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Academic literature on the topic 'AS160'

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Published: 4 June 2021
Last updated: 1 February 2022

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Journal articles on the topic "AS160"

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Kim, Hyo-Young, Hyo-Jung Choi, Jung-Suk Lim, Eui-Jung Park, Hyun Jun Jung, Yu-Jung Lee, Sang-Yeob Kim, and Tae-Hwan Kwon. "Emerging role of Akt substrate protein AS160 in the regulation of AQP2 translocation." American Journal of Physiology-Renal Physiology 301, no. 1 (July 2011): F151—F161. http://dx.doi.org/10.1152/ajprenal.00519.2010.

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AS160, a novel Akt substrate of 160 kDa, contains a Rab GTPase-activating protein (GAP) domain. The present study examined the role of Akt and AS160 in aquaporin-2 (AQP2) trafficking. The main strategy was to examine the changes in AQP2 translocation in response to small interfering RNA (siRNA)-mediated AS160 knockdown in mouse cortical collecting duct cells (M-1 cells and mpkCCDc14 cells). Short-term dDAVP treatment in M-1 cells stimulated phosphorylation of Akt (S473) and AS160, which was also seen in mpkCCDc14 cells. Conversely, the phosphoinositide 3-kinase (PI3K) inhibitor LY 294002 diminished phosphorylation of Akt (S473) and AS160. Moreover, siRNA-mediated Akt1 knockdown was associated with unchanged total AS160 but decreased phospho-AS160 expression, indicating that phosphorylation of AS160 is dependent on PI3K/Akt pathways. siRNA-mediated AS160 knockdown significantly decreased total AS160 and phospho-AS160 expression. Immunocytochemistry revealed that AS160 knockdown in mpkCCDc14 cells was associated with increased AQP2 density in the plasma membrane [135 ± 3% of control mpkCCDc14 cells ( n = 65), P < 0.05, n = 64] despite the absence of dDAVP stimulation. Moreover, cell surface biotinylation assays of mpkCCDc14 cells with AS160 knockdown exhibited significantly higher AQP2 expression [150 ± 15% of control mpkCCDc14 cells ( n = 3), P < 0.05, n = 3]. Taken together, PI3K/Akt pathways mediate the dDAVP-induced AS160 phosphorylation, and AS160 knockdown is associated with higher AQP2 expression in the plasma membrane. Since AS160 contains a GAP domain leading to a decrease in the active GTP-bound form of AS160 target Rab proteins for vesicle trafficking, decreased expression of AS160 is likely to play a role in the translocation of AQP2 to the plasma membrane.
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Hargett, Stefan R., Natalie N. Walker, and Susanna R. Keller. "Rab GAPs AS160 and Tbc1d1 play nonredundant roles in the regulation of glucose and energy homeostasis in mice." American Journal of Physiology-Endocrinology and Metabolism 310, no. 4 (February 15, 2016): E276—E288. http://dx.doi.org/10.1152/ajpendo.00342.2015.

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The related Rab GTPase-activating proteins (Rab GAPs) AS160 and Tbc1d1 regulate the trafficking of the glucose transporter GLUT4 that controls glucose uptake in muscle and fat cells and glucose homeostasis. AS160- and Tbc1d1-deficient mice exhibit different adipocyte- and skeletal muscle-specific defects in glucose uptake, GLUT4 expression and trafficking, and glucose homeostasis. A recent study analyzed male mice with simultaneous deletion of AS160 and Tbc1d1 (AS160−/−/Tbc1d1−/− mice). Herein, we describe abnormalities in male and female AS160−/−/Tbc1d1−/− mice on another strain background. We confirm the earlier observation that GLUT4 expression and glucose uptake defects of single-knockout mice join in AS160−/−/Tbc1d1−/− mice to affect all skeletal muscle and adipose tissues. In large mixed fiber-type skeletal muscles, changes in relative basal GLUT4 plasma membrane association in AS160−/− and Tbc1d1−/− mice also combine in AS160−/−/Tbc1d1−/− mice. However, we found different glucose uptake abnormalities in isolated skeletal muscles and adipocytes than reported previously, resulting in different interpretations of how AS160 and Tbc1d1 regulate GLUT4 translocation to the cell surface. In support of a larger role for AS160 in glucose homeostasis, in contrast with the previous study, we find similarly impaired glucose and insulin tolerance in AS160−/−/Tbc1d1−/− and AS160−/− mice. However, in vivo glucose uptake abnormalities in AS160−/−/Tbc1d1−/− skeletal muscles differ from those observed previously in AS160−/− mice, indicating additional defects due to Tbc1d1 deletion. Similar to AS160- and Tbc1d1-deficient mice, AS160−/−/Tbc1d1−/− mice show sex-specific abnormalities in glucose and energy homeostasis. In conclusion, our study supports nonredundant functions for AS160 and Tbc1d1.
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Lansey, Melissa N., Natalie N. Walker, Stefan R. Hargett, Joseph R. Stevens, and Susanna R. Keller. "Deletion of Rab GAP AS160 modifies glucose uptake and GLUT4 translocation in primary skeletal muscles and adipocytes and impairs glucose homeostasis." American Journal of Physiology-Endocrinology and Metabolism 303, no. 10 (November 15, 2012): E1273—E1286. http://dx.doi.org/10.1152/ajpendo.00316.2012.

