Kurt Højlund

Odense University Hospital, Odense, South Denmark, Denmark

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Publications (107)652 Total impact

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    ABSTRACT: The aim of the study was to determine the steady-state pharmacokinetics of metformin in healthy volunteers with different numbers of reduced-function alleles in the organic cation transporter 1 gene (OCT1). The study was conducted as part of a randomized cross-over trial. Thirty-four healthy volunteers with known OCT1 genotypes (12 with two wild-type alleles, 13 with one and 9 with two reduced-function alleles) were included. In one of the study periods, they were titrated to steady-state with 1 g metformin twice daily. Neither AUC0-12, C max nor Clrenal were statistically significantly affected by the number of reduced-function alleles (0, 1 or 2) in OCT1: (AUC0-12: 0, 1, 2: 14, 13 and 14 h ng/L (P= 0.61)); (C max: 0, 1, 2: 2192, 1934 and 2233 ng/mL, (P = 0.26)) and (Clrenal: 0, 1, 2: 31, 28 and 30 L/h (P = 0.57)) CONCLUSIONS: In a cohort of healthy volunteers, we found no impact of different OCT1 genotypes on metformin steady-state pharmacokinetics.
    European Journal of Clinical Pharmacology 05/2015; 71(6). DOI:10.1007/s00228-015-1853-8 · 2.70 Impact Factor
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    ABSTRACT: We aimed to investigate metabolic risk factors, insulin sensitivity and insulin secretion in adolescent offspring of mothers with type 1 diabetes compared with offspring of non-diabetic mothers. During 1993-1999, pregnancies of women with type 1 diabetes in Denmark were prospectively reported to a central registry in the Danish Diabetes Association. Data included information on maternal demography, diabetes status and pregnancy outcome. We invited 746 eligible children from this cohort (index offspring) to a follow-up examination. Control offspring were identified through The Danish Central Office of Civil Registration and matched with respect to date of birth, sex and postal code. Anthropometric measurements and blood sampling for metabolic characterisation, including an oral glucose tolerance test, were performed. We examined 278 index offspring (mean age 16.7 years; range 13.0-19.8 years) and 303 control offspring (mean age 16.8 years; range 13.5-20.4 years). Index offspring had higher BMI SD score (0.44: 95% CI 0.21, 0.66) compared with controls, after adjustments for pubertal development and maternal pre-pregnancy BMI. Furthermore, index offspring had a higher prevalence of components included in metabolic syndrome and prediabetes (impaired fasting glucose and/or impaired glucose tolerance), with reduced insulin sensitivity and relative insulin secretion deficiency, compared with controls. Maternal HbA1c levels in pregnancy were not directly associated with offspring metabolic outcomes. Adolescent offspring of mothers with type 1 diabetes had a less favourable metabolic profile and higher frequency of prediabetes than the background population. Significant associations between these outcomes and maternal HbA1c levels in pregnancy could not be demonstrated. ClinicalTrials.gov NCT01559181.
    Diabetologia 04/2015; DOI:10.1007/s00125-015-3589-5 · 6.88 Impact Factor
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    ABSTRACT: Insulin and exercise stimulate skeletal muscle glycogen synthase (GS) activity by dephosphorylation and changes in kinetic properties. The aim of this study was to investigate the effects of insulin, exercise and post-exercise insulin stimulation on GS phosphorylation, activity and substrate affinity in obesity and type 2 diabetes. Obese men with type 2 diabetes (n = 13) and weight-matched controls (n = 14) underwent euglycaemic-hyperinsulinaemic clamps in the rested state and 3 h after 60 min of cycling (70% maximal pulmonary oxygen uptake [[Formula: see text]]). Biopsies from vastus lateralis muscle were obtained before and after clamps, and before and immediately after exercise. Insulin-stimulated glucose uptake was lower in diabetic patients vs obese controls with or without prior exercise. Post exercise, glucose partitioning shifted away from oxidation and towards storage in both groups. Insulin and, more potently, exercise increased GS activity (fractional velocity [FV]) and substrate affinity in both groups. Both stimuli caused dephosphorylation of GS at sites 3a + 3b, with exercise additionally decreasing phosphorylation at sites 2 + 2a. In both groups, changes in GS activity, substrate affinity and dephosphorylation at sites 3a + 3b by exercise were sustained 3 h post exercise and further enhanced by insulin. Post exercise, reduced GS activity and substrate affinity as well as increased phosphorylation at sites 2 + 2a were found in diabetic patients vs obese controls. Exercise-induced activation of muscle GS in obesity and type 2 diabetes involves dephosphorylation of GS at sites 3a + 3b and 2 + 2a and enhanced substrate affinity, which is likely to facilitate glucose partitioning towards storage. Lower GS activity and increased phosphorylation at sites 2 + 2a in type 2 diabetes in the recovery period imply an impaired response to exercise.
