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Article ; Online: Metformin treatment for 8 days impacts multiple intestinal parameters in high-fat high-sucrose fed mice.

Bravard, Amélie / Gérard, Céline / Defois, Clémence / Benoit, Bérengère / Makki, Kassem / Meugnier, Emmanuelle / Rainteau, Dominique / Rieusset, Jennifer / Godet, Murielle / Vidal, Hubert

Scientific reports

2021 Volume 11, Issue 1, Page(s) 16684

Abstract: Although the mechanism of action of the antidiabetic drug metformin is still a matter of discussions, it is well accepted that the gut plays an important role. To gain more insights into the mechanisms occurring in the different regions of the intestine, ...

Abstract	Although the mechanism of action of the antidiabetic drug metformin is still a matter of discussions, it is well accepted that the gut plays an important role. To gain more insights into the mechanisms occurring in the different regions of the intestine, adult male mice were fed a high-fat-high sucrose (HFS) diet for 8 days and treated with metformin by gavage (300 mg/day/kg body weight) during the HFS diet. Metformin counteracted HFS diet-induced overexpression of a network of genes involved in the transport of glucose and fatty acids in the different regions of the small intestine. It also induced beneficial modification of secondary bile acid profile in the caecum, with a reduction of deoxycholic acid and lithocholic acid levels and increased abundance of ursodeoxycholic acid and tauroursodeoxycholic acid, potentially leading to FRX inhibition. In parallel, metformin treatment was associated with specific changes of the microbiota composition in the lumen of the different regions of the intestine. Metformin induced a marked increase in the abundance of Akkermansia muciniphila in the lumen all along the gut and counteracted the effects of HFS diet on the abundances of some bacterial groups generally associated with metabolic disturbances (f-Lachnospiraceae, f-Petostreptococcaceae, g-Clostidium). Therefore, the present work clearly emphasises the role of all the regions of the intestinal tract in the beneficial action of the antidiabetic drug metformin in a prediabetic mouse model.
MeSH term(s)	Animals ; Diet, Carbohydrate Loading/adverse effects ; Dietary Sucrose/metabolism ; Gastrointestinal Microbiome/drug effects ; Hypoglycemic Agents/pharmacology ; Hypoglycemic Agents/therapeutic use ; Intestinal Mucosa/drug effects ; Intestinal Mucosa/metabolism ; Intestines/drug effects ; Male ; Metformin/pharmacology ; Metformin/therapeutic use ; Mice ; Mice, Inbred C57BL ; Prediabetic State/drug therapy ; Prediabetic State/etiology ; Prediabetic State/metabolism ; Prediabetic State/microbiology
Chemical Substances	Dietary Sucrose ; Hypoglycemic Agents ; Metformin (9100L32L2N)
Language	English
Publishing date	2021-08-17
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-021-95117-0
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Metformin treatment for 8 days impacts multiple intestinal parameters in high-fat high-sucrose fed mice

Amélie Bravard / Céline Gérard / Clémence Defois / Bérengère Benoit / Kassem Makki / Emmanuelle Meugnier / Dominique Rainteau / Jennifer Rieusset / Murielle Godet / Hubert Vidal

Scientific Reports, Vol 11, Iss 1, Pp 1-

2021 Volume 12

Abstract: Abstract Although the mechanism of action of the antidiabetic drug metformin is still a matter of discussions, it is well accepted that the gut plays an important role. To gain more insights into the mechanisms occurring in the different regions of the ... ...