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Tight control of glucose uptake in skeletal muscles and adipocytes is crucial to glucose homeostasis and is mediated by regulating glucose transporter GLUT4 subcellular distribution. In cultured cells, Rab GAP AS160 controls GLUT4 intracellular retention and release to the cell surface and consequently regulates glucose uptake into cells. To determine AS160 function in GLUT4 trafficking in primary skeletal muscles and adipocytes and investigate its role in glucose homeostasis, we characterized AS160 knockout (AS160−/−) mice. We observed increased and normal basal glucose uptake in isolated AS160−/− adipocytes and soleus, respectively, while insulin-stimulated glucose uptake was impaired and GLUT4 expression decreased in both. No such abnormalities were found in isolated AS160−/− extensor digitorum longus muscles. In plasma membranes isolated from AS160−/− adipose tissue and gastrocnemius/quadriceps, relative GLUT4 levels were increased under basal conditions and remained the same after insulin treatment. Concomitantly, relative levels of cell surface-exposed GLUT4, determined with a glucose transporter photoaffinity label, were increased in AS160−/− adipocytes and normal in AS160−/− soleus under basal conditions. Insulin augmented cell surface-exposed GLUT4 in both. These observations suggest that AS160 is essential for GLUT4 intracellular retention and regulation of glucose uptake in adipocytes and skeletal muscles in which it is normally expressed. In vivo studies revealed impaired insulin tolerance in the presence of normal (male) and impaired (female) glucose tolerance. Concurrently, insulin-elicited increases in glucose disposal were abolished in all AS160−/− skeletal muscles and liver but not in AS160−/− adipose tissues. This suggests AS160 as a target for differential manipulation of glucose homeostasis.
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Alkhateeb, Hakam, Adrian Chabowski, Jan F. C. Glatz, Brendon Gurd, Joost J. F. P. Luiken, and Arend Bonen. "Restoring AS160 phosphorylation rescues skeletal muscle insulin resistance and fatty acid oxidation while not reducing intramuscular lipids." American Journal of Physiology-Endocrinology and Metabolism 297, no. 5 (November 2009): E1056—E1066. http://dx.doi.org/10.1152/ajpendo.90908.2008.

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We examined whether AICAR or leptin rapidly rescued skeletal muscle insulin resistance via increased palmitate oxidation, reductions in intramuscular lipids, and/or restoration of insulin-stimulated AS60 phosphorylation. Incubation with palmitate (2 mM, 0–18 h) induced insulin resistance in soleus muscle. From 12–18 h, palmitate was removed or AICAR or leptin was provided while 2 mM palmitate was maintained. Palmitate oxidation, intramuscular triacylglycerol, diacylglycerol, ceramide, AMPK phosphorylation, basal and insulin-stimulated glucose transport, plasmalemmal GLUT4, and Akt and AS160 phosphorylation were examined at 0, 6, 12, and 18 h. Palmitate treatment (12 h) increased intramuscular lipids (triacylglycerol +54%, diacylglycerol +11%, total ceramide +18%, C16:0 ceramide +60%) and AMPK phosphorylation (+118%), whereas it reduced fatty acid oxidation (−60%) and insulin-stimulated glucose transport (−70%), GLUT4 translocation (−50%), and AS160 phosphorylation (−40%). Palmitate removal did not rescue insulin resistance or associated parameters. The AICAR and leptin treatments did not consistently reduce intramuscular lipids, but they did rescue palmitate oxidation and insulin-stimulated glucose transport, GLUT4 translocation, and AS160 phosphorylation. Increased AMPK phosphorylation was associated with these improvements only when AICAR and leptin were present. Hence, across all experiments, AMPK phosphorylation did not correlate with any parameters. In contrast, palmitate oxidation and insulin-stimulated AS160 phosphorylation were highly correlated ( r = 0.83). We speculate that AICAR and leptin activate both of these processes concomitantly, involving activation of unknown kinases in addition to AMPK. In conclusion, despite the maintenance of high concentrations of palmitate (2 mM), as well as increased concentrations of intramuscular lipids (triacylglycerol, diacylglycerol, and ceramide), the rapid AICAR- and leptin-mediated rescue of palmitate-induced insulin resistance is attributable to the restoration of insulin-stimulated AS160 phosphorylation and GLUT4 translocation.
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Cartee, Gregory D., and Jørgen F. P. Wojtaszewski. "Role of Akt substrate of 160 kDa in insulin-stimulated and contraction-stimulated glucose transport." Applied Physiology, Nutrition, and Metabolism 32, no. 3 (March 2007): 557–66. http://dx.doi.org/10.1139/h07-026.