    Diabetologia 04/2015; DOI:10.1007/s00125-015-3582-z · 6.88 Impact Factor
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    Atherosclerosis 03/2015; 239(1):288. DOI:10.1016/j.atherosclerosis.2015.01.019 · 3.97 Impact Factor
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    Diabetes Care 02/2015; 38(2):e31. DOI:10.2337/dc14-2671 · 8.57 Impact Factor
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    ABSTRACT: We aimed to identify microRNAs (miRNAs) associated with type 2 diabetes and risk of developing the disease in skeletal muscle biopsies from phenotypically well-characterised twins. We measured muscle miRNA levels in monozygotic (MZ) twins discordant for type 2 diabetes using arrays. Further investigations of selected miRNAs included target prediction, pathway analysis, silencing in cells and association analyses in a separate cohort of 164 non-diabetic MZ and dizygotic twins. The effects of elevated glucose and insulin levels on miRNA expression were examined, and the effect of low birthweight (LBW) was studied in rats. We identified 20 miRNAs that were downregulated in MZ twins with diabetes compared with their non-diabetic co-twins. Differences for members of the miR-15 family (miR-15b and miR-16) were the most statistically significant, and these miRNAs were predicted to influence insulin signalling. Indeed, miR-15b and miR-16 levels were associated with levels of key insulin signalling proteins, miR-15b was associated with the insulin receptor in non-diabetic twins and knockdown of miR-15b/miR-16 in myocytes changed the levels of insulin signalling proteins. LBW in twins and undernutrition during pregnancy in rats were, in contrast to overt type 2 diabetes, associated with increased expression of miR-15b and/or miR-16. Elevated glucose and insulin suppressed miR-16 expression in vitro. Type 2 diabetes is associated with non-genetic downregulation of several miRNAs in skeletal muscle including miR-15b and miR-16, potentially targeting insulin signalling. The paradoxical findings in twins with overt diabetes and twins at increased risk of the disease underscore the complexity of the regulation of muscle insulin signalling in glucose homeostasis.
    Diabetologia 11/2014; 58(2). DOI:10.1007/s00125-014-3434-2 · 6.88 Impact Factor
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    ABSTRACT: Retraction of DiabetologiaDOI 10.1007/s00125-011-2276-4Abstract 59, presented at the 47th Annual Meeting of the EASD in 2011, has been retracted at the request of the Dean of Sahlgrenska Academy at the University of Gothenburg, Professor Larkö. The University has investigated this case and The Committee on Academic Misconduct finds that Pontus Boström is guilty of misdemeanour with reference to the points (1) conscious fabrication, corruption or suppression of basic material, and (2) conscious preparation and presentation of falsified results, and therefore finds reason to believe that scientific misconduct has occurred. The primary finding reported in the abstract—reduced protein levels of syntaxin-5 in diabetic muscle—could not be reproduced.
