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Article: Validation of a short turnaround time automated method for the 24/7 determination of plasma d-lactate on Roche Cobas c502.

Turban, Adrien / Gaubert, Sophie / Luque-Paz, David / René, Céline / Collet, Nicolas / Pawlowski, Maxime / Bendavid, Claude / Lefèvre, Charles R

Practical laboratory medicine

2023 Volume 36, Page(s) e00317

Language	English
Publishing date	2023-06-19
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2834973-8
ISSN	2352-5517
ISSN	2352-5517
DOI	10.1016/j.plabm.2023.e00317
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Article ; Online: MG53 is not a critical regulator of insulin signaling pathway in skeletal muscle.

Philouze, Clothilde / Turban, Sophie / Cremers, Beatrice / Caliez, Audrey / Lamarche, Gwladys / Bernard, Catherine / Provost, Nicolas / Delerive, Philippe

PloS one

2021 Volume 16, Issue 2, Page(s) e0245179

Abstract: In type 2 diabetes (T2D), both muscle and liver are severely resistant to insulin action. Muscle insulin resistance accounts for more than 80% of the impairment in total body glucose disposal in T2D patients and is often characterized by an impaired ... ...

Abstract	In type 2 diabetes (T2D), both muscle and liver are severely resistant to insulin action. Muscle insulin resistance accounts for more than 80% of the impairment in total body glucose disposal in T2D patients and is often characterized by an impaired insulin signaling. Mitsugumin 53 (MG53), a muscle-specific TRIM family protein initially identified as a key regulator of cell membrane repair machinery has been suggested to be a critical regulator of muscle insulin signaling pathway by acting as ubiquitin E3 ligase targeting both the insulin receptor and insulin receptor substrate 1 (IRS1). Here, we show using in vitro and in vivo approaches that MG53 is not a critical regulator of insulin signaling and glucose homeostasis. First, MG53 expression is not consistently regulated in skeletal muscle from various preclinical models of insulin resistance. Second, MG53 gene knock-down in muscle cells does not lead to impaired insulin response as measured by Akt phosphorylation on Serine 473 and glucose uptake. Third, recombinant human MG53 does not alter insulin response in both differentiated C2C12 and human skeletal muscle cells. Fourth, ectopic expression of MG53 in HEK293 cells lacking endogenous MG53 expression fails to alter insulin response as measured by Akt phosphorylation. Finally, both male and female mg53 -/- mice were not resistant to high fat induced obesity and glucose intolerance compared to wild-type mice. Taken together, these results strongly suggest that MG53 is not a critical regulator of insulin signaling pathway in skeletal muscle.
MeSH term(s)	Animals ; Antigens, CD/metabolism ; Carrier Proteins/metabolism ; Female ; HEK293 Cells ; Humans ; Insulin/metabolism ; Insulin Receptor Substrate Proteins/metabolism ; Insulin Resistance/physiology ; Male ; Membrane Proteins/genetics ; Membrane Proteins/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Muscle Fibers, Skeletal/metabolism ; Muscle, Skeletal/metabolism ; Receptor, Insulin/metabolism ; Signal Transduction ; Tripartite Motif Proteins/genetics ; Tripartite Motif Proteins/metabolism ; Ubiquitin-Protein Ligases/metabolism ; Ubiquitination
Chemical Substances	Antigens, CD ; Carrier Proteins ; Insulin ; Insulin Receptor Substrate Proteins ; MG53 protein, mouse ; Membrane Proteins ; TRIM72 protein, human ; Tripartite Motif Proteins ; Ubiquitin-Protein Ligases (EC 2.3.2.27) ; INSR protein, human (EC 2.7.10.1) ; Receptor, Insulin (EC 2.7.10.1)
Language	English
Publishing date	2021-02-10
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.0245179
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Article ; Online: MG53 is not a critical regulator of insulin signaling pathway in skeletal muscle.

