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Katherine Cianflone - One of the best experts on this subject based on the ideXlab platform.
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Cholinergic activation suppresses palmitate-induced macrophage activation and improves Acylation Stimulating Protein resistance in co-cultured adipocytes.
Experimental biology and medicine (Maywood N.J.), 2017Co-Authors: Zhou-yang Jiao, Hao-hao Zhang, Katherine CianfloneAbstract:Acylation-Stimulating Protein (ASP), produced through activation of the alternative complement immune system, modulates lipid metabolism. Using a trans-well co-culture cell model, the mitigating role of α7-nicotinic acetylcholine receptor (α7nAChR)-mediated cholinergic pathway on ASP resistance was evaluated. ASP signaling in adipocytes via its receptor C5L2 and signaling intermediates Gαq, Gβ, phosphorylated Protein kinase C-α, and Protein kinase C-ζ were markedly suppressed in the presence of TNFα or medium from palmitate-treated RAW264.7 macrophages, indicating ASP resistance. There was no direct effect of α7nAChR activation in 3T3-L1 cell culture. However, α7nAChR activation almost completely reversed the ASP resistance in adipocytes co-cultured with palmitate-treated RAW264.7 macrophages. Further, α7nAChR activation could suppress the production of pro-inflammatory molecules TNFα and interleukin-6 produced from palmitate-treated co-cultured macrophages. These results suggest that macrophages play a significant role in the pathogenesis of ASP resistance and α7nAChR activation secondarily improves adipose ASP resistance through suppression of inflammation in macrophages. Impact statement 1. Adipocyte-macrophage interaction in Acylation-Stimulating Protein (ASP) resistance 2. Lipotoxicity induced inflammatory response in ASP resistance 3. A vicious circle between lipotoxicity and inflammatory response in ASP resistance 4. Cholinergic modulation of inflammatory response in adipocyte and macrophage.
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Effects of Sugar-sweetened Beverages on plasma Acylation Stimulating Protein, Leptin & Adiponectin and Metabolic Parameters
2016Co-Authors: Reza Rezvani, Katherine Cianflone, Ph. D, John P. Mcgahan, Lars Berglund, Andrew A. Bremer, Nancy L. KeimAbstract:Objective—We determined the effects of fructose and glucose consumption on plasma Acylation Stimulating Protein (ASP), adiponectin, and leptin concentrations relative to energy intake, body weight, adiposity, circulating triglycerides, and insulin sensitivity. Design and Methods—32 overweight/obese adults consumed glucose- or fructose-sweetened beverages (25 % energy requirement) with their ad libitum diets for 8 weeks, followed by sweetened beverage consumption for 2 weeks with a standardized, energy-balanced diet. Plasma variables were measured at baseline, 2, 8 and 10 weeks, and body adiposity and insulin sensitivity at baseline and 10 weeks. Results—Fasting and postprandial ASP concentrations increased at 2 and/or 8 weeks. ASP increases correlated with changes in late-evening triglyceride concentrations. At 10 weeks, fasting adiponectin levels decreased in both groups, and decreases were inversely associated with baseline intra-abdominal fat volume. Sugar consumption increased fasting leptin concentrations; increases were associated with body weight changes. 24-h leptin profiles increased during glucose consumption and decreased during fructose consumption. These changes correlated with change
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Cross-talk between α7 nAChR-mediated cholinergic pathway and Acylation Stimulating Protein signaling in 3T3-L1 adipocytes: role of NFκB and STAT3
Biochemistry and cell biology = Biochimie et biologie cellulaire, 2015Co-Authors: Zhou-yang Jiao, Hao-hao Zhang, Zhe Zhang, Zhi-hui Tang, Katherine CianfloneAbstract:Inflammation is a key feature in adipose tissue, especially in association with obesity comorbidies. The novel adipokine Acylation Stimulating Protein (ASP) is one factor implicated in the inflammatory response. The disruption of the α7 nicotine acetylcholine receptor (α7nAChR), an important component of the endogenous non-neural cholinergic defense system, may exacerbate sustained inflammatory phenotype. We examined cholinergic regulation of ASP-initiated inflammatory response in 3T3-L1 adipocytes. Our results show that preincubation of 3T3-L1 cells with α7nAChR agonist GTS-21 significantly reduces ASP-mediated chemokine MCP-1 secretion, which is regulated though nuclear factor κB (NFκB) and signal transducer and activator of transcription 3 (STAT3). Treatment of 3T3-L1 cells with GTS-21 significantly reduced NFκB activation by DNA binding and STAT3 activation by disturbing post-translational modification.