    Diabetologia 11/2014; DOI:10.1007/s00125-014-3431-5 · 6.88 Impact Factor
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    ABSTRACT: AimsTo investigate whether the presence of glutamic acid decarboxylase (GAD) autoantibodies post-partum in women with prior gestational diabetes mellitus was associated with changes in metabolic characteristics, including β–cell function and insulin sensitivity.Methods During 1997–2010, 407 women with gestational diabetes mellitus were offered a 3–month post-partum follow-up including anthropometrics, serum lipid profile, HbA1c and GAD autoantibodies, as well as a 2–h oral glucose tolerance test (OGTT) with blood glucose, serum insulin and C–peptide at 0, 30 and 120 min. Indices of insulin sensitivity and insulin secretion were estimated to assess insulin secretion adjusted for insulin sensitivity, disposition index (DI).ResultsTwenty-two (5.4%) women were positive for GAD autoantibodies (GAD+ve) and the remainder (94.6%) were negative for GAD autoantibodies (GAD–ve). The two groups had similar age and prevalence of diabetes mellitus. Women who were GAD+ve had significantly higher 2–h OGTT glucose concentrations during their index-pregnancy (10.5 vs. 9.8 mmol/l, P = 0.001), higher fasting glucose (5.2 vs. 5.0 mmol/l, P = 0.02) and higher 2–h glucose (7.8 vs. 7.1 mmol/l, P = 0.05) post-partum. Fasting levels of C–peptide and insulin were lower in GAD+ve women compared with GAD–ve women (520 vs. 761 pmol/l, P = 0.02 and 33 vs. 53 pmol/l, P = 0.05) Indices of insulin sensitivity were similar in GAD+ve and GAD–ve women, whereas all estimates of DI were significantly reduced in GAD+ve women.ConclusionGAD+ve women had higher glucose levels and impaired insulin secretion adjusted for insulin sensitivity (DI) compared with GAD–ve women. The combination of OGTT and GAD autoantibodies post-partum identify women with impaired β–cell function. These women should be followed with special focus on development of Type 1 diabetes.This article is protected by copyright. All rights reserved.
    Diabetic Medicine 10/2014; 32(2). DOI:10.1111/dme.12615 · 3.06 Impact Factor
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    ABSTRACT: Skeletal muscle is a heterogeneous tissue composed of different fiber types. Studies suggest that insulin-mediated glucose metabolism is different between muscle fiber types. We hypothesized that differences are due to fiber-type specific expression/regulation of insulin signaling elements and/or metabolic enzymes. Pools of type I and II fibers were prepared from biopsies of the vastus lateralis muscles from lean, obese and type 2 diabetic subjects before and after a hyperinsulinemic-euglycemic clamp. Type I fibers compared to type II fibers have higher protein levels of the insulin receptor, GLUT4, hexokinase II, glycogen synthase (GS), pyruvate dehydrogenase (PDH-E1α) and a lower protein content of Akt2, TBC1D4 and TBC1D1. In type I fibers compared to type II fibers, the phosphorylation-response to insulin was similar (TBC1D4, TBC1D1 and GS) or decreased (Akt and PDH-E1α). Phosphorylation-responses to insulin adjusted for protein level were not different between fiber types. Independently of fiber type, insulin signaling was similar (TBC1D1, GS and PDH-E1α) or decreased (Akt and TBC1D4) in muscle from patients with type 2 diabetes compared to lean and obese subjects. We conclude that human type I muscle fibers compared to type II fibers have a higher glucose handling capacity but a similar sensitivity for phosphor-regulation by insulin.
    Diabetes 09/2014; 64(2). DOI:10.2337/db14-0590 · 8.47 Impact Factor
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    ABSTRACT: AimsOur object was to investigate the steady-state pharmacokinetic and pharmacodynamic interaction between the antidepressive herbal medicine St. John's wort (SJW) and the antidiabetic drug metformin.Methods We performed an open cross-over study in 20 healthy male subjects who received 1 g of metformin twice daily for 1 week with and without 21 days of preceding and concomitant treatment with SJW. The pharmacokinetics of metformin was determined, and a 2-hour oral glucose tolerance test was performed.ResultsSJW decreased the renal clearance of metformin but did not affect any other metformin pharmacokinetic parameters. The addition of SJW decreased the area under the glucose concentration-time curve (702 mmol/L/h (95% confidence interval (643; 761)) vs. 629 mmol/L/h (95% confidence interval (568; 690)), p = 0.003), and this effect was caused by a statistically significantly higher acute insulin response.ConclusionsSJW improves glucose tolerance by enhancing insulin secretion independently of insulin sensitivity in healthy male subjects taking metformin.
