Comparison of plasma pigment epithelium-derived factor (PEDF), retinol binding protein 4 (RBP-4), chitinase-3-like protein 1 (YKL-40) and brain-derived neurotrophic factor (BDNF) for the identification of insulin resistance

Toloza, Freddy J.K.; Pérez-Matos, Maria Camila; Ricardo-Silgado, Maria Laura; Morales-Álvarez, Martha Catalina; Mantilla-Rivas, Jose O; Pinzón-Cortés, Jairo A; Pérez-Mayorga, Maritza; Arévalo-García, M.L.; Tolosa-González, Giovanni; Mendivil, Carlos O.

doi:10.1016/j.jdiacomp.2017.06.002

Cited by 11 publications

(14 citation statements)

References 41 publications

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“…Besides, plasma CHI3L1 level was not associated with insulin resistance in a human study using hyperinsulinemic-euglycemic clamp. 45 A study by Park et al 46 conducted in Koreans showed higher CHI3L1 levels in diabetic patients compared to nondiabetic F I G U R E 8 Associations among plasma CHI3L1 levels, CHI3L1 genetic variants, and lymphocytic CHI31L mRNA expression. A, Plasma CHI3L1 levels of young NGT (n = 20) and old NGT (n = 20).…”

Section: Discussionmentioning

confidence: 99%

Effect of chitinase‐3‐like protein 1 on glucose metabolism: In vitro skeletal muscle and human genetic association study

et al. 2020

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We investigated the effect of chitinase‐3‐like protein 1 (CHI3L1) on glucose metabolism and its underlying mechanisms in skeletal muscle cells, and evaluated whether the observed effects are relevant in humans. CHI3L1 was associated with increased glucose uptake in skeletal muscles in an AMP‐activated protein kinase (AMPK)‐dependent manner, and with increased intracellular calcium levels via PAR2. The improvement in glucose metabolism observed in an intraperitoneal glucose tolerance test on male C57BL/6J mice supported this association. Inhibition of the CaMKK was associated with suppression of CHI3L1‐mediated glucose uptake. Additionally, CHI3L1 was found to influence glucose uptake through the PI3K/AKT pathway. Results suggested that CHI3L1 stimulated the phosphorylation of AS160 and p38 MAPK downstream of AMPK and AKT, and the resultant GLUT4 translocation. In primary myoblast cells, stimulation of AMPK and AKT was observed in response to CHI3L1, underscoring the biological relevance of CHI3L1. CHI3L1 levels were elevated in cells under conditions that mimic exercise in vitro and in exercised mice in vivo, indicating that CHI3L1 is secreted during muscle contraction. Finally, similar associations between CHI3L1 and metabolic parameters were observed in humans alongside genotype associations between CHI3L1 and diabetes at the population level. CHI3L1 may be a potential therapeutic target for the treatment of diabetes.

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Section: Discussionmentioning

confidence: 99%

Effect of chitinase‐3‐like protein 1 on glucose metabolism: In vitro skeletal muscle and human genetic association study

et al. 2020

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“…The study included 18 participants between 33 and 76 years old, selected from a project about new biomarkers of insulin resistance (34). Exclusion criteria were known diabetes mellitus or use of antidiabetic medications, other endocrine disorders, diseases of the exocrine pancreas, pregnancy or use of oral anticoagulants or lipid-lowering drugs.…”

Section: Study Design and Participantsmentioning

confidence: 99%

“…It is known that besides apoA-I (the natural cofactor of LCAT) (31), apoE is able to activate LCAT in vitro (32), while an increase in the apoC-III content of synthetic HDL exerts the opposite effect (33). ApoE is able to partially rescue LCAT activity In apoA-I knockout mice, albeit only in VLDL and LDL, not in HDL (34). Despite their major relevance in lipoprotein metabolism, the in uence of apoE and apoC-III over LCAT and CETP in humans is very poorly understood.…”

Section: Introductionmentioning

confidence: 99%

ApoE and apoC-III-defined HDL subtypes: A descriptive study of their lecithin cholesterol acyl transferase and cholesteryl ester transfer protein content and activity

Amaya-Montoya

Pinzón-Cortés

Silva-Bermúdez

et al. 2020

Preprint

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Background The functionality of high-density lipoproteins (HDL) is a better cardiovascular risk predictor than HDL concentrations. One of the key elements of HDL functionality is its apolipoprotein composition. Lecithin-cholesterol acyl transferase (LCAT) and cholesterol-ester transfer protein (CETP) are enzymes involved in HDL-mediated reverse cholesterol transport. This study assessed the concentration and activity of LCAT and CETP in HDL subspecies defined by their content of apolipoproteins E (apoE) and C-III (apoC-III) in humans. Methods Eighteen adults (ten women and eight men, mean age 55.6, BMI 26.9 Kg/m 2 , HbA1c 5.4%) were studied. HDL from each participant were isolated and divided into four subspecies containing respectively: No apoE and no apoC-III (E-C-), apoE but not apoC-III (E+C-), apoC-III but no apoE (E-C+) and both apoE and apoC-III (E+C+). The concentration and enzymatic activity of LCAT and CETP were measured within each HDL subspecies using immunoenzymatic and fluorometric methods. Additionally, the size distribution of HDL in each apolipoprotein-defined fraction was determined using non-denaturing electrophoresis and anti-apoA-I western blotting. Results HDL without apoE or apoC-III was the predominant HDL subtype. The size distribution of HDL was very similar in all the four apolipoprotein-defined subtypes. LCAT was most abundant in E-C- HDL (3.58 mg/mL, 59.6 % of plasma LCAT mass), while HDL with apoE or apoC-III had much less LCAT (19.8%, 12.2% and 8.37% of plasma LCAT respectively for E+C-, E-C+ and E+C+). LCAT mass was lower in E+C- HDL relative to E-C- HDL, but LCAT activity was similar in both fractions, signaling a greater activity-to-mass ratio associated with the presence of apoE. Both CETP mass and CETP activity showed only slight variations across HDL subspecies. There was an inverse correlation between plasma LCAT activity and concentrations of both E-C+ pre-beta HDL (r=-0.55, P =0.017) and E-C- alpha 1 HDL (r=-0.49, P =0.041). Conversely, there was a direct correlation between plasma CETP activity and concentrations of E-C+ alpha 1 HDL (r=0.52, P =0.025). Conclusions The presence of apoE in small HDL is correlated with increased LCAT activity and esterification of plasma cholesterol. These results favor an interpretation that LCAT and apoE interact to enhance anti-atherogenic pathways of HDL.

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“…We studied 18 patients (8 male, 10 female) aged 33 to 76, selected from a project about new biomarkers of insulin resistance (34). We excluded individuals with known diabetes mellitus or use of anti-diabetic medications, other endocrine disorders, diseases of the exocrine pancreas, pregnant women or patients who received oral anticoagulants or lipid-lowering drugs.…”

Section: Study Design and Participantsmentioning

confidence: 99%

“…It is known that besides apoA-I (the natural cofactor of LCAT) (31), apoE is able to activate LCAT in vitro (32), while an increase in the apoC-III content of synthetic HDL shows the opposite effect (33). In apoA-I knockout mice, apoE is able to partially rescue LCAT activity, albeit in VLDL and LDL, not in HDL (34). Despite their major relevance in lipoprotein metabolism, little is known about the influence of apoE and apoC-III over LCAT and CETP in humans.…”

mentioning

confidence: 99%

ApoE and apoC-III-defined HDL subtypes: A descriptive study of their LCAT and CETP content and activity

Amaya-Montoya

Pinzón-Cortés

Silva-Bermúdez

et al. 2020

Preprint

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Background High-density lipoproteins (HDL) functionality predicts cardiovascular risk better than HDL concentrations. The apolipoprotein composition of HDL may be a determinant of their function. Lecithin-cholesterol acyl transferase (LCAT) and cholesterol-ester transfer protein (CETP) are key enzymes for HDL-mediated reverse cholesterol transport. We assessed the distribution and activity of LCAT and CETP in HDL subspecies defined by their content of apolipoproteins E (apoE) and C-III (apoC-III) in humans. Methods We isolated in 18 adult humans of both sexes (mean age 55.6, BMI 26.9 Kg/m2, HbA1c 5.4%), four subspecies of HDL containing respectively: No apoE and no apoC-III (E-C-), apoE but not apoC-III (E+C-), apoC-III but no apoE (E-C+) and both apoE and apoC-III (E+C+). In each HDL subspecies, we measured LCAT and CETP concentration and activity using immunoenzymatic and fluorometric methods. Additionally, we determined the size distribution of HDL in each apolipoprotein-defined fraction using non-denaturing electrophoresis and anti-ApoA-I western blot. Results Similar to previous studies, HDL in the E-C- fraction was the predominant subtype. The size distribution of HDL was very similar across all four apolipoprotein-defined fractions. LCAT was most abundant in E-C- HDL (3.58 mg/mL, 59.6 % of plasma LCAT mass), while HDL with apoE or apoC-III had much less LCAT (19.8%, 12.2% and 8.37% of plasma LCAT respectively for E+C-, E-C+ and E+C+). LCAT mass was lower in E+C- HDL relative to E-C- HDL, but LCAT activity was similar in both fractions, signaling a greater activity-to-mass ratio associated with the presence of apoE. Both CETP mass and CETP activity showed only slight variations across HDL subspecies. There was an inverse correlation between plasma LCAT activity and both E-C+ pre-beta HDL (r=-0.55, p=0.017) and E-C- alpha 1 HDL (r=-0.49, p=0.041). Conversely, there was a direct correlation between E-C+ alpha 1 HDL and CETP activity in plasma (r=0.52, p=0.025). Conclusions Our results suggest that LCAT activity in humans is influenced by the presence of small interchangeable apolipoproteins. The presence of apoE in small HDL is correlated with increased LCAT activity and esterification of plasma cholesterol.

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Comparison of plasma pigment epithelium-derived factor (PEDF), retinol binding protein 4 (RBP-4), chitinase-3-like protein 1 (YKL-40) and brain-derived neurotrophic factor (BDNF) for the identification of insulin resistance

Cited by 11 publications

References 41 publications

Effect of chitinase‐3‐like protein 1 on glucose metabolism: In vitro skeletal muscle and human genetic association study

Effect of chitinase‐3‐like protein 1 on glucose metabolism: In vitro skeletal muscle and human genetic association study

ApoE and apoC-III-defined HDL subtypes: A descriptive study of their lecithin cholesterol acyl transferase and cholesteryl ester transfer protein content and activity

ApoE and apoC-III-defined HDL subtypes: A descriptive study of their LCAT and CETP content and activity

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