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ethnic differences in Acylation Stimulating Protein asp in xinjiang uygur autonomous region china
International Journal of Clinical and Experimental Medicine, 2015Co-Authors: Ying Gao, Katherine Cianflone, Marc Lapointe, Xiang Xie, Jie Guan, Dan Chen, Gao Wa Bai Bujiaer, Wei-yun ZhaoAbstract:Background: Acylation Stimulating Protein (ASP) stimulates adipocyte triglyceride synthesis and glucose transport. The aim was to examine ethnic difference in ASP and the relation to lipid profile and other parameters among Han, Uygur, and Kazak healthy populations matched for BMI, age and gender distribution. Methods: 331 healthy persons were recruited in total (age 30-60 yr): 137 Han, 114 Uygur, and 80 Kazak. Anthropometric measurements including height, weight, waist circumference, hip circumference, blood pressure, ankle brachial index (ABI), and pulse wave velocity (PWV) were measured in all participants. Fasting concentrations of fasting glucose, uric acid, and lipids, including triglyceride (TG), total cholesterol (TC), low density lipoProtein cholesterol (LDL-C), high density lipoProtein cholesterol (HDL-C), ASP, complement C3, insulin, non-esterified fatty acid (NEFA) and C-reactive Protein (CRP) were measured. Results: ASP in Uygurs was significantly lower than Han subjects (P=0.0003). The Uygurs demonstrated the highest C3 (P<0.001), CRP (P=0.001), and NEFA concentrations (P=0.008), the lowest %ASP/C3 (P<0.001) and TC levels (P=0.0008) vs those in Han and Kazak populations. In the Han group, glucose, the average ABI (an index of peripheral response) and diastolic blood pressure were significantly different from both Uygur and Kazak group (P=0.0007, P=0.0003, P=0.0001) while Kazaks show the lowest waist/hip circumference (WHR) (P=0.0003). Conclusion: There are ethnic differences in ASP, C3, CRP and lipid profiles in healthy Han, Uygur, and Kazak populations. Overall, the Uygur populations presents with a disadvantageous metabolic profile as compared to Han and Kazak groups.
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Ethnic differences in Acylation Stimulating Protein (ASP) in Xinjiang Uygur autonomous region, China
International journal of clinical and experimental medicine, 2015Co-Authors: Ying Gao, Katherine Cianflone, Marc Lapointe, Xiang Xie, Jie Guan, Gao Wa Bai Bu-jiaer, Dan Chen, Wei-yun ZhaoAbstract:Background: Acylation Stimulating Protein (ASP) stimulates adipocyte triglyceride synthesis and glucose transport. The aim was to examine ethnic difference in ASP and the relation to lipid profile and other parameters among Han, Uygur, and Kazak healthy populations matched for BMI, age and gender distribution. Methods: 331 healthy persons were recruited in total (age 30-60 yr): 137 Han, 114 Uygur, and 80 Kazak. Anthropometric measurements including height, weight, waist circumference, hip circumference, blood pressure, ankle brachial index (ABI), and pulse wave velocity (PWV) were measured in all participants. Fasting concentrations of fasting glucose, uric acid, and lipids, including triglyceride (TG), total cholesterol (TC), low density lipoProtein cholesterol (LDL-C), high density lipoProtein cholesterol (HDL-C), ASP, complement C3, insulin, non-esterified fatty acid (NEFA) and C-reactive Protein (CRP) were measured. Results: ASP in Uygurs was significantly lower than Han subjects (P=0.0003). The Uygurs demonstrated the highest C3 (P
Allan D. Sniderman - One of the best experts on this subject based on the ideXlab platform.
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Fasting Acylation-Stimulating Protein is predictive of postprandial triglyceride clearance.
Journal of lipid research, 2003Co-Authors: Katherine Cianflone, Robert Zakarian, Charles Couillard, Bernadette Delplanque, Jean-pierre Després, Allan D. SnidermanAbstract:Postprandial plasma triglyceride (ppTG) and NEFA clearance were stratified by plasma Acylation-Stimulating Protein (ASP) and gender to determine the contribution of fasting ASP in a normal population (70 men; 71 women). In the highest ASP tertile only, ASP decreased over 8 h (90 ′ 9.7 nM to 70 ′ 5.9 nM, P < 0.05 males; 61.9 ′ 4.0 nM to 45.6 ′ 6.2 nM, P < 0.01 females). Fasting ASP correlated positively with ppTG response. ppTG (P < 0.0001, 2-way ANOVA, both genders) and NEFA levels progressively increased from lowest to highest ASP tertile, with the greatest differences in males. By stepwise multiple regression, the best prediction of ppTG was: (fasting ASP + apolipoProtein B + insulin + TG; r = 0.806) for men and (fasting ASP + total cholesterol; r = 0.574) for women. Leptin, body mass index, and other fasting variables did not improve the prediction. Thus, in men and women, ASP significantly predicted ppTG and NEFA clearance and, based on lower ASP, women may be more ASP sensitive than men. Plasma ASP may be useful as a fasting variable that will provide additional information regarding ppTG and NEFA clearance.