    British Journal of Clinical Pharmacology 09/2014; 79(2). DOI:10.1111/bcp.12510 · 3.69 Impact Factor
  • Diabetologie und Stoffwechsel 05/2014; 9(S 01). DOI:10.1055/s-0034-1374898 · 0.31 Impact Factor
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    ABSTRACT: Recent studies indicate that serum testosterone in aging men is associated with insulin sensitivity and expression of oxidative phosphorylation (OxPhos) genes, and that testosterone treatment increases lipid oxidation. Here, we investigated the effect of testosterone therapy on regulators of mitochondrial biogenesis and markers of OxPhos and lipid metabolism in skeletal muscle of aging men with subnormal bioavailable testosterone levels. Skeletal muscle biopsies were obtained before and after treatment with either testosterone gel (n=12) or placebo (n=13) for 6 months. Insulin sensitivity and substrate oxidation were assessed by euglycemic-hyperinsulinemic clamp and indirect calorimetry. Muscle mRNA levels and protein abundance and phosphorylation of enzymes involved in mitochondrial biogenesis, OxPhos and lipid metabolism were examined by quantitative real-time PCR and western blotting. Despite an increase in lipid oxidation (P<0.05), testosterone therapy had no effect on insulin sensitivity or mRNA levels of genes involved in mitochondrial biogenesis (PPARGC1A, PRKAA2 and PRKAG3), OxPhos (NDUFS1, ETFA, SDHA, UQCRC1, and COX5B,) or lipid metabolism (ACADVL, CD36, CPT1B, HADH, and PDK4). Consistently, protein abundance of OxPhos subunits encoded by both nuclear (SDHA, UQCRC1) and mitochondrial DNA (ND6), and protein abundance and phosphorylation of AMP-activated protein kinase and p38 MAPK were unaffected by testosterone therapy. The beneficial effect of testosterone treatment on lipid oxidation is not explained by increased abundance or phosphorylation-dependent activity of enzymes known to regulate mitochondrial biogenesis or markers of OxPhos and lipid metabolism in skeletal muscle of aging men with subnormal bioavailable testosterone levels.
    European Journal of Endocrinology 04/2014; DOI:10.1530/EJE-14-0006 · 3.69 Impact Factor
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    ABSTRACT: There is increasing evidence that multiple proteins involved in key regulatory processes in mitochondria are phosphorylated in mammalian tissues. Insulin regulates glucose metabolism by phosphorylation-dependent signaling, and has been shown to stimulate ATP synthesis in human skeletal muscle. Here, we investigated the effect of insulin on the phosphorylation of mitochondrial proteins in human skeletal muscle in vivo. Using a combination of TiO2 phosphopeptide-enrichment, HILIC fractionation and LC-MS/MS, we compared the phosphoproteomes of isolated mitochondria from skeletal muscle samples obtained from healthy individuals before and after four hours of insulin infusion. In total, we identified 207 phosphorylation sites in 95 mitochondrial proteins. Of these phosphorylation sites, 45% were identified in both basal and insulin-stimulated samples. Insulin caused a 2-fold increase in the number of different mitochondrial phosphopeptides (87±7 vs. 40±7, p=0.015) and phosphoproteins (46±2 vs. 26±3, p=0.005) identified in each mitochondrial preparation. Almost half of the mitochondrial phosphorylation sites (n=94) were exclusively identified in the insulin-stimulated state and included the majority of novel sites. Phosphorylation sites detected more often or exclusively in insulin-stimulated samples include multiple sites in mitochondrial proteins involved in oxidative phosphorylation, tricarboxylic acid cycle, fatty acid metabolism, as well as several components of the newly defined mitochondrial inner membrane organizing system (MINOS). In conclusion, the present study demonstrates that insulin increases the phosphorylation of several mitochondrial proteins in human skeletal muscle in vivo, and provides a first step in the understanding of how insulin potentially regulates mitochondrial processes by phosphorylation-dependent mechanisms.
    Journal of Proteome Research 03/2014; 13(5). DOI:10.1021/pr401163t · 5.00 Impact Factor
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    ABSTRACT: OBJECTIVE Accumulating evidence suggests an association between insulin sensitivity and albuminuria, which, even in the normal range, is a risk factor for cardiovascular diseases. We evaluated whether insulin sensitivity is associated with albuminuria in healthy subjects.RESEARCH DESIGN AND METHODS We investigated 1,415 healthy, nondiabetic participants (mean age 43.9 ± 8.3 years; 54.3% women) from the RISC (Relationship between Insulin Sensitivity and Cardiovascular Disease) study, of whom 852 participated in a follow-up examination after 3 years. At baseline, insulin sensitivity was assessed by hyperinsulinemic-euglycemic clamps, expressed as the M/I value. Oral glucose tolerance test-based insulin sensitivity (OGIS), homeostasis model assessment of insulin resistance (HOMA-IR), and urinary albumin-to-creatinine ratio (UACR) were determined at baseline and follow-up.RESULTSMicroalbuminuria (UACR ≥30 mg/g) was present in fewer than 2% at either study visit. After multivariate adjustments, there was no cross-sectional association between UACR and any measure of insulin sensitivity. Neither OGIS nor HOMA-IR were significantly associated with follow-up UACR, but in a multivariate regression analysis, baseline M/I emerged as an independent predictor of UACR at follow-up (β-coefficient -0.14; P = 0.001).CONCLUSIONS In healthy middle-aged adults, reduced insulin sensitivity, assessed by hyperinsulinemic-euglycemic clamp, is continuously associated with a greater risk of increasing albuminuria. This finding suggests that reduced insulin sensitivity is either simply related to or might causally contribute to the initial pathogenesis of albuminuria.