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Insulin and exercise, the most important physiological stimuli to increase glucose transport in skeletal muscle, trigger a redistribution of GLUT4 glucose transporter proteins from the cell interior to the cell surface, thereby increasing glucose transport capacity. The most distal insulin signaling protein that has been linked to GLUT4 translocation, Akt substrate of 160 kDa (AS160), becomes phosphorylated in insulin-stimulated 3T3-L1 adipocytes; this is im​portant for insulin-stimulated GLUT4 translocation and glucose transport. Insulin also induces a rapid and dose-dependent increase in AS160 phosphorylation in skeletal muscle. Available data from skeletal muscle support the concepts developed in adipocytes with regard to the role AS160 plays in the regulation of insulin-stimulated glucose transport. In vivo exercise, in vitro contractions, or in situ contractions can also stimulate AS160 phosphorylation. AMP-activated protein kinase (AMPK) is likely important for phosphorylating AS160 in response to exercise/contractile activity, whereas Akt2 appears to be important for insulin-stimulated AS160 phosphorylation in muscle. Evidence of a role for AS160 in exercise/contraction-stimulated glucose uptake is currently inconclusive. The distinct signaling pathways that are stimulated by insulin and exercise/contraction converge at AS160. Although AS160 phosphorylation is apparently important for insulin-stimulated GLUT4 translocation and glucose transport, it is uncertain whether elevated AS160 phosphorylation plays a similar role with exercise/contraction.
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Liang, Xiubin, Michael B. Butterworth, Kathryn W. Peters, and Raymond A. Frizzell. "AS160 Modulates Aldosterone-stimulated Epithelial Sodium Channel Forward Trafficking." Molecular Biology of the Cell 21, no. 12 (June 15, 2010): 2024–33. http://dx.doi.org/10.1091/mbc.e10-01-0042.

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Aldosterone-induced increases in apical membrane epithelial sodium channel (ENaC) density and Na transport involve the induction of 14-3-3 protein expression and their association with Nedd4-2, a substrate of serum- and glucocorticoid-induced kinase (SGK1)-mediated phosphorylation. A search for other 14-3-3 binding proteins in aldosterone-treated cortical collecting duct (CCD) cells identified the Rab-GAP, AS160, an Akt/PKB substrate whose phosphorylation contributes to the recruitment of GLUT4 transporters to adipocyte plasma membranes in response to insulin. In CCD epithelia, aldosterone (10 nM, 24 h) increased AS160 protein expression threefold, with a time-course similar to increases in SGK1 expression. In the absence of aldosterone, AS160 overexpression increased total ENaC expression 2.5-fold but did not increase apical membrane ENaC or amiloride-sensitive Na current (Isc). In AS160 overexpressing epithelia, however, aldosterone increased apical ENaC and Isc 2.5-fold relative to aldosterone alone, thus recruiting the accumulated ENaC to the apical membrane. Conversely, AS160 knockdown increased apical membrane ENaC and Isc under basal conditions to ∼80% of aldosterone-stimulated values, attenuating further steroid effects. Aldosterone induced AS160 phosphorylation at five sites, predominantly at the SGK1 sites T568 and S751, and evoked AS160 binding to the steroid-induced 14-3-3 isoforms, β and ε. AS160 mutations at SGK1 phospho-sites blocked its selective interaction with 14-3-3β and ε and suppressed the ability of expressed AS160 to augment aldosterone action. These findings indicate that the Rab protein regulator, AS160, stabilizes ENaC in a regulated intracellular compartment under basal conditions, and that aldosterone/SGK1-dependent AS160 phosphorylation permits ENaC forward trafficking to the apical membrane to augment Na absorption.
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Ducommun, Serge, Hong Yu Wang, Kei Sakamoto, Carol MacKintosh, and Shuai Chen. "Thr649Ala-AS160 knock-in mutation does not impair contraction/AICAR-induced glucose transport in mouse muscle." American Journal of Physiology-Endocrinology and Metabolism 302, no. 9 (May 1, 2012): E1036—E1043. http://dx.doi.org/10.1152/ajpendo.00379.2011.