Clothilde Philouze / Sophie Turban / Beatrice Cremers / Audrey Caliez / Gwladys Lamarche / Catherine Bernard / Nicolas Provost / Philippe Delerive

PLoS ONE, Vol 16, Iss 2, p e

2021 Volume 0245179

Abstract	In type 2 diabetes (T2D), both muscle and liver are severely resistant to insulin action. Muscle insulin resistance accounts for more than 80% of the impairment in total body glucose disposal in T2D patients and is often characterized by an impaired insulin signaling. Mitsugumin 53 (MG53), a muscle-specific TRIM family protein initially identified as a key regulator of cell membrane repair machinery has been suggested to be a critical regulator of muscle insulin signaling pathway by acting as ubiquitin E3 ligase targeting both the insulin receptor and insulin receptor substrate 1 (IRS1). Here, we show using in vitro and in vivo approaches that MG53 is not a critical regulator of insulin signaling and glucose homeostasis. First, MG53 expression is not consistently regulated in skeletal muscle from various preclinical models of insulin resistance. Second, MG53 gene knock-down in muscle cells does not lead to impaired insulin response as measured by Akt phosphorylation on Serine 473 and glucose uptake. Third, recombinant human MG53 does not alter insulin response in both differentiated C2C12 and human skeletal muscle cells. Fourth, ectopic expression of MG53 in HEK293 cells lacking endogenous MG53 expression fails to alter insulin response as measured by Akt phosphorylation. Finally, both male and female mg53 -/- mice were not resistant to high fat induced obesity and glucose intolerance compared to wild-type mice. Taken together, these results strongly suggest that MG53 is not a critical regulator of insulin signaling pathway in skeletal muscle.
Keywords	Medicine ; R ; Science ; Q
Subject code	571
Language	English
Publishing date	2021-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
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Article ; Online: Protein kinase C isoforms: mediators of reactive lipid metabolites in the development of insulin resistance.

Turban, Sophie / Hajduch, Eric

FEBS letters

2011 Volume 585, Issue 2, Page(s) 269–274

Abstract: The role of protein kinase C (PKCs) isoforms in the regulation of glucose metabolism by insulin is complex, partly due to the large PKC family consisting of three sub-groups: conventional, novel and atypical. Activation of some conventional and novel ... ...

Abstract	The role of protein kinase C (PKCs) isoforms in the regulation of glucose metabolism by insulin is complex, partly due to the large PKC family consisting of three sub-groups: conventional, novel and atypical. Activation of some conventional and novel PKCs in response to increased levels of diacylglycerol (DAG) have been shown to counteract insulin signalling. However, roles of atypical PKCs (aPKCs) remain poorly understood. aPKCs act as molecular switches by promoting or suppressing signalling pathways, in response to insulin or ceramides respectively. Understanding how DAG- and ceramide-activated PKCs impair insulin signalling would help to develop treatments to fight insulin resistance.
MeSH term(s)	Ceramides ; Diglycerides ; Humans ; Insulin Resistance ; Lipid Metabolism ; Protein Isoforms ; Protein Kinase C/metabolism
Chemical Substances	1,2-diacylglycerol ; Ceramides ; Diglycerides ; Protein Isoforms ; Protein Kinase C (EC 2.7.11.13)
Language	English
Publishing date	2011-01-21
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1016/j.febslet.2010.12.022
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Article: Protein kinase C isoforms: Mediators of reactive lipid metabolites in the development of insulin resistance

Turban, Sophie / Hajduch, Eric

FEBS letters. 2011 Jan. 21, v. 585, no. 2

2011

Abstract	The role of protein kinase C (PKCs) isoforms in the regulation of glucose metabolism by insulin is complex, partly due to the large PKC family consisting of three sub-groups: conventional, novel and atypical. Activation of some conventional and novel PKCs in response to increased levels of diacylglycerol (DAG) have been shown to counteract insulin signalling. However, roles of atypical PKCs (aPKCs) remain poorly understood. aPKCs act as molecular switches by promoting or suppressing signalling pathways, in response to insulin or ceramides respectively. Understanding how DAG- and ceramide-activated PKCs impair insulin signalling would help to develop treatments to fight insulin resistance.
Keywords	ceramides ; glucose ; insulin ; insulin resistance ; metabolism ; metabolites ; protein isoforms ; protein kinase C ; signal transduction
Language	English
Dates of publication	2011-0121
Size	p. 269-274.
Publishing place	Elsevier B.V.
Document type	Article
ZDB-ID	212746-5
ISSN	1873-3468 ; 0014-5793
ISSN (online)	1873-3468
ISSN	0014-5793
DOI	10.1016/j.febslet.2010.12.022
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Article ; Online: PHOSPHO1 is a skeletal regulator of insulin resistance and obesity.