    Diabetes care 03/2014; 37(6). DOI:10.2337/dc13-2573 · 8.57 Impact Factor
  • Experimental and Clinical Endocrinology & Diabetes 03/2014; 122(03). DOI:10.1055/s-0034-1371980 · 1.76 Impact Factor
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    ABSTRACT: Insulin receptor substrate-1 (IRS1) is a key mediator of insulin signal transduction. Perturbations involving IRS1 complexes may lead to the development of insulin resistance and type 2 diabetes. Surprisingly, little is known about the proteins that interact with IRS1 in humans in health and disease conditions. We used a proteomic approach to assess IRS1 interaction partners in skeletal muscle from lean healthy controls (LC), obese insulin resistant non-diabetic controls (OC), and type 2 diabetic participants (T2D) before and after insulin infusion. We identified 113 novel endogenous IRS1 interaction partners, which represents the largest IRS1 interactome in humans and provides new targets for studies of IRS1 complexes in various diseases. Furthermore, we generated the 1st global picture of IRS1 interaction partners in LC, and how they differ in OC and T2D. Interestingly, dozens of proteins in OC and/or T2D exhibited increased associations with IRS1 compared to LC under the basal and/or insulin-stimulated conditions, revealing multiple new dysfunctional IRS1 pathways in OC and T2D. This novel abnormality, increased interaction of multiple proteins with IRS1 in obesity and type 2 diabetes in humans, provides new insights into the molecular mechanism of insulin resistance, and identifies new targets for type 2 diabetes drug development.
    Diabetes 02/2014; 63(6). DOI:10.2337/db13-1872 · 8.47 Impact Factor
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    ABSTRACT: Insulin resistance in obesity and type 2 diabetes is related to abnormalities in mitochondrial oxidative phosphorylation (OxPhos) in skeletal muscle. We tested the hypothesis that mitochondrial oxidative metabolism is impaired in muscle of patients with inherited insulin resistance and defective insulin signalling. Skeletal muscle biopsies obtained from carriers (n = 6) of a mutation in the tyrosine kinase domain of the insulin receptor gene (INSR) and matched healthy controls (n = 15) were used for discovery-mode microarray-based transcriptional profiling combined with biological pathway analysis. Findings were validated by quantitative real-time PCR, immunoblotting and activity assays. In INSR mutation carriers, insulin resistance was associated with a coordinated downregulation of OxPhos genes in skeletal muscle. This was related to a 46% decrease in mRNA levels (p = 0.036) of peroxisome proliferator-activated receptor-γ coactivator-1α (PGC-1α), and 25-50% lower protein content of OxPhos subunits encoded by mitochondrial (ND6, p = 0.042) and nuclear DNA (UQCRC1, p = 0.001; SDHA, p = 0.067; COX5A, p = 0.017 and ATP5B, p = 0.005), as well as reduced citrate synthase activity (p = 0.025). Moreover, mutation carriers showed a marked reduction in type 1 muscle fibres (35% vs 62%, p = 0.0005) and increased type 2a fibres (53% vs 32%; p = 0.002) compared with controls. There were no differences in protein content and phosphorylation of 5' AMP-activated protein kinase, p38 mitogen-activated protein kinase, Erk1 and Erk2. These data indicate that inherited insulin resistance coincides with reduced mitochondrial oxidative capacity in a PGC-1α- and muscle fibre type-related manner. Whether this co-existence is directly or indirectly related to insulin resistance remains to be elucidated.