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AS160 and its closely related protein TBC1D1 have emerged as key mediators for both insulin- and contraction-stimulated muscle glucose uptake through regulating GLUT4 trafficking. Insulin increases AS160 phosphorylation at multiple Akt/PKB consensus sites, including Thr649, and promotes its binding to 14-3-3 proteins through phospho-Thr649. We recently provided genetic evidence that AS160-Thr649 phosphorylation/14-3-3 binding plays a key role in mediating insulin-stimulated glucose uptake in muscle. Contraction has also been proposed to increase phosphorylation of AS160 and TBC1D1 via AMPK, which could be detected by a generic phospho-Akt substrate (PAS) antibody. Here, analysis of AS160 immunoprecipitates from muscle extracts with site-specific phospho-antibodies revealed that contraction and AICAR caused no increase but rather a slight decrease in phosphorylation of the major PAS recognition site AS160-Thr649. In line with this, contraction failed to enhance 14-3-3 binding to AS160. Consistent with previous reports, we also observed that in situ contraction stimulated the signal intensity of PAS antibody immunoreactive protein of ∼150–160 kDa in muscle extracts. Using a TBC1D1 deletion mutant mouse, we showed that TBC1D1 protein accounted for the majority of the PAS antibody immunoreactive signals of ∼150–160 kDa in extracts of contracted muscles. Consistent with the proposed role of AS160-Thr649 phosphorylation/14-3-3 binding in mediating glucose uptake, AS160-Thr649Ala knock-in mice displayed normal glucose uptake upon contraction and AICAR in isolated muscles. We conclude that the previously reported PAS antibody immunoreactive band ∼150–160 kDa, which were increased upon contraction, does not represent AS160 but TBC1D1, and that AS160-Thr649Ala substitution impairs insulin- but neither contraction- nor AICAR-stimulated glucose uptake in mouse skeletal muscle.
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Dreyer, Hans C., Micah J. Drummond, Erin L. Glynn, Satoshi Fujita, David L. Chinkes, Elena Volpi, and Blake B. Rasmussen. "Resistance exercise increases human skeletal muscle AS160/TBC1D4 phosphorylation in association with enhanced leg glucose uptake during postexercise recovery." Journal of Applied Physiology 105, no. 6 (December 2008): 1967–74. http://dx.doi.org/10.1152/japplphysiol.90562.2008.

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Akt substrate of 160 kDa (AS160/TBC1D4) is associated with insulin and contraction-mediated glucose uptake. Human skeletal muscle AS160 phosphorylation is increased during aerobic exercise but not immediately following resistance exercise. It is not known whether AS160 phosphorylation is altered during recovery from resistance exercise. Therefore, we hypothesized that muscle AS160/TBC1D4 phosphorylation and glucose uptake across the leg would be increased during recovery following resistance exercise. We studied 9 male subjects before, during, and for 2 h of postexercise recovery. We utilized femoral catheterizations and muscle biopsies in combination with indirect calorimetry and immunoblotting to determine whole body glucose and fat oxidation, leg glucose uptake, muscle AMPKα2 activity, and the phosphorylation of muscle Akt and AS160/TBC1D4. Glucose oxidation was reduced while fat oxidation increased (∼35%) during postexercise recovery ( P ≤ 0.05). Glucose uptake increased during exercise and postexercise recovery ( P ≤ 0.05). Akt phosphorylation was increased at 1 h and AMPKα2 activity increased at 2 h postexercise ( P ≤ 0.05). Phospho(Ser/Thr)-Akt substrate (PAS) phosphorylation (often used as a marker for AS160) was unchanged immediately postexercise and increased at 1 h ( P ≤ 0.05) and 2 h postexercise ( P = 0.07). The PAS antibody is not always specific for AS160/TBC1D4 and can detect proteins at a similar molecular weight. Therefore, we immunoprecipitated AS160/TBC1D4 and then blotted with the PAS antibody, which confirmed that PAS phosphorylation is occurring on AS160/TBC1D4. There was also a positive correlation between PAS phosphorylation and leg glucose uptake during recovery ( P < 0.05). We conclude that resistance exercise increases AS160/TBC1D4 phosphorylation in association with an increase in leg glucose uptake during postexercise recovery.
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Wang, Hong Yu, Serge Ducommun, Chao Quan, Bingxian Xie, Min Li, David H. Wasserman, Kei Sakamoto, Carol Mackintosh, and Shuai Chen. "AS160 deficiency causes whole-body insulin resistance via composite effects in multiple tissues." Biochemical Journal 449, no. 2 (December 14, 2012): 479–89. http://dx.doi.org/10.1042/bj20120702.