BMC biology

2020 Volume 18, Issue 1, Page(s) 149

Abstract: Background: The classical functions of the skeleton encompass locomotion, protection and mineral homeostasis. However, cell-specific gene deletions in the mouse and human genetic studies have identified the skeleton as a key endocrine regulator of ... ...

Abstract	Background: The classical functions of the skeleton encompass locomotion, protection and mineral homeostasis. However, cell-specific gene deletions in the mouse and human genetic studies have identified the skeleton as a key endocrine regulator of metabolism. The bone-specific phosphatase, Phosphatase, Orphan 1 (PHOSPHO1), which is indispensable for bone mineralisation, has been recently implicated in the regulation of energy metabolism in humans, but its role in systemic metabolism remains unclear. Here, we probe the mechanism underlying metabolic regulation by analysing Phospho1 mutant mice. Results: Phospho1 Conclusion: We show that mice lacking the bone mineralisation enzyme PHOSPHO1 exhibit improved basal glucose homeostasis and resist high-fat-diet-induced weight gain and diabetes. This study identifies PHOSPHO1 as a potential bone-derived therapeutic target for the treatment of obesity and diabetes.
Language	English
Publishing date	2020-10-22
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ISSN	1741-7007
ISSN (online)	1741-7007
DOI	10.1186/s12915-020-00880-7
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Article ; Online: PHOSPHO1 is a skeletal regulator of insulin resistance and obesity

BMC Biology, Vol 18, Iss 1, Pp 1-

2020 Volume 20

Abstract: Abstract Background The classical functions of the skeleton encompass locomotion, protection and mineral homeostasis. However, cell-specific gene deletions in the mouse and human genetic studies have identified the skeleton as a key endocrine regulator ... ...

Abstract	Abstract Background The classical functions of the skeleton encompass locomotion, protection and mineral homeostasis. However, cell-specific gene deletions in the mouse and human genetic studies have identified the skeleton as a key endocrine regulator of metabolism. The bone-specific phosphatase, Phosphatase, Orphan 1 (PHOSPHO1), which is indispensable for bone mineralisation, has been recently implicated in the regulation of energy metabolism in humans, but its role in systemic metabolism remains unclear. Here, we probe the mechanism underlying metabolic regulation by analysing Phospho1 mutant mice. Results Phospho1 −/− mice exhibited improved basal glucose homeostasis and resisted high-fat-diet-induced weight gain and diabetes. The metabolic protection in Phospho1 −/− mice was manifested in the absence of altered levels of osteocalcin. Osteoblasts isolated from Phospho1 −/− mice were enriched for genes associated with energy metabolism and diabetes; Phospho1 both directly and indirectly interacted with genes associated with glucose transport and insulin receptor signalling. Canonical thermogenesis via brown adipose tissue did not underlie the metabolic protection observed in adult Phospho1 −/− mice. However, the decreased serum choline levels in Phospho1 −/− mice were normalised by feeding a 2% choline rich diet resulting in a normalisation in insulin sensitivity and fat mass. Conclusion We show that mice lacking the bone mineralisation enzyme PHOSPHO1 exhibit improved basal glucose homeostasis and resist high-fat-diet-induced weight gain and diabetes. This study identifies PHOSPHO1 as a potential bone-derived therapeutic target for the treatment of obesity and diabetes.
Keywords	PHOSPHO1 ; Osteocalcin ; Choline ; Bone ; Energy metabolism ; Insulin ; Biology (General) ; QH301-705.5
Subject code	616
Language	English
Publishing date	2020-10-01T00:00:00Z
Publisher	BMC
Document type	Article ; Online
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Article: β-Cell-Specific Glucocorticoid Reactivation Attenuates Inflammatory β-Cell Destruction.

Liu, Xiaoxia / Turban, Sophie / Carter, Roderick N / Ahmad, Shakil / Ramage, Lynne / Webster, Scott P / Walker, Brian R / Seckl, Jonathan R / Morton, Nicholas M

Frontiers in endocrinology

2014 Volume 5, Page(s) 165

Abstract: Progression and severity of type 1 diabetes is dependent upon inflammatory induction of nitric oxide production and consequent pancreatic β-cell damage. Glucocorticoids (GCs) are highly effective anti-inflammatory agents but have been precluded in type 1 ...