Abstract	Abstract Although the mechanism of action of the antidiabetic drug metformin is still a matter of discussions, it is well accepted that the gut plays an important role. To gain more insights into the mechanisms occurring in the different regions of the intestine, adult male mice were fed a high-fat-high sucrose (HFS) diet for 8 days and treated with metformin by gavage (300 mg/day/kg body weight) during the HFS diet. Metformin counteracted HFS diet-induced overexpression of a network of genes involved in the transport of glucose and fatty acids in the different regions of the small intestine. It also induced beneficial modification of secondary bile acid profile in the caecum, with a reduction of deoxycholic acid and lithocholic acid levels and increased abundance of ursodeoxycholic acid and tauroursodeoxycholic acid, potentially leading to FRX inhibition. In parallel, metformin treatment was associated with specific changes of the microbiota composition in the lumen of the different regions of the intestine. Metformin induced a marked increase in the abundance of Akkermansia muciniphila in the lumen all along the gut and counteracted the effects of HFS diet on the abundances of some bacterial groups generally associated with metabolic disturbances (f-Lachnospiraceae, f-Petostreptococcaceae, g-Clostidium). Therefore, the present work clearly emphasises the role of all the regions of the intestinal tract in the beneficial action of the antidiabetic drug metformin in a prediabetic mouse model.
Keywords	Medicine ; R ; Science ; Q
Subject code	630
Language	English
Publishing date	2021-08-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: The expression of FTO in human adipose tissue is influenced by fat depot, adiposity, and insulin sensitivity.

Bravard, Amélie / Veilleux, Alain / Disse, Emmanuel / Laville, Martine / Vidal, Hubert / Tchernof, André / Rieusset, Jennifer

Obesity (Silver Spring, Md.)

2013 Volume 21, Issue 6, Page(s) 1165–1173

Abstract: Objective: The fat mass and obesity associated (FTO) gene is related to obesity, but the regulation of FTO expression in adipose tissue is not fully understood. We investigated FTO expression in paired subcutaneous and omental adipose tissues (SAT and ... ...

Abstract	Objective: The fat mass and obesity associated (FTO) gene is related to obesity, but the regulation of FTO expression in adipose tissue is not fully understood. We investigated FTO expression in paired subcutaneous and omental adipose tissues (SAT and OAT) from healthy women undergoing gynecological surgeries, and its relation with adiposity and insulin sensitivity. Design and methods: FTO expression in SAT of type 2 diabetic patients treated or not with Rosiglitazone was also compared. Results: Both the mRNA and protein levels of FTO were higher in OAT from women than in SAT. Only OAT FTO protein levels negatively correlated with BMI and body fat mass, whereas SAT FTO mRNA levels were negatively correlated with subcutaneous fat deposition. In addition, SAT FTO mRNA and protein levels were increased in insulin resistant women (high HOMA) compared to insulin sensitive women (low HOMA), whereas OAT FTO expression was not different between these two subgroups. Interestingly, FTO mRNA levels were increased in SAT of type 2 diabetic patients, and treatment of diabetics with Rosiglitazone improved insulin sensitivity and reduced SAT FTO mRNA levels. Lastly, FTO expression was transiently increased in the early phase of 3T3-L1 cell differentiation, which coincides with the induction of PPARγ2 expression. However, partial reduction of FTO did not impact PPARγ2 expression and adipocyte differentiation. Conclusion: Therefore, FTO gene expression is higher in OAT than in SAT in lean to moderately obese women. OAT FTO expression is associated with adiposity, whereas SAT FTO expression is associated with insulin sensitivity. These associations are independent of an effect of FTO on adipocyte differentiation.
MeSH term(s)	3T3-L1 Cells ; Adipogenesis/genetics ; Adipose Tissue/metabolism ; Adiposity/physiology ; Adult ; Alpha-Ketoglutarate-Dependent Dioxygenase FTO ; Animals ; Body Mass Index ; Cell Differentiation ; Diabetes Mellitus, Type 2/genetics ; Diabetes Mellitus, Type 2/metabolism ; Female ; Gene Expression ; Humans ; Hypoglycemic Agents/pharmacology ; Insulin Resistance/physiology ; Male ; Mice ; Middle Aged ; Obesity/genetics ; Obesity/metabolism ; Omentum/metabolism ; PPAR gamma/genetics ; PPAR gamma/metabolism ; Proteins/genetics ; Proteins/metabolism ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Thiazolidinediones/pharmacology
Chemical Substances	Hypoglycemic Agents ; PPAR gamma ; Proteins ; RNA, Messenger ; Thiazolidinediones ; rosiglitazone (05V02F2KDG) ; Alpha-Ketoglutarate-Dependent Dioxygenase FTO (EC 1.14.11.33) ; FTO protein, human (EC 1.14.11.33)
Language	English
Publishing date	2013-06
Publishing country	United States
Document type	Journal Article
ZDB-ID	2230457-5
ISSN	1930-739X ; 1071-7323 ; 1930-7381
ISSN (online)	1930-739X
ISSN	1071-7323 ; 1930-7381
DOI	10.1002/oby.20110
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Article ; Online: FTO contributes to hepatic metabolism regulation through regulation of leptin action and STAT3 signalling in liver.

