T. Fair ◽  
P. Lonergan
Keyword(s):  
Glucose Metabolism ◽  
Protein Expression ◽  
Glucose Uptake ◽  
Glucose Transporter ◽  
Glycogen Synthase ◽  
Bovine Embryos ◽  
High Concentration ◽  
Glucose Transporter 1 ◽  
Male And Female ◽  
Glut 1

Previous studies have shown that developmental kinetic rates following IVF are lower in female than in male blastocysts and that this may be related to differences in glucose metabolism. In addition, an inhibition of phosphatidylinositol 3-kinase (PI3-K) inhibits glucose uptake in murine blastocysts. Therefore, the aim of this study was to identify and compare the expression of proteins involved in glucose metabolism (hexokinase-I, HK-I; phosphofructokinase-1, PFK-1; pyruvate kinase1/2, PK1/2; glyceraldehyde-3-phosphate dehydrogenase, GAPDH; glucose transporter-1, GLUT-1; and glycogen synthase kinase-3, GSK-3) in male and female bovine blastocysts to determine whether PI3-K has a role in the regulation of the expression of these proteins. Hexokinase-I, PFK-1, PK1/2, GAPDH and GLUT-1 were present in bovine embryos. Protein expression of these proteins and GSK-3 was significantly higher in male compared with female blastocysts. Inhibition of PI3-K with LY294002 significantly decreased the expression of HK-I, PFK-1, GAPDH, GSK-3 A/B and GLUT-1. Results showed that the expression of glycolytic proteins HK-I, PFK-1, GAPDH and PK1/2, and the transporters GLUT-1 and GSK-3 is regulated by PI3-K in bovine blastocysts. Moreover, the differential protein expression observed between male and female blastocysts might explain the faster developmental kinetics seen in males, as the expression of main proteins involved in glycolysis and glycogenogenesis was significantly higher in male than female bovine embryos and also could explain the sensitivity of male embryos to a high concentration of glucose, as a positive correlation between GLUT-1 expression and glucose uptake in embryos has been demonstrated.

scholarly journals Topology of the Glut 1 glucose transporter deduced from glycosylation scanning mutagenesis.

1994 ◽  
Vol 269 (32) ◽  
pp. 20482-20488 ◽  
Author(s):  
R.C. Hresko ◽  
M. Kruse ◽  
M. Strube ◽  
M. Mueckler
Keyword(s):  
Glucose Transporter ◽  
Glut 1

Effect of endurance training on glucose transport capacity and glucose transporter expression in rat skeletal muscle

1990 ◽  
Vol 259 (6) ◽  
pp. E778-E786 ◽  
Author(s):  
T. Ploug ◽  
B. M. Stallknecht ◽  
O. Pedersen ◽  
B. B. Kahn ◽  
T. Ohkuwa ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Glucose Transport ◽  
Glucose Transporter ◽  
Training Session ◽  
Residual Effect ◽  
Exercise Session ◽  
Transport Capacity ◽  
Glut 1 ◽  
Glut 4 ◽  
Fast Twitch

The effect of 10 wk endurance swim training on 3-O-methylglucose (3-MG) uptake (at 40 mM 3-MG) in skeletal muscle was studied in the perfused rat hindquarter. Training resulted in an increase of approximately 33% for maximum insulin-stimulated 3-MG transport in fast-twitch red fibers and an increase of approximately 33% for contraction-stimulated transport in slow-twitch red fibers compared with nonexercised sedentary muscle. A fully additive effect of insulin and contractions was observed both in trained and untrained muscle. Compared with transport in control rats subjected to an almost exhaustive single exercise session the day before experiment both maximum insulin- and contraction-stimulated transport rates were increased in all muscle types in trained rats. Accordingly, the increased glucose transport capacity in trained muscle was not due to a residual effect of the last training session. Half-times for reversal of contraction-induced glucose transport were similar in trained and untrained muscles. The concentrations of mRNA for GLUT-1 (the erythrocyte-brain-Hep G2 glucose transporter) and GLUT-4 (the adipocyte-muscle glucose transporter) were increased approximately twofold by training in fast-twitch red muscle fibers. In parallel to this, Western blot demonstrated a approximately 47% increase in GLUT-1 protein and a approximately 31% increase in GLUT-4 protein. This indicates that the increases in maximum velocity for 3-MG transport in trained muscle is due to an increased number of glucose transporters.

scholarly journals The Ubiquitous Glucose Transporter GLUT-1 Is a Receptor for HTLV

Cell ◽  
2003 ◽  
Vol 115 (4) ◽  
pp. 449-459 ◽  
Author(s):  
Nicolas Manel ◽  
Felix J. Kim ◽  
Sandrina Kinet ◽  
Naomi Taylor ◽  
Marc Sitbon ◽  
...  
Keyword(s):  
Glucose Transporter ◽  
Glut 1

Interaction of Leptin and Amylin in the Long-term Maintenance of Weight Loss in Diet-induced Obese Rats

Obesity ◽  
2010 ◽  
Vol 18 (1) ◽  
pp. 21-26 ◽  
Author(s):  
James L. Trevaskis ◽  
Chunli Lei ◽  
Joy E. Koda ◽  
Christian Weyer ◽  
David G. Parkes ◽  
...  
Keyword(s):  
Weight Loss ◽  
Obese Rats ◽  
Term Maintenance
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