Abstract	Progression and severity of type 1 diabetes is dependent upon inflammatory induction of nitric oxide production and consequent pancreatic β-cell damage. Glucocorticoids (GCs) are highly effective anti-inflammatory agents but have been precluded in type 1 diabetes and in islet transplantation protocols because they exacerbated insulin resistance and suppressed β-cell insulin secretion at the high-doses employed clinically. In contrast, physiological-range elevation of GC action within β-cells ameliorated lipotoxic β-cell failure in transgenic mice overexpressing the intracellular enzyme 11β-hydroxysteroid dehydrogenase type 1 (MIP-HSD1(tg/+) mice). Here, we tested the hypothesis that elevated β-cell 11beta-HSD1 protects against the β-cell destruction elicited by streptozotocin (STZ), a toxin that dose-dependently mimics aspects of inflammatory and autoimmune β-cell destruction. MIP-HSD1(tg/+) mice exhibited an episodic protection from the severe hyperglycemia caused by a single high dose of STZ associated with higher and sustained β-cell survival, maintained β-cell replicative potential, higher plasma and islet insulin levels, reduced inflammatory macrophage infiltration and increased anti-inflammatory T regulatory cell content. MIP-HSD1(tg/+) mice also completely resisted mild hyperglycemia and insulitis induced by multiple low-dose STZ administration. In vitro, MIP-HSD1(tg/+) islets exhibited attenuated STZ-induced nitric oxide production, an effect reversed with a specific 11beta-HSD1 inhibitor. GC regeneration selectively within β-cells protects against inflammatory β-cell destruction, suggesting therapeutic targeting of 11beta-HSD1 may ameliorate processes that exacerbate type 1 diabetes and that hinder islet transplantation.
Language	English
Publishing date	2014-10-14
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2592084-4
ISSN	1664-2392
ISSN	1664-2392
DOI	10.3389/fendo.2014.00165
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Article ; Online: Pregnancy in obese mice protects selectively against visceral adiposity and is associated with increased adipocyte estrogen signalling.

Pedroni, Silvia M A / Turban, Sophie / Kipari, Tiina / Dunbar, Donald R / McInnes, Kerry / Saunders, Philippa T K / Morton, Nicholas M / Norman, Jane E

PloS one

2014 Volume 9, Issue 4, Page(s) e94680

Abstract: Maternal obesity is linked with increased adverse pregnancy outcomes for both mother and child. The metabolic impact of excessive fat within the context of pregnancy is not fully understood. We used a mouse model of high fat (HF) feeding to induce ... ...

Abstract	Maternal obesity is linked with increased adverse pregnancy outcomes for both mother and child. The metabolic impact of excessive fat within the context of pregnancy is not fully understood. We used a mouse model of high fat (HF) feeding to induce maternal obesity to identify adipose tissue-mediated mechanisms driving metabolic dysfunction in pregnant and non-pregnant obese mice. As expected, chronic HF-feeding for 12 weeks preceding pregnancy increased peripheral (subcutaneous) and visceral (mesenteric) fat mass. However, unexpectedly at late gestation (E18.5) HF-fed mice exhibited a remarkable normalization of visceral but not peripheral adiposity, with a 53% reduction in non-pregnant visceral fat mass expressed as a proportion of body weight (P<0.001). In contrast, in control animals, pregnancy had no effect on visceral fat mass proportion. Obesity exaggerated glucose intolerance at mid-pregnancy (E14.5). However by E18.5, there were no differences, in glucose tolerance between obese and control mice. Transcriptomic analysis of visceral fat from HF-fed dams at E18.5 revealed reduced expression of genes involved in de novo lipogenesis (diacylglycerol O-acyltransferase 2--Dgat2) and inflammation (chemokine C-C motif ligand 20--Ccl2) and upregulation of estrogen receptor α (ERα) compared to HF non pregnant. Attenuation of adipose inflammation was functionally confirmed by a 45% reduction of CD11b+CD11c+ adipose tissue macrophages (expressed as a proportion of all stromal vascular fraction cells) in HF pregnant compared to HF non pregnant animals (P<0.001). An ERα selective agonist suppressed both de novo lipogenesis and expression of lipogenic genes in adipocytes in vitro. These data show that, in a HF model of maternal obesity, late gestation is associated with amelioration of visceral fat hypertrophy, inflammation and glucose intolerance, and suggest that these effects are mediated in part by elevated visceral adipocyte ERα signaling.
MeSH term(s)	Adipocytes/cytology ; Adipocytes/metabolism ; Adiposity ; Animals ; Estrogens/metabolism ; Female ; Glucose/metabolism ; Glucose Tolerance Test ; Intra-Abdominal Fat/metabolism ; Macrophages/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Obese ; Mice, Transgenic ; Oligonucleotide Array Sequence Analysis ; Pregnancy ; Pregnancy, Animal ; Receptors, Estrogen/metabolism ; Signal Transduction ; Time Factors ; Transcriptome
Chemical Substances	Estrogens ; Receptors, Estrogen ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2014-04-14
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0094680
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Article ; Online: Characterising the inhibitory actions of ceramide upon insulin signaling in different skeletal muscle cell models: a mechanistic insight.