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AS160 (Akt substrate of 160 kDa) is a Rab GTPase-activating protein implicated in insulin control of GLUT4 (glucose transporter 4) trafficking. In humans, a truncation mutation (R363X) in one allele of AS160 decreased the expression of the protein and caused severe postprandial hyperinsulinaemia during puberty. To complement the limited studies possible in humans, we generated an AS160-knockout mouse. In wild-type mice, AS160 expression is relatively high in adipose tissue and soleus muscle, low in EDL (extensor digitorum longus) muscle and detectable in liver only after enrichment. Despite having lower blood glucose levels under both fasted and random-fed conditions, the AS160-knockout mice exhibited insulin resistance in both muscle and liver in a euglycaemic clamp study. Consistent with this paradoxical phenotype, basal glucose uptake was higher in AS160-knockout primary adipocytes and normal in isolated soleus muscle, but their insulin-stimulated glucose uptake and overall GLUT4 levels were markedly decreased. In contrast, insulin-stimulated glucose uptake and GLUT4 levels were normal in EDL muscle. The liver also contributes to the AS160-knockout phenotype via hepatic insulin resistance, elevated hepatic expression of phosphoenolpyruvate carboxykinase isoforms and pyruvate intolerance, which are indicative of increased gluconeogenesis. Overall, as well as its catalytic function, AS160 influences expression of other proteins, and its loss deregulates basal and insulin-regulated glucose homoeostasis, not only in tissues that normally express AS160, but also by influencing liver function.
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Howlett, Kirsten F., Alicia Mathews, Andrew Garnham, and Kei Sakamoto. "The effect of exercise and insulin on AS160 phosphorylation and 14-3-3 binding capacity in human skeletal muscle." American Journal of Physiology-Endocrinology and Metabolism 294, no. 2 (February 2008): E401—E407. http://dx.doi.org/10.1152/ajpendo.00542.2007.

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AS160 is an Akt substrate of 160 kDa implicated in the regulation of both insulin- and contraction-mediated GLUT4 translocation and glucose uptake. The effects of aerobic exercise and subsequent insulin stimulation on AS160 phosphorylation and the binding capacity of 14-3-3, a novel protein involved in the dissociation of AS160 from GLUT4 vesicles, in human skeletal muscle are unknown. Hyperinsulinemic-euglycemic clamps were performed on seven men at rest and immediately and 3 h after a single bout of cycling exercise. Skeletal muscle biopsies were taken before and after the clamps. The insulin sensitivity index calculated during the final 30 min of the clamp was 8.0 ± 0.8, 9.1 ± 0.5, and 9.2 ± 0.8 for the rest, postexercise, and 3-h postexercise trials, respectively. AS160 phosphorylation increased immediately after exercise and remained elevated 3 h after exercise. In contrast, the 14-3-3 binding capacity of AS160 and phosphorylation of Akt and AMP-activated protein kinase were only increased immediately after exercise. Insulin increased AS160 phosphorylation and 14-3-3 binding capacity and insulin receptor substrate-1 and Akt phosphorylation, but the response to insulin was not enhanced by prior exercise. In conclusion, the 14-3-3 binding capacity of AS160 is increased immediately after acute exercise in human skeletal muscle, but this is not maintained 3 h after exercise completion despite sustained AS160 phosphorylation. Insulin increases AS160 phosphorylation and 14-3-3 binding capacity, but prior exercise does not appear to enhance the response to insulin.
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Dissertations / Theses on the topic "AS160"

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Purificação, Thais Almeida 1980. "Participação das proteínas AS160 e Rab27A na secreção de insulina de ratos controles e insulino-resistentes por dexametasona." [s.n.], 2012. http://repositorio.unicamp.br/jspui/handle/REPOSIP/313950.