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the chemoattractant receptor like Protein c5l2 binds the c3a des arg77 Acylation Stimulating Protein
Journal of Biological Chemistry, 2003Co-Authors: David Kalant, Katherine Cianflone, Magdalena Maslowska, Allan D. Sniderman, Stuart A. Cain, Peter N. MonkAbstract:Abstract The orphan receptor C5L2 has recently been described as a high affinity binding Protein for complement fragments C5a and C3a that, unlike the previously described C5a receptor (CD88), couples only weakly to Gi-like G Proteins (Cain, S. A., and Monk, P. N. (2002) J. Biol. Chem. 277, 7165–7169). Here we demonstrate that C5L2 binds the metabolites of C4a and C3a, C4a des-Arg77, and C3a des-Arg77 (also known as the Acylation-Stimulating Protein or ASP) at a site distinct from the C5a binding site. The binding of these metabolites to C5L2 does not stimulate the degranulation of transfected rat basophilic leukemia cells either through endogenous rat G Proteins or when co-transfected with human Gα16. C3a des-Arg77/ASP and C3a can potently stimulate triglyceride synthesis in human skin fibroblasts and 3T3-L1 preadipocytes. Here we show that both cell types and human adipose tissue express C5L2 mRNA and that the human fibroblasts express C5L2 Protein at the cell surface. This is the first demonstration of the expression of C5L2 in cells that bind and respond to C3a des-Arg77/ASP and C3a. Thus C5L2, a promiscuous complement fragment-binding Protein with a high affinity site that binds C3a des-Arg77/ASP, may mediate the Acylation-Stimulating properties of this peptide.
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The Chemoattractant Receptor-like Protein C5L2 Binds the C3a des-Arg77/Acylation-Stimulating Protein
The Journal of biological chemistry, 2003Co-Authors: David Kalant, Katherine Cianflone, Magdalena Maslowska, Allan D. Sniderman, Stuart A. Cain, Peter N. MonkAbstract:Abstract The orphan receptor C5L2 has recently been described as a high affinity binding Protein for complement fragments C5a and C3a that, unlike the previously described C5a receptor (CD88), couples only weakly to Gi-like G Proteins (Cain, S. A., and Monk, P. N. (2002) J. Biol. Chem. 277, 7165–7169). Here we demonstrate that C5L2 binds the metabolites of C4a and C3a, C4a des-Arg77, and C3a des-Arg77 (also known as the Acylation-Stimulating Protein or ASP) at a site distinct from the C5a binding site. The binding of these metabolites to C5L2 does not stimulate the degranulation of transfected rat basophilic leukemia cells either through endogenous rat G Proteins or when co-transfected with human Gα16. C3a des-Arg77/ASP and C3a can potently stimulate triglyceride synthesis in human skin fibroblasts and 3T3-L1 preadipocytes. Here we show that both cell types and human adipose tissue express C5L2 mRNA and that the human fibroblasts express C5L2 Protein at the cell surface. This is the first demonstration of the expression of C5L2 in cells that bind and respond to C3a des-Arg77/ASP and C3a. Thus C5L2, a promiscuous complement fragment-binding Protein with a high affinity site that binds C3a des-Arg77/ASP, may mediate the Acylation-Stimulating properties of this peptide.
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Acylation-Stimulating Protein (ASP) Deficiency Induces Obesity Resistance and Increased Energy Expenditure in ob/obMice
The Journal of biological chemistry, 2002Co-Authors: Zhunan Xia, Allan D. Sniderman, Katherine CianfloneAbstract:Abstract Acylation-Stimulating Protein (ASP) acts as a paracrine signal to increase triglyceride synthesis in adipocytes. ASP administration results in more rapid postprandial lipid clearance. In mice, C3 (the precursor to ASP) knockout results in ASP deficiency and leads to reduced body fat and leptin levels. The protective potential of ASP deficiency against obesity and involvement of the leptin pathway were examined in ob/ob C3(−/−) double knockout mice (2KO). Compared with age-matched ob/ob mice, 2KO mice had delayed postprandial triglyceride and fatty acid clearance; associated with decreased body weight (4–17 weeks age: male: −13.7%, female: −20.6%, p < 0.0001) and HOMA (homeostasis model assessment) index (−37.7%), suggesting increased insulin sensitivity. By contrast, food intake in 2KO mice was +9.1% higher overob/ob mice (p < 0.001, 2KO 5.1 ± 0.2 g/day, ob/ob 4.5 ± 0.2 g/day, wild type 2.6 ± 0.1 g/day). The hyperphagia/leanness was balanced by a 28.5% increase in energy expenditure (oxygen consumption: 2KO, 131 ± 8.9 ml/h; ob/ob, 102 ± 4.5 ml/h; p< 0.01; wild type, 144 ± 8.9 ml/h). These results suggest that the ASP regulation of energy storage may influence energy expenditure and dynamic metabolic balance.
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Regulation by retinoic acid of Acylation-Stimulating Protein and complement C3 in human adipocytes
Biochemical Journal, 2001Co-Authors: Thea Scantlebury, Allan D. Sniderman, Katherine CianfloneAbstract:Acylation-Stimulating Protein (ASP), a product of complement C3, stimulates triacylglycerol synthesis in adipocytes. Previous studies have identified transthyretin, associated with chylomicrons, as a stimulator of C3 and ASP production. Since both transthyretin and chylomicrons transport retinyl ester/retinol, our goal was to investigate whether retinoic acid (RA) could be a potential hormonal mediator of the effect. Inhibitors of Protein synthesis and Protein secretion eliminated the stimulatory effects of chylomicrons on both C3 and ASP production in human differentiated adipocytes, suggesting that de novo Protein synthesis and secretion are both required. Incubation with chylomicrons increased C3 mRNA levels (37+/-1.5%). RA alone or with chylomicrons had a stimulatory effect on C3 production (29-fold at 16.6 nM RA) and ASP production. An RA receptor antagonist blocked stimulation of C3 mRNA and C3 secretion by both RA and chylomicrons. Finally, RA and chylomicrons activated a 1.8 kb C3-promoter-luciferase construct transfected into 3T3-F442 and 3T3-L1 cells (by 41+/-0.2% and 69+/-0.3% respectively), possibly via RA receptor half-sites identified by sequence analysis. This is the first evidence documenting stimulation by RA of the C3 gene. Thus we propose RA as a novel cellular trigger in chylomicrons that subsequently results in increased ASP production by adipocytes after a meal.
Magdalena Maslowska - One of the best experts on this subject based on the ideXlab platform.
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Targeting the signaling pathway of Acylation Stimulating Protein.
Journal of lipid research, 2005Co-Authors: Magdalena Maslowska, Helen Legakis, Farzad Assadi, Katherine CianfloneAbstract:Acylation Stimulating Protein (ASP; C3adesArg) stimulates triglyceride synthesis (TGS) and glucose transport in preadipocytes/adipocytes through C5L2, a G-Protein-coupled receptor. Here, ASP signaling is compared with insulin in 3T3-L1 cells. ASP stimulation is not Galpha(s) or Galpha(i) mediated (pertussis and cholera toxin insensitive), suggesting G(alphaq) as a candidate. Phospholipase C (PLC) is required, because the Ca(2+) chelator 1,2-bis(o-aminophenoxy) ethane-N,N,N',N'-tetraacetic acid tetra(acetoxymethyl) ester and the PLC inhibitor U73122 decreased ASP stimulation of TGS by 93.1% (P < 0.0.001) and 86.1% (P < 0.004), respectively. Wortmannin and LY294002 blocked ASP effect by 69% (P < 0.001) and 116.1% (P < 0.003), respectively, supporting phosphatidylinositol 3-kinase (PI3K) involvement. ASP induced rapid, transient Akt phosphorylation (maximal, 5 min; basal, 45 min), which was blocked by Akt inhibition, resembling treatment by insulin. Downstream of PI3K, mamalian target of rapaycin (mTOR) is required for insulin but not ASP action. By contrast, both ASP and insulin activate the mitogen-activated Protein kinase/extracellular signal-regulated kinase (MAPK/ERK(1/2)) pathway, with rapid, pronounced increases in ERK(1/2) phosphorylation, effects partially blocked by PD98059 (64.7% and 65.9% inhibition, respectively; P < 0.001). Time-dependent (maximal, 30 min) transient calcium-dependent phospholipase A(2) (cPLA(2))(-Ser505) phosphorylation (by MAPK/ERK(1/2)) was demonstrated by Western blot analysis. ASP signaling involves sequential activation of PI3K and PLC, with downstream activation of Protein kinase C, Akt, MAPK/ERK(1/2), and cPLA(2), all of which leads to an effective and prolonged stimulation of TGS.
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the chemoattractant receptor like Protein c5l2 binds the c3a des arg77 Acylation Stimulating Protein
Journal of Biological Chemistry, 2003Co-Authors: David Kalant, Katherine Cianflone, Magdalena Maslowska, Allan D. Sniderman, Stuart A. Cain, Peter N. MonkAbstract:Abstract The orphan receptor C5L2 has recently been described as a high affinity binding Protein for complement fragments C5a and C3a that, unlike the previously described C5a receptor (CD88), couples only weakly to Gi-like G Proteins (Cain, S. A., and Monk, P. N. (2002) J. Biol. Chem. 277, 7165–7169). Here we demonstrate that C5L2 binds the metabolites of C4a and C3a, C4a des-Arg77, and C3a des-Arg77 (also known as the Acylation-Stimulating Protein or ASP) at a site distinct from the C5a binding site. The binding of these metabolites to C5L2 does not stimulate the degranulation of transfected rat basophilic leukemia cells either through endogenous rat G Proteins or when co-transfected with human Gα16. C3a des-Arg77/ASP and C3a can potently stimulate triglyceride synthesis in human skin fibroblasts and 3T3-L1 preadipocytes. Here we show that both cell types and human adipose tissue express C5L2 mRNA and that the human fibroblasts express C5L2 Protein at the cell surface. This is the first demonstration of the expression of C5L2 in cells that bind and respond to C3a des-Arg77/ASP and C3a. Thus C5L2, a promiscuous complement fragment-binding Protein with a high affinity site that binds C3a des-Arg77/ASP, may mediate the Acylation-Stimulating properties of this peptide.
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The Chemoattractant Receptor-like Protein C5L2 Binds the C3a des-Arg77/Acylation-Stimulating Protein
The Journal of biological chemistry, 2003Co-Authors: David Kalant, Katherine Cianflone, Magdalena Maslowska, Allan D. Sniderman, Stuart A. Cain, Peter N. MonkAbstract:Abstract The orphan receptor C5L2 has recently been described as a high affinity binding Protein for complement fragments C5a and C3a that, unlike the previously described C5a receptor (CD88), couples only weakly to Gi-like G Proteins (Cain, S. A., and Monk, P. N. (2002) J. Biol. Chem. 277, 7165–7169). Here we demonstrate that C5L2 binds the metabolites of C4a and C3a, C4a des-Arg77, and C3a des-Arg77 (also known as the Acylation-Stimulating Protein or ASP) at a site distinct from the C5a binding site. The binding of these metabolites to C5L2 does not stimulate the degranulation of transfected rat basophilic leukemia cells either through endogenous rat G Proteins or when co-transfected with human Gα16. C3a des-Arg77/ASP and C3a can potently stimulate triglyceride synthesis in human skin fibroblasts and 3T3-L1 preadipocytes. Here we show that both cell types and human adipose tissue express C5L2 mRNA and that the human fibroblasts express C5L2 Protein at the cell surface. This is the first demonstration of the expression of C5L2 in cells that bind and respond to C3a des-Arg77/ASP and C3a. Thus C5L2, a promiscuous complement fragment-binding Protein with a high affinity site that binds C3a des-Arg77/ASP, may mediate the Acylation-Stimulating properties of this peptide.
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Of mice and men (and women) and the Acylation-Stimulating Protein pathway.
Current opinion in lipidology, 2000Co-Authors: Allan D. Sniderman, Magdalena Maslowska, Katherine CianfloneAbstract:The storage and release of energy by adipocytes is of fundamental biologic importance. Not surprisingly, therefore, the rate at which these processes occur can be modulated by a variety of physiologic molecules. A newly recognized participant is produced by adipocytes themselves: Acylation-Stimulating Protein (ASP). This article focuses on the most recent in-vivo evidence regarding how the ASP pathway may influence energy storage and release. In brief, the rate at which triglycerides are cleared from plasma (i.e. the rate at which they are hydrolysed) is determined by lipoProtein lipase and insulin, which is the principal hormone that regulates lipoProtein lipase. By contrast, the ASP pathway modulates the rate at which fatty acids are taken up and converted to triglycerides by adipocytes. Under certain circumstances, however, reduction of activity of the ASP pathway may negatively impact on the first step of the process. ASP also influences the rate at which fatty acids are released by adipocytes, and it is clear that insulin and ASP interact in a variety of ways that involve energy storage and release. Accordingly, to understand the impact of any intervention on energy storage and release by adipocytes, the effects of both insulin and ASP must be taken into account.
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Acylation Stimulating Protein (ASP), an adipocyte autocrine: new directions.
Seminars in cell & developmental biology, 1999Co-Authors: Katherine Cianflone, Magdalena Maslowska, Allan D. SnidermanAbstract:Acylation Stimulating Protein (ASP) is an adipocyte-derived Protein which has potent anabolic effects on human adipose tissue for both glucose and free fatty acid (FFA) storage. Our hypothesis is that: (i) ASP is produced by adipocytes in specific response to stimuli that initiate efficient fat storage; (ii) ASP interacts with a specific adipocyte receptor triggering an intracellular signalling pathway which activates triglyceride synthesis and fat storage; and (iii) that absence (ASP knockout mouse) or excess (in normal or obese mice) of ASP will result in physiological changes of plasma fat clearance and adipose tissue metabolism. The present review focuses on advances in ASP within the last 2 years with particular emphasis on these three aspects of ASP.
Marc Lapointe - One of the best experts on this subject based on the ideXlab platform.
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Ethnic differences in Acylation Stimulating Protein (ASP) in Xinjiang Uygur autonomous region, China
International journal of clinical and experimental medicine, 2015Co-Authors: Ying Gao, Katherine Cianflone, Marc Lapointe, Xiang Xie, Jie Guan, Gao Wa Bai Bu-jiaer, Dan Chen, Wei-yun ZhaoAbstract:Background: Acylation Stimulating Protein (ASP) stimulates adipocyte triglyceride synthesis and glucose transport. The aim was to examine ethnic difference in ASP and the relation to lipid profile and other parameters among Han, Uygur, and Kazak healthy populations matched for BMI, age and gender distribution. Methods: 331 healthy persons were recruited in total (age 30-60 yr): 137 Han, 114 Uygur, and 80 Kazak. Anthropometric measurements including height, weight, waist circumference, hip circumference, blood pressure, ankle brachial index (ABI), and pulse wave velocity (PWV) were measured in all participants. Fasting concentrations of fasting glucose, uric acid, and lipids, including triglyceride (TG), total cholesterol (TC), low density lipoProtein cholesterol (LDL-C), high density lipoProtein cholesterol (HDL-C), ASP, complement C3, insulin, non-esterified fatty acid (NEFA) and C-reactive Protein (CRP) were measured. Results: ASP in Uygurs was significantly lower than Han subjects (P=0.0003). The Uygurs demonstrated the highest C3 (P
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ethnic differences in Acylation Stimulating Protein asp in xinjiang uygur autonomous region china
International Journal of Clinical and Experimental Medicine, 2015Co-Authors: Ying Gao, Katherine Cianflone, Marc Lapointe, Xiang Xie, Jie Guan, Dan Chen, Gao Wa Bai Bujiaer, Wei-yun ZhaoAbstract:Background: Acylation Stimulating Protein (ASP) stimulates adipocyte triglyceride synthesis and glucose transport. The aim was to examine ethnic difference in ASP and the relation to lipid profile and other parameters among Han, Uygur, and Kazak healthy populations matched for BMI, age and gender distribution. Methods: 331 healthy persons were recruited in total (age 30-60 yr): 137 Han, 114 Uygur, and 80 Kazak. Anthropometric measurements including height, weight, waist circumference, hip circumference, blood pressure, ankle brachial index (ABI), and pulse wave velocity (PWV) were measured in all participants. Fasting concentrations of fasting glucose, uric acid, and lipids, including triglyceride (TG), total cholesterol (TC), low density lipoProtein cholesterol (LDL-C), high density lipoProtein cholesterol (HDL-C), ASP, complement C3, insulin, non-esterified fatty acid (NEFA) and C-reactive Protein (CRP) were measured. Results: ASP in Uygurs was significantly lower than Han subjects (P=0.0003). The Uygurs demonstrated the highest C3 (P<0.001), CRP (P=0.001), and NEFA concentrations (P=0.008), the lowest %ASP/C3 (P<0.001) and TC levels (P=0.0008) vs those in Han and Kazak populations. In the Han group, glucose, the average ABI (an index of peripheral response) and diastolic blood pressure were significantly different from both Uygur and Kazak group (P=0.0007, P=0.0003, P=0.0001) while Kazaks show the lowest waist/hip circumference (WHR) (P=0.0003). Conclusion: There are ethnic differences in ASP, C3, CRP and lipid profiles in healthy Han, Uygur, and Kazak populations. Overall, the Uygur populations presents with a disadvantageous metabolic profile as compared to Han and Kazak groups.
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Acylation Stimulating Protein complement c3 and lipid metabolism in ketosis prone diabetic subjects
PLOS ONE, 2014Co-Authors: Yan Liu, Marc Lapointe, Priyanka Gupta, Thewjitcharoen Yotsapon, Sunthornyothin Sarat, Katherine CianfloneAbstract:Background Ketosis-prone diabetes (KPDM) is new-onset diabetic ketoacidosis without precipitating factors in non-type 1 diabetic patients; after management, some are withdrawn from exogenous insulin, although determining factors remain unclear. Methods Twenty KPDM patients and twelve type 1 diabetic patients (T1DM), evaluated at baseline, 12 and 24 months with/without insulin maintenance underwent a standardized mixed-meal tolerance test (MMTT) for 2 h. Results At baseline, triglyceride and C3 were higher during MMTT in KPDM vs. T1DM (p<0.0001) with no differences in non-esterified fatty acids (NEFA) while Acylation Stimulating Protein (ASP) tended to be higher. Within 12 months, 11 KPDM were withdrawn from insulin treatment (KPDM-ins), while 9 were maintained (KPDM+ins). NEFA was lower in KPDM-ins vs. KPDM+ins at baseline (p = 0.0006), 12 months (p<0.0001) and 24 months (p<0.0001) during MMTT. NEFA in KPDM-ins decreased over 30–120 minutes (p<0.05), but not in KPDM+ins. Overall, C3 was higher in KPDM-ins vs KPDM+ins at 12 months (p = 0.0081) and 24 months (p = 0.0019), while ASP was lower at baseline (p = 0.0024) and 12 months (p = 0.0281), with a decrease in ASP/C3 ratio. Conclusions Notwithstanding greater adiposity in KPDM-ins, greater NEFA decreases and lower ASP levels during MMTT suggest better insulin and ASP sensitivity in these patients.
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Preoperative Fasting Vaspin, Acylation Stimulating Protein and IL-6 levels.
2014Co-Authors: Ponce Cedric Fouejeu Wamba, Julie Martin, Paul Poirier, Marc Lapointe, Marjorie Bastien, Katherine CianfloneAbstract:Fasting vaspin (ng/mL), Acylation Stimulating Protein (ASP, nmol/L) and interleukin-6 (IL-6, pg/mL) levels were measured in 77 severely obese patients (22 men and 55 women). Distribution of fasting plasma vaspin levels (ng/mL) according to frequency is given in all subjects (A), women (B) and men (C). D) Spearman correlation of fasting vaspin to fasting ASP (r = 0.371, p = 0.001). E) Spearman correlation of fasting vaspin to fasting IL-6 (r = .303, p = 0.01).
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Preoperative and postoperative profile of fasting plasma Acylation Stimulating Protein, Interleukin-6 and Visfatin.
2014Co-Authors: Ponce Cedric Fouejeu Wamba, Julie Martin, Paul Poirier, Marc Lapointe, Marjorie Bastien, Katherine CianfloneAbstract:Fasting plasma Acylation Stimulating Protein (ASP) (A), Interleukin-6 (IL-6) (B), and Visfatin (C) were assessed at multiple time points: preoperative baseline (BSL) and postoperative 24 hours (24H), 5 days (5D), 6 and 12 months (6M and 12M). Patients were separated into 2 groups based on preoperative fasting vaspin levels: high vaspin (HI-grp, vaspin ≥2.5 ng/mL, black circles and low vaspin (LO-grp, vaspin
Jessica Smith - One of the best experts on this subject based on the ideXlab platform.
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cross sectional associations of Acylation Stimulating Protein asp and adipose tissue gene expression with estradiol and progesterone in pre and postmenopausal women
Clinical Endocrinology, 2014Co-Authors: Reza Rezvani, Abhishek Gupta, Jessica Smith, Pegah Poursharifi, Picard Marceau, Louis Pérusse, Claude Bouchard, André Tchernof, Katherine CianfloneAbstract:SummaryObjective Sex steroid hormones play an important regulatory role in fat metabolism and obesity. We hypothesized involvement of interactions between ovarian hormones with Acylation Stimulating Protein (ASP). Design, patients and measurements In 392 women with wide age (18–69 years) and body size (BMI: 17 to 90 kg/m2) ranges, fasting plasma levels of ASP, ovarian hormones, glucose, adiponectin and lipids/apolipoProteins were assessed, along with determination of metabolic syndrome (MS) features. Gene expression of C3 (ASP precursor) and related receptors C5L2, C3aR and C5aR in subcutaneous and omental adipose tissues was measured in a subset. Results Acylation Stimulating Protein correlated negatively with concentrations of estradiol (P < 0·0001), adiponectin (P < 0·001) and apolipoProtein A1 (P < 0·001) and positively with apolipoProtein B levels (P < 0·001), systolic blood pressure (P < 0·001), waist circumference (P < 0·001), and triglyceride concentrations (P < 0·01). In age-matched groups of lean, overweight, metabolically healthy obese (MHO) and obese with metabolic syndrome (MSO), there was a stepwise increase in ASP levels (P < 0·001) while concentrations of adiponectin (P < 0·0001) and estradiol (P < 0·001) but not those of progesterone decreased. Progesterone but not estradiol levels correlated positively with C3 gene expression in omental adipose tissue (P < 0·05) and negatively with C5L2 expression in both omental (P < 0·01) and subcutaneous (P < 0·05) adipose tissues. Conclusion Our results are consistent with the concept that sex hormones differentially influence circulating ASP and adipose tissue gene expression of its related Proteins in a depot-specific manner. ASP may play a role in the regulation of regional fat metabolism through interactions with sex hormones in women.
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Cross-sectional associations of Acylation Stimulating Protein (ASP) and adipose tissue gene expression with estradiol and progesterone in pre- and postmenopausal women.
Clinical endocrinology, 2014Co-Authors: Reza Rezvani, Abhishek Gupta, Jessica Smith, Pegah Poursharifi, Picard Marceau, Louis Pérusse, Claude Bouchard, André Tchernof, Katherine CianfloneAbstract:SummaryObjective Sex steroid hormones play an important regulatory role in fat metabolism and obesity. We hypothesized involvement of interactions between ovarian hormones with Acylation Stimulating Protein (ASP). Design, patients and measurements In 392 women with wide age (18–69 years) and body size (BMI: 17 to 90 kg/m2) ranges, fasting plasma levels of ASP, ovarian hormones, glucose, adiponectin and lipids/apolipoProteins were assessed, along with determination of metabolic syndrome (MS) features. Gene expression of C3 (ASP precursor) and related receptors C5L2, C3aR and C5aR in subcutaneous and omental adipose tissues was measured in a subset. Results Acylation Stimulating Protein correlated negatively with concentrations of estradiol (P
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Acylation Stimulating Protein is higher in inuit from nunavik compared to a southern quebec population
International Journal of Circumpolar Health, 2009Co-Authors: Jessica Smith, Katherine Cianflone, Eric Dewailly, Marieludivine Châteaudegat, Marieclaude Vohl, Pierre JulienAbstract:Objectives. The Inuit of Nunavik in northern Quebec have a lower risk for ischemic heart disease (IHD) compared to Caucasian populations. Acylation Stimulating Protein (ASP), which is involved in the storage of dietary fat, may play a role. The objective of the study was to determine plasma concentration of ASP in an Inuit and a southern Quebec Caucasian population. Study design. This is a cross-sectional study evaluating the relationship between ASP and dietary factors, such as retinol, whose intake is higher in the Inuit. As well, concentrations of ASP were evaluated in relationship to components of the metabolic syndrome. Methods. Medical history was collected via a questionnaire and anthropometric measurements and blood samples were collected. Results. ASP was significantly higher in both the Inuit men and women compared to Caucasian men (66.1±4.1 nM vs 27.5±2.5 nM, p<0.0001) and women (71.8±3.8 nM vs 29.4±1.3 nM, p<0.0001). In addition, ASP significantly correlated with total retinol (r=0.17, p=0.02) and free retinol (r=0.15, p=0.04) in Inuit men but not with other distinctive dietary markers such as omega- 3 fatty acids. Conclusions. Inuit men and women have higher ASP which was unrelated to the number of risk factors for IHD that were present. (Int J Circumpolar Health 2009; 68(5): 421–432) Keywords: Acylation Stimulating Protein (ASP), Inuit, retinol, metabolic syndrome
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Acylation Stimulating Protein is higher in Inuit from nunavik compared to a southern Quebec population
International journal of circumpolar health, 2009Co-Authors: Jessica Smith, Katherine Cianflone, Eric Dewailly, Marieclaude Vohl, Marie-ludivine Château-degat, Pierre JulienAbstract:Objectives. The Inuit of Nunavik in northern Quebec have a lower risk for ischemic heart disease (IHD) compared to Caucasian populations. Acylation Stimulating Protein (ASP), which is involved in the storage of dietary fat, may play a role. The objective of the study was to determine plasma concentration of ASP in an Inuit and a southern Quebec Caucasian population. Study design. This is a cross-sectional study evaluating the relationship between ASP and dietary factors, such as retinol, whose intake is higher in the Inuit. As well, concentrations of ASP were evaluated in relationship to components of the metabolic syndrome. Methods. Medical history was collected via a questionnaire and anthropometric measurements and blood samples were collected. Results. ASP was significantly higher in both the Inuit men and women compared to Caucasian men (66.1±4.1 nM vs 27.5±2.5 nM, p
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change in plasma Acylation Stimulating Protein during euglycaemic hyperinsulinaemic clamp in overweight and obese postmenopausal women a monet study
Clinical Endocrinology, 2009Co-Authors: David H Stpierre, Katherine Cianflone, Jessica Smith, Lise Coderre, Antony D. Karelis, Pascal Imbeault, Jean-marc Lavoie, Remi RabasalhoretAbstract:St-Pierre DH, Cianflone K, Smith J, Coderre L, Karelis AD, Imbeault P, Lavoie JM, Rabasa-Lhoret R. OBJECTIVE : Acylation-Stimulating Protein (ASP) has been shown to positively stimulate fatty acid esterification and glucose uptake in adipocytes. In vitro studies demonstrate that insulin stimulates ASP secretion from adipocytes. Individuals with obesity and/or metabolic disturbances (insulin resistance and type 2 diabetes) have increased plasma ASP. DESIGN : The present study was designed to (...)