Bravard, Amélie / Vial, Guillaume / Chauvin, Marie-Agnès / Rouillé, Yves / Bailleul, Bernard / Vidal, Hubert / Rieusset, Jennifer

Cell communication and signaling : CCS

2014 Volume 12, Page(s) 4

Abstract: Background: The fat mass and obesity associated (FTO) gene is related to obesity and type 2 diabetes, but its function is still largely unknown. A link between leptin receptor-signal transducers and activators of transcription 3 (LepR-STAT3) signalling ... ...

Abstract	Background: The fat mass and obesity associated (FTO) gene is related to obesity and type 2 diabetes, but its function is still largely unknown. A link between leptin receptor-signal transducers and activators of transcription 3 (LepR-STAT3) signalling pathway and FTO was recently suggested in the hypothalamus. Because of the presence of FTO in liver and the role of LepR-STAT3 in the control of hepatic metabolism, we investigated both in vitro and in vivo the potential interrelationship between FTO and LepR-STAT3 signalling pathway in liver and the impact of FTO overexpression on leptin action and glucose homeostasis in liver of mice. Results: We found that FTO protein expression is regulated by both leptin and IL-6, concomitantly to an induction of STAT3 tyrosine phosphorylation, in leptin receptor (LepRb) expressing HuH7 cells. In addition, FTO overexpression in vitro altered both leptin-induced Y705 and S727 STAT3 phosphorylation, leading to dysregulation of glucose-6-phosphatase (G6P) expression and mitochondrial density, respectively. In vivo, liver specific FTO overexpression in mice induced a reducetion of Y705 phosphorylation of STAT3 in nuclear fraction, associated with reduced SOCS3 and LepR mRNA levels and with an increased G6P expression. Interestingly, FTO overexpression also induced S727 STAT3 phosphorylation in liver mitochondria, resulting in an increase of mitochondria function and density. Altogether, these data indicate that FTO promotes mitochondrial recruitment of STAT3 to the detriment of its nuclear localization, affecting in turn oxidative metabolism and the expression of leptin-targeted genes. Interestingly, these effects were associated in mice with alterations of leptin action and hyperleptinemia, as well as hyperglycemia, hyperinsulinemia and glucose intolerance. Conclusions: Altogether, these data point a novel regulatory loop between FTO and leptin-STAT3 signalling pathways in liver cells, and highlight a new role of FTO in the regulation of hepatic leptin action and glucose metabolism.
MeSH term(s)	Alpha-Ketoglutarate-Dependent Dioxygenase FTO ; Animals ; Cell Line, Tumor ; Cells, Cultured ; Glucose-6-Phosphate/metabolism ; Humans ; Liver/metabolism ; Mice ; Mice, Inbred C57BL ; Mitochondria, Liver/metabolism ; Mixed Function Oxygenases/genetics ; Mixed Function Oxygenases/metabolism ; Mutation ; Oxo-Acid-Lyases/genetics ; Oxo-Acid-Lyases/metabolism ; Protein Transport ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Rats ; Receptors, Leptin/genetics ; Receptors, Leptin/metabolism ; STAT3 Transcription Factor/genetics ; STAT3 Transcription Factor/metabolism ; Signal Transduction ; Suppressor of Cytokine Signaling 3 Protein ; Suppressor of Cytokine Signaling Proteins/genetics ; Suppressor of Cytokine Signaling Proteins/metabolism
Chemical Substances	RNA, Messenger ; Receptors, Leptin ; STAT3 Transcription Factor ; Socs3 protein, mouse ; Suppressor of Cytokine Signaling 3 Protein ; Suppressor of Cytokine Signaling Proteins ; leptin receptor, mouse ; Glucose-6-Phosphate (56-73-5) ; Mixed Function Oxygenases (EC 1.-) ; FTO protein, mouse (EC 1.14.11.-) ; Alpha-Ketoglutarate-Dependent Dioxygenase FTO (EC 1.14.11.33) ; Oxo-Acid-Lyases (EC 4.1.3.-)
Language	English
Publishing date	2014-01-10
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1478-811X
ISSN (online)	1478-811X
DOI	10.1186/1478-811X-12-4
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Article ; Online: Reduction of endoplasmic reticulum stress using chemical chaperones or Grp78 overexpression does not protect muscle cells from palmitate-induced insulin resistance.

Rieusset, Jennifer / Chauvin, Marie-Agnès / Durand, Annie / Bravard, Amélie / Laugerette, Fabienne / Michalski, Marie-Caroline / Vidal, Hubert

Biochemical and biophysical research communications

2012 Volume 417, Issue 1, Page(s) 439–445

Abstract: Endoplasmic reticulum (ER) stress is proposed as a novel link between elevated fatty acids levels, obesity and insulin resistance in liver and adipose tissue. However, it is unknown whether ER stress also contributes to lipid-induced insulin resistance ... ...

Abstract	Endoplasmic reticulum (ER) stress is proposed as a novel link between elevated fatty acids levels, obesity and insulin resistance in liver and adipose tissue. However, it is unknown whether ER stress also contributes to lipid-induced insulin resistance in skeletal muscle, the major tissue responsible of insulin-stimulated glucose disposal. Here, we investigated the possible role of ER stress in palmitate-induced alterations of insulin action, both in vivo, in gastrocnemius of high-palm diet fed mice, and in vitro, in palmitate-treated C(2)C(12) myotubes. We demonstrated that 8 weeks of high-palm diet increased the expression of ER stress markers in muscle of mice, whereas ex-vivo insulin-stimulated PKB phosphorylation was not altered in this tissue. In addition, exposure of C(2)C(12) myotubes to either tuncamycine or palmitate induced ER stress and altered insulin-stimulated PKB phosphorylation. However, alleviation of ER stress by either TUDCA or 4-PBA treatments, or by overexpressing Grp78, did not restore palmitate-induced reduction of insulin-stimulated PKB phosphorylation in C(2)C(12) myotubes. This work highlights that, even ER stress is associated with palmitate-induced alterations of insulin signaling, ER stress is likely not the major culprit of this effect in myotubes, suggesting that the previously proposed link between ER stress and insulin resistance is less important in skeletal muscle than in adipose tissue and liver.
MeSH term(s)	Animals ; Butylamines/pharmacology ; Diet/adverse effects ; Dietary Fats/administration & dosage ; Dietary Fats/adverse effects ; Dietary Fats/pharmacology ; Endoplasmic Reticulum Stress/drug effects ; Endoplasmic Reticulum Stress/genetics ; Endoplasmic Reticulum Stress/physiology ; Heat-Shock Proteins/biosynthesis ; Heat-Shock Proteins/genetics ; Insulin/metabolism ; Insulin/pharmacology ; Insulin Resistance ; Male ; Mice ; Mice, Inbred C57BL ; Muscle Fibers, Skeletal/drug effects ; Muscle Fibers, Skeletal/physiology ; Palmitates/administration & dosage ; Palmitates/adverse effects ; Palmitates/pharmacology ; Taurochenodeoxycholic Acid/pharmacology ; Tunicamycin/pharmacology
Chemical Substances	4-phenylbutylamine ; Butylamines ; Dietary Fats ; Heat-Shock Proteins ; Insulin ; Palmitates ; molecular chaperone GRP78 ; Tunicamycin (11089-65-9) ; Taurochenodeoxycholic Acid (516-35-8) ; tauroursodeoxycholic acid (60EUX8MN5X)
Language	English
Publishing date	2012-01-06
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	205723-2
ISSN	1090-2104 ; 0006-291X ; 0006-291X
ISSN (online)	1090-2104 ; 0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2011.11.135
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Article ; Online: Inhibition of xanthine oxidase reduces hyperglycemia-induced oxidative stress and improves mitochondrial alterations in skeletal muscle of diabetic mice.

Bravard, Amélie / Bonnard, Charlotte / Durand, Annie / Chauvin, Marie-Agnès / Favier, Roland / Vidal, Hubert / Rieusset, Jennifer

American journal of physiology. Endocrinology and metabolism

2011 Volume 300, Issue 3, Page(s) E581–91

Abstract: Reactive oxygen species (ROS) have been widely implicated in the pathogenesis of diabetes and more recently in mitochondrial alterations in skeletal muscle of diabetic mice. However, so far the exact sources of ROS in skeletal muscle have remained ... ...

Abstract	Reactive oxygen species (ROS) have been widely implicated in the pathogenesis of diabetes and more recently in mitochondrial alterations in skeletal muscle of diabetic mice. However, so far the exact sources of ROS in skeletal muscle have remained elusive. Aiming at better understanding the causes of mitochondrial alterations in diabetic muscle, we designed this study to characterize the sites of ROS production in skeletal muscle of streptozotocin (STZ)-induced diabetic mice. Hyperglycemic STZ mice showed increased markers of systemic and muscular oxidative stress, as evidenced by increased circulating H(2)O(2) and muscle carbonylated protein levels. Interestingly, insulin treatment reduced hyperglycemia and improved systemic and muscular oxidative stress in STZ mice. We demonstrated that increased oxidative stress in muscle of STZ mice is associated with an increase of xanthine oxidase (XO) expression and activity and is mediated by an induction of H(2)O(2) production by both mitochondria and XO. Finally, treatment of STZ mice, as well as high-fat and high-sucrose diet-fed mice, with oxypurinol reduced markers of systemic and muscular oxidative stress and prevented structural and functional mitochondrial alterations, confirming the in vivo relevance of XO in ROS production in diabetic mice. These data indicate that mitochondria and XO are the major sources of hyperglycemia-induced ROS production in skeletal muscle and that the inhibition of XO reduces oxidative stress and improves mitochondrial alterations in diabetic muscle.
MeSH term(s)	Adenosine Triphosphate/biosynthesis ; Animals ; Antioxidants/metabolism ; Diabetes Mellitus, Experimental/enzymology ; Diabetes Mellitus, Experimental/metabolism ; Diabetes Mellitus, Type 1/chemically induced ; Diabetes Mellitus, Type 1/metabolism ; Diabetes Mellitus, Type 2/chemically induced ; Diabetes Mellitus, Type 2/metabolism ; Diet ; Enzyme Inhibitors/pharmacology ; Hydrogen Peroxide/metabolism ; Hyperglycemia/complications ; Insulin/metabolism ; Male ; Mice ; Mice, Inbred C57BL ; Microscopy, Electron, Transmission ; Mitochondria, Muscle/enzymology ; Mitochondria, Muscle/physiology ; Muscle, Skeletal/enzymology ; Muscle, Skeletal/metabolism ; Oxidative Stress/physiology ; Oxypurinol/pharmacology ; Protein Carbonylation/drug effects ; RNA/genetics ; Reverse Transcriptase Polymerase Chain Reaction ; Xanthine Oxidase/antagonists & inhibitors
Chemical Substances	Antioxidants ; Enzyme Inhibitors ; Insulin ; RNA (63231-63-0) ; Adenosine Triphosphate (8L70Q75FXE) ; Hydrogen Peroxide (BBX060AN9V) ; Xanthine Oxidase (EC 1.17.3.2) ; Oxypurinol (G97OZE5068)
Language	English
Publishing date	2011-03
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	603841-4
ISSN	1522-1555 ; 0193-1849
ISSN (online)	1522-1555
ISSN	0193-1849
DOI	10.1152/ajpendo.00455.2010
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Article: Reduction of endoplasmic reticulum stress using chemical chaperones or Grp78 overexpression does not protect muscle cells from palmitate-induced insulin resistance

Rieusset, Jennifer / Chauvin, Marie-Agnès / Durand, Annie / Bravard, Amélie / Laugerette, Fabienne / Michalski, Marie-Caroline / Vidal, Hubert

Biochemical and biophysical research communications. 2012 Jan. 6, v. 417, no. 1

2012

Abstract	Endoplasmic reticulum (ER) stress is proposed as a novel link between elevated fatty acids levels, obesity and insulin resistance in liver and adipose tissue. However, it is unknown whether ER stress also contributes to lipid-induced insulin resistance in skeletal muscle, the major tissue responsible of insulin-stimulated glucose disposal. Here, we investigated the possible role of ER stress in palmitate-induced alterations of insulin action, both in vivo, in gastrocnemius of high-palm diet fed mice, and in vitro, in palmitate-treated C₂C₁₂ myotubes. We demonstrated that 8weeks of high-palm diet increased the expression of ER stress markers in muscle of mice, whereas ex-vivo insulin-stimulated PKB phosphorylation was not altered in this tissue. In addition, exposure of C₂C₁₂ myotubes to either tuncamycine or palmitate induced ER stress and altered insulin-stimulated PKB phosphorylation. However, alleviation of ER stress by either TUDCA or 4-PBA treatments, or by overexpressing Grp78, did not restore palmitate-induced reduction of insulin-stimulated PKB phosphorylation in C₂C₁₂ myotubes. This work highlights that, even ER stress is associated with palmitate-induced alterations of insulin signaling, ER stress is likely not the major culprit of this effect in myotubes, suggesting that the previously proposed link between ER stress and insulin resistance is less important in skeletal muscle than in adipose tissue and liver.
Keywords	adipose tissue ; diet ; endoplasmic reticulum ; fatty acids ; glucose ; insulin ; insulin resistance ; liver ; mice ; muscles ; myocytes ; obesity ; phosphorylation ; skeletal muscle
Language	English
Dates of publication	2012-0106
Size	p. 439-445.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	205723-2
ISSN	0006-291X ; 0006-291X
ISSN (online)	0006-291X
ISSN	0006-291X
DOI	10.1016/j.bbrc.2011.11.135
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Article ; Online: Mitochondria-associated endoplasmic reticulum membrane (MAM) integrity is required for insulin signaling and is implicated in hepatic insulin resistance.

Tubbs, Emily / Theurey, Pierre / Vial, Guillaume / Bendridi, Nadia / Bravard, Amélie / Chauvin, Marie-Agnès / Ji-Cao, Jingwei / Zoulim, Fabien / Bartosch, Birke / Ovize, Michel / Vidal, Hubert / Rieusset, Jennifer

Diabetes

2014 Volume 63, Issue 10, Page(s) 3279–3294

Abstract: Mitochondria-associated endoplasmic reticulum (ER) membranes (MAMs) are functional domains between both organelles involved in Ca(2+) exchange, through the voltage-dependent anion channel (VDAC)-1/glucose-regulated protein 75 (Grp75)/inositol 1,4,5- ... ...

Abstract	Mitochondria-associated endoplasmic reticulum (ER) membranes (MAMs) are functional domains between both organelles involved in Ca(2+) exchange, through the voltage-dependent anion channel (VDAC)-1/glucose-regulated protein 75 (Grp75)/inositol 1,4,5-triphosphate receptor (IP3R)-1 complex, and regulating energy metabolism. Whereas mitochondrial dysfunction, ER stress, and altered Ca(2+) homeostasis are associated with altered insulin signaling, the implication of MAM dysfunctions in insulin resistance is unknown. Here we validated an approach based on in situ proximity ligation assay to detect and quantify VDAC1/IP3R1 and Grp75/IP3R1 interactions at the MAM interface. We demonstrated that MAM integrity is required for insulin signaling and that induction of MAM prevented palmitate-induced alterations of insulin signaling in HuH7 cells. Disruption of MAM integrity by genetic or pharmacological inhibition of the mitochondrial MAM protein, cyclophilin D (CypD), altered insulin signaling in mouse and human primary hepatocytes and treatment of CypD knockout mice with metformin improved both insulin sensitivity and MAM integrity. Furthermore, ER-mitochondria interactions are altered in liver of both ob/ob and diet-induced insulin-resistant mice and improved by rosiglitazone treatment in the latter. Finally, increasing organelle contacts by overexpressing CypD enhanced insulin action in primary hepatocytes of diabetic mice. Collectively, our data reveal a new role of MAM integrity in hepatic insulin action and resistance, providing a novel target for the modulation of insulin action.
MeSH term(s)	Animals ; Cell Line ; Cells, Cultured ; Endoplasmic Reticulum/metabolism ; Hepatocytes/cytology ; Hepatocytes/metabolism ; Humans ; Insulin/metabolism ; Insulin Resistance/physiology ; Intracellular Membranes/metabolism ; Liver/metabolism ; Male ; Mice ; Mice, Inbred C57BL ; Mitochondria/metabolism ; Signal Transduction/physiology
Chemical Substances	Insulin
Language	English
Publishing date	2014-10
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80085-5
ISSN	1939-327X ; 0012-1797
ISSN (online)	1939-327X
ISSN	0012-1797
DOI	10.2337/db13-1751
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Article ; Online: Insulin resistance is associated with MCP1-mediated macrophage accumulation in skeletal muscle in mice and humans.

Patsouris, David / Cao, Jingwei-Ji / Vial, Guillaume / Bravard, Amelie / Lefai, Etienne / Durand, Annie / Durand, Christine / Chauvin, Marie-Agnés / Laugerette, Fabienne / Debard, Cyrille / Michalski, Marie-Caroline / Laville, Martine / Vidal, Hubert / Rieusset, Jennifer

PloS one

2014 Volume 9, Issue 10, Page(s) e110653

Abstract: Inflammation is now recognized as a major factor contributing to type 2 diabetes (T2D). However, while the mechanisms and consequences associated with white adipose tissue inflammation are well described, very little is known concerning the situation in ... ...

Abstract	Inflammation is now recognized as a major factor contributing to type 2 diabetes (T2D). However, while the mechanisms and consequences associated with white adipose tissue inflammation are well described, very little is known concerning the situation in skeletal muscle. The aim of this study was to investigate, in vitro and in vivo, how skeletal muscle inflammation develops and how in turn it modulates local and systemic insulin sensitivity in different mice models of T2D and in humans, focusing on the role of the chemokine MCP1. Here, we found that skeletal muscle inflammation and macrophage markers are increased and associated with insulin resistance in mice models and humans. In addition, we demonstrated that intra-muscular TNFα expression is exclusively restricted to the population of intramuscular leukocytes and that the chemokine MCP1 was associated with skeletal muscle inflammatory markers in these models. Furthermore, we demonstrated that exposure of C2C12 myotubes to palmitate elevated the production of the chemokine MCP1 and that the muscle-specific overexpression of MCP1 in transgenic mice induced the local recruitment of macrophages and altered local insulin sensitivity. Overall our study demonstrates that skeletal muscle inflammation is clearly increased in the context of T2D in each one of the models we investigated, which is likely consecutive to the lipotoxic environment generated by peripheral insulin resistance, further increasing MCP1 expression in muscle. Consequently, our results suggest that MCP1-mediated skeletal muscle macrophages recruitment plays a role in the etiology of T2D.
MeSH term(s)	Animals ; Cell Line ; Cell Movement ; Chemokine CCL2/physiology ; Diabetes Mellitus, Type 2/immunology ; Diabetes Mellitus, Type 2/metabolism ; Humans ; Insulin Resistance/immunology ; Macrophages/immunology ; Male ; Mice, Inbred C57BL ; Mice, Obese ; Mice, Transgenic ; Muscle, Skeletal/immunology ; Muscle, Skeletal/metabolism ; Muscle, Skeletal/pathology ; Myositis/immunology ; Myositis/metabolism
Chemical Substances	Ccl2 protein, mouse ; Chemokine CCL2
Language	English
Publishing date	2014-10-22
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1932-6203
ISSN (online)	1932-6203
DOI	10.1371/journal.pone.0110653
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Article ; Online: Disruption of calcium transfer from ER to mitochondria links alterations of mitochondria-associated ER membrane integrity to hepatic insulin resistance.

Diabetologia

2015 Volume 59, Issue 3, Page(s) 614–623

Abstract: Aims/hypothesis: Mitochondria-associated endoplasmic reticulum membranes (MAMs) are regions of the endoplasmic reticulum (ER) tethered to mitochondria and controlling calcium (Ca(2+)) transfer between both organelles through the complex formed between ... ...

Abstract	Aims/hypothesis: Mitochondria-associated endoplasmic reticulum membranes (MAMs) are regions of the endoplasmic reticulum (ER) tethered to mitochondria and controlling calcium (Ca(2+)) transfer between both organelles through the complex formed between the voltage-dependent anion channel, glucose-regulated protein 75 and inositol 1,4,5-triphosphate receptor (IP3R). We recently identified cyclophilin D (CYPD) as a new partner of this complex and demonstrated a new role for MAMs in the control of insulin's action in the liver. Here, we report on the mechanisms by which disruption of MAM integrity induces hepatic insulin resistance in CypD (also known as Ppif)-knockout (KO) mice. Methods: We used either in vitro pharmacological and genetic inhibition of CYPD in HuH7 cells or in vivo loss of CYPD in mice to investigate ER-mitochondria interactions, inter-organelle Ca(2+) exchange, organelle homeostasis and insulin action. Results: Pharmacological and genetic inhibition of CYPD concomitantly reduced ER-mitochondria interactions, inhibited inter-organelle Ca(2+) exchange, induced ER stress and altered insulin signalling in HuH7 cells. In addition, histamine-stimulated Ca(2+) transfer from ER to mitochondria was blunted in isolated hepatocytes of CypD-KO mice and this was associated with an increase in ER calcium store. Interestingly, disruption of inter-organelle Ca(2+) transfer was associated with ER stress, mitochondrial dysfunction, lipid accumulation, activation of c-Jun N-terminal kinase (JNK) and protein kinase C (PKC)ε and insulin resistance in liver of CypD-KO mice. Finally, CYPD-related alterations of insulin signalling were mediated by activation of PKCε rather than JNK in HuH7 cells. Conclusions/interpretation: Disruption of IP3R-mediated Ca(2+) signalling in the liver of CypD-KO mice leads to hepatic insulin resistance through disruption of organelle interaction and function, increase in lipid accumulation and activation of PKCε. Modulation of ER-mitochondria Ca(2+) exchange may thus provide an exciting new avenue for treating hepatic insulin resistance.
MeSH term(s)	Animals ; Calcium/metabolism ; Cell Line ; Peptidyl-Prolyl Isomerase F ; Cyclophilins/genetics ; Cyclophilins/metabolism ; Endoplasmic Reticulum/metabolism ; Hepatocytes/metabolism ; Humans ; Inositol 1,4,5-Trisphosphate Receptors/metabolism ; Insulin Resistance/physiology ; Liver/metabolism ; Male ; Mice ; Mice, Knockout ; Mitochondria/metabolism
Chemical Substances	Peptidyl-Prolyl Isomerase F ; Inositol 1,4,5-Trisphosphate Receptors ; PPIF protein, mouse ; Cyclophilins (EC 5.2.1.-) ; Calcium (SY7Q814VUP)
Language	English
Publishing date	2015-12-10
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1694-9
ISSN	1432-0428 ; 0012-186X
ISSN (online)	1432-0428
ISSN	0012-186X
DOI	10.1007/s00125-015-3829-8
Database	MEDical Literature Analysis and Retrieval System OnLINE

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