    Diabetologia 02/2014; DOI:10.1007/s00125-014-3187-y · 6.88 Impact Factor
  • Diabetes Care 12/2013; 36(12):4125-31. · 8.57 Impact Factor
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    ABSTRACT: Type 2 diabetes, obesity and insulin resistance are characterized by hypertriglyceridemia and ectopic accumulation of lipids in liver and skeletal muscle. AGPAT6 encodes a novel glycerol-3 phosphate acyltransferase, GPAT4, which catalyzes the first step in the de novo triglyceride synthesis. AGPAT6-deficient mice show lower weight and resistance to diet- and genetically induced obesity. Here, we examined whether common or low-frequency variants in AGPAT6 associate with type 2 diabetes or related metabolic traits in a Danish population. Eleven variants selected by a candidate gene approach capturing the common and low-frequency variation of AGPAT6 were genotyped in 12,068 Danes from four study populations of middle-aged individuals. The case--control study involved 4,638 type 2 diabetic and 5,934 glucose-tolerant individuals, while studies of quantitative metabolic traits were performed in 5,645 non-diabetic participants of the Inter99 Study. None of the eleven AGPAT6 variants were robustly associated with type 2 diabetes in the Danish case--control study. Moreover, none of the AGPAT6 variants showed association with measures of obesity (waist circumference and BMI), serum lipid concentrations, fasting or 2-h post-glucose load levels of plasma glucose and serum insulin, or estimated indices of insulin secretion or insulin sensitivity. Common and low-frequency variants in AGPAT6 do not significantly associate with type 2 diabetes susceptibility, or influence related phenotypic traits such as obesity, dyslipidemia or indices of insulin sensitivity or insulin secretion in the population studied.
    BMC Medical Genetics 10/2013; 14(1):113. DOI:10.1186/1471-2350-14-113 · 2.45 Impact Factor
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    ABSTRACT: OBJECTIVE We evaluated whether the association of insulin sensitivity with HDL cholesterol (HDL) and triglycerides is influenced by major plasma apolipoproteins, as suggested by recent experimental evidence.RESEARCH DESIGN AND METHODS Cross-sectional analysis of the RISC Study, a multicenter European clinical investigation in 1,017 healthy volunteers balanced in sex (women 54%) and age strata (range 30-60 years). Insulin sensitivity (M/I in µmol ⋅ min(-1) ⋅ kgFFM(-1) ⋅ nM(-1)) was measured by the clamp technique and apolipoproteins (ApoB, -C3, -A1, and -E) by Multiplex Technology.RESULTSThe center-, sex-, and age-adjusted standardized regression coefficients (STDβ) with M/I were similar for HDL and triglycerides (+19.9 ± 1.9 vs. -20.0 ± 2.0, P < 0.0001). Further adjustment for triglycerides (or HDL), BMI, and adiponectin (or nonesterified fatty acid) attenuated the strength of the association of M/I with both HDL (STDβ +6.4 ± 2.3, P < 0.01) and triglycerides (-9.5 ± 2.1, P < 0.001). Neither ApoA1 nor ApoE and ApoB showed any association with M/I independent from plasma HDL cholesterol and triglycerides. ApoC3, in contrast, in both men and women, was positively associated with M/I independently of plasma lipids. A relative enrichment of plasma lipids with ApoC3 is associated with lower body fat percentage and lower plasma alanine amino transferase.CONCLUSIONS Our results suggest that HDL cholesterol modulates insulin sensitivity through a mechanism that is partially mediated by BMI and adiponectin but not by ApoA1. Similarly, the influence of triglycerides on insulin sensitivity is in part mediated by BMI and is unrelated to ApoE or ApoB, but it is significantly modulated by ApoC3, which appears to protect from the negative effect of plasma lipids.
    Diabetes care 10/2013; 36(12). DOI:10.2337/dc13-0682 · 8.57 Impact Factor

Publication Stats

3k Citations
652.00 Total Impact Points


  • 2001–2015
    • Odense University Hospital
      • Department of Endocrinology - M
      Odense, South Denmark, Denmark
  • 2003–2014
    • University of Southern Denmark
      • Institute of Clinical Research
      Odense, South Denmark, Denmark
    • Novo Nordisk
      København, Capital Region, Denmark
  • 2009–2010
    • Arizona State University
      • Center for Metabolic Biology
      Phoenix, Arizona, United States
  • 2008
    • Aarhus University Hospital
      • Department of Clinical Biochemistry
      Aarhus, Central Jutland, Denmark
  • 2004
    • Steno Diabetes Center
      Gjentofte, Capital Region, Denmark