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Orientadores: Antonio Carlos Boschiero, Alex Rafacho
Dissertação (mestrado) - Universidade Estadual de Campinas, Instituto de Biologia
Made available in DSpace on 2018-08-20T10:53:44Z (GMT). No. of bitstreams: 1 Purificacao_ThaisAlmeida_M.pdf: 1255549 bytes, checksum: 5142cacf6ca932aa0dd1a86b9eef5074 (MD5) Previous issue date: 2012
Resumo: Administração de glicocorticóides em roedores e humanos aumenta a resistência à insulina (RI). A RI, provocada por dexametasona, leva a hiperinsulinemia por aumento da secreção do hormônio pelas ilhotas pancreáticas. Recentemente, demonstrou-se que a AS160, uma GAP (proteína ativadora de GTPase), participa no tráfego de vesículas em diferentes tipos celulares que, por sua vez, pode ser alterado por dexametasona. Neste trabalho, avaliamos possível participação da AS160 na secreção de insulina em ilhotas de ratos RI por dexametasona, para isto foram avaliadas proteínas envolvidas no processo de secreção; pAS160, Akt e AMPK. Ratos Wistar adultos foram tratados com o glicocorticóide (DEX) com 1mg/kg (ip) de peso corporal, ou salina (CTL), durante 5 dias. Ao final do período de tratamento, os ratos foram submetidos a um Teste de Tolerância à Glicose intraperitoneal (ipGTT) e, após sacrifício, amostras de sangue foram coletadas para dosagem de insulina. As ilhotas pancreáticas foram isoladas por digestão do pâncreas com colagenase. As proteínas insulares foram avaliadas por Western Blot e os genes por RCP-TR. A insulina, contida nas amostras de sangue e nas incubações de ilhotas, foi medida por radioimunoensaio (RIA). A razão pAS160/AS160 foi aumentada nas ilhotas DEX (P<0,05). Nestas ilhotas, resultados semelhantes foram observados para a razão pAkt/Akt (P<0,05). O tratamento com DEX também aumentou a expressão gênica e protéica da Rab27A (P<0,05), contudo, reduziu significativamente sua associação com a AS160 (P<0,05). A associação entre essas duas proteínas foi observada pela primeira vez nas ilhotas neste trabalho. O tratamento com DEX também reduziu as expressões gênica e protéica bem como a fosforilação da AMPK. A secreção de insulina foi maior nas ilhotas DEX comparado à CTL e, em ambas, a secreção foi diminuída pela wortmanina (inibidor da PI3K). Ilhotas de ratos CTL e DEX, tratados com anti-sense anti-AS160, tiveram o conteúdo protéico da AS160 reduzido em ± 80%, comparado ao CTL (P<0,05). Nas ilhotas de ratos CTL knockdown, a secreção de insulina foi maior que nos CTL e, nas ilhotas dos DEX knockdown a secreção foi semelhante às DEX. Concluindo, o aumento da secreção de insulina em ilhotas de ratos RI por dexametasona envolve a participação da AS160 e, essa potencialização parece ser mediada pela via PI3K/Akt. Esse aumento de secreção parece também ser diretamente proporcional ao aumento da dissociação entre a Rab27A e a AS160
Abstract: It is well known that glucocorticoids induce insulin resistance (IR). It is also known that dexamethasone-induced IR is linked to increased levels of plasma insulin due to higher insulin secretion by pancreatic islets. Recent findings show that the Rab-GTPase AS160 plays a role in the traffic of vesicles in different cells type that, in turn, may be affected by dexamethasone. Here, we evaluated the participation of AS160 in the insulin secretion in islets from dexamethasone treated rats. Adult rats were treated with dexamethasone (DEX) with 1.0 mg/kg, body weight (ip) or saline (CTL) for 5 consecutive days. Insulin resistance was evaluated by intraperitoneal Glucose Tolerance Test (ipGTT). After, the rats were sacrificed and the islets isolated by the digestion of their pancreases with collagenase. Protein was measured by Western- Blot, and insulin by RIA. AS160 expression, phosphorylation, and the pAS160/AS160 ratio were increased in DEX islets (P<0.05). Similar results were observed for Akt (P<0.05). Dexamethasone also increased Rab27a protein and gene expression but significantly reduced its association with AS160. The association between these two proteins was observed in pancreatic islets for the first time in this work. AMPK gene and protein expression as well as phosphorylation were reduