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Acylation Stimulating Protein

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Katherine Cianflone – One of the best experts on this subject based on the ideXlab platform.

Allan D. Sniderman – One of the best experts on this subject based on the ideXlab platform.

  • Fasting AcylationStimulating Protein is predictive of postprandial triglyceride clearance.
    Journal of lipid research, 2003
    Co-Authors: Katherine Cianflone, Robert Zakarian, Charles Couillard, Bernadette Delplanque, Jean-pierre Després, Allan D. Sniderman
    Abstract:

    Postprandial plasma triglyceride (ppTG) and NEFA clearance were stratified by plasma AcylationStimulating 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.

  • the chemoattractant receptor like Protein c5l2 binds the c3a des arg77 Acylation Stimulating Protein
    Journal of Biological Chemistry, 2003
    Co-Authors: David Kalant, Katherine Cianflone, Allan D. Sniderman, Magdalena Maslowska, Stuart A. Cain, Peter N. Monk
    Abstract:

    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 AcylationStimulating 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 AcylationStimulating properties of this peptide.

  • The Chemoattractant Receptor-like Protein C5L2 Binds the C3a des-Arg77/AcylationStimulating Protein
    The Journal of biological chemistry, 2003
    Co-Authors: David Kalant, Katherine Cianflone, Allan D. Sniderman, Magdalena Maslowska, Stuart A. Cain, Peter N. Monk
    Abstract:

    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 AcylationStimulating 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 AcylationStimulating properties of this peptide.

Magdalena Maslowska – One of the best experts on this subject based on the ideXlab platform.

  • Targeting the signaling pathway of Acylation Stimulating Protein.
    Journal of lipid research, 2005
    Co-Authors: Magdalena Maslowska, Helen Legakis, Farzad Assadi, Katherine Cianflone
    Abstract:

    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.

  • the chemoattractant receptor like Protein c5l2 binds the c3a des arg77 Acylation Stimulating Protein
    Journal of Biological Chemistry, 2003
    Co-Authors: David Kalant, Katherine Cianflone, Allan D. Sniderman, Magdalena Maslowska, Stuart A. Cain, Peter N. Monk
    Abstract:

    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 AcylationStimulating 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 AcylationStimulating properties of this peptide.

  • The Chemoattractant Receptor-like Protein C5L2 Binds the C3a des-Arg77/AcylationStimulating Protein
    The Journal of biological chemistry, 2003
    Co-Authors: David Kalant, Katherine Cianflone, Allan D. Sniderman, Magdalena Maslowska, Stuart A. Cain, Peter N. Monk
    Abstract:

    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 AcylationStimulating 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 AcylationStimulating properties of this peptide.

Marc Lapointe – One of the best experts on this subject based on the ideXlab platform.

  • Ethnic differences in Acylation Stimulating Protein (ASP) in Xinjiang Uygur autonomous region, China
    International journal of clinical and experimental medicine, 2015
    Co-Authors: Ying Gao, Katherine Cianflone, Marc Lapointe, Xiang Xie, Jie Guan, Gao Wa Bai Bu-jiaer, Dan Chen, Wei-yun Zhao
    Abstract:

    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

  • ethnic differences in Acylation Stimulating Protein asp in xinjiang uygur autonomous region china
    International Journal of Clinical and Experimental Medicine, 2015
    Co-Authors: Ying Gao, Katherine Cianflone, Marc Lapointe, Xiang Xie, Jie Guan, Dan Chen, Gao Wa Bai Bujiaer, Wei-yun Zhao
    Abstract:

    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.

  • Acylation Stimulating Protein complement c3 and lipid metabolism in ketosis prone diabetic subjects
    PLOS ONE, 2014
    Co-Authors: Yan Liu, Marc Lapointe, Priyanka Gupta, Thewjitcharoen Yotsapon, Sunthornyothin Sarat, Katherine Cianflone
    Abstract:

    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.

Jessica Smith – One of the best experts on this subject based on the ideXlab platform.