Mahfouz, Rana / Khoury, Rhéa / Blachnio-Zabielska, Agnieszka / Turban, Sophie / Loiseau, Nicolas / Lipina, Christopher / Stretton, Clare / Bourron, Olivier / Ferré, Pascal / Foufelle, Fabienne / Hundal, Harinder S / Hajduch, Eric

PloS one

2014 Volume 9, Issue 7, Page(s) e101865

Abstract: Ceramides are known to promote insulin resistance in a number of metabolically important tissues including skeletal muscle, the predominant site of insulin-stimulated glucose disposal. Depending on cell type, these lipid intermediates have been shown to ... ...

Abstract	Ceramides are known to promote insulin resistance in a number of metabolically important tissues including skeletal muscle, the predominant site of insulin-stimulated glucose disposal. Depending on cell type, these lipid intermediates have been shown to inhibit protein kinase B (PKB/Akt), a key mediator of the metabolic actions of insulin, via two distinct pathways: one involving the action of atypical protein kinase C (aPKC) isoforms, and the second dependent on protein phosphatase-2A (PP2A). The main aim of this study was to explore the mechanisms by which ceramide inhibits PKB/Akt in three different skeletal muscle-derived cell culture models; rat L6 myotubes, mouse C2C12 myotubes and primary human skeletal muscle cells. Our findings indicate that the mechanism by which ceramide acts to repress PKB/Akt is related to the myocellular abundance of caveolin-enriched domains (CEM) present at the plasma membrane. Here, we show that ceramide-enriched-CEMs are markedly more abundant in L6 myotubes compared to C2C12 myotubes, consistent with their previously reported role in coordinating aPKC-directed repression of PKB/Akt in L6 muscle cells. In contrast, a PP2A-dependent pathway predominantly mediates ceramide-induced inhibition of PKB/Akt in C2C12 myotubes. In addition, we demonstrate for the first time that ceramide engages an aPKC-dependent pathway to suppress insulin-induced PKB/Akt activation in palmitate-treated cultured human muscle cells as well as in muscle cells from diabetic patients. Collectively, this work identifies key mechanistic differences, which may be linked to variations in plasma membrane composition, underlying the insulin-desensitising effects of ceramide in different skeletal muscle cell models that are extensively used in signal transduction and metabolic studies.
MeSH term(s)	Animals ; Caveolins/genetics ; Caveolins/metabolism ; Ceramides/pharmacology ; Gene Expression Regulation ; Humans ; Insulin/metabolism ; Insulin/pharmacology ; Mice ; Muscle Fibers, Skeletal/cytology ; Muscle Fibers, Skeletal/drug effects ; Muscle Fibers, Skeletal/metabolism ; Muscle, Skeletal/cytology ; Muscle, Skeletal/drug effects ; Muscle, Skeletal/metabolism ; Primary Cell Culture ; Protein Kinase C/genetics ; Protein Kinase C/metabolism ; Protein Phosphatase 2/genetics ; Protein Phosphatase 2/metabolism ; Proto-Oncogene Proteins c-akt/genetics ; Proto-Oncogene Proteins c-akt/metabolism ; Rats ; Signal Transduction/drug effects
Chemical Substances	Caveolins ; Ceramides ; Insulin ; Proto-Oncogene Proteins c-akt (EC 2.7.11.1) ; Protein Kinase C (EC 2.7.11.13) ; Protein Phosphatase 2 (EC 3.1.3.16)
Language	English
Publishing date	2014-07-24
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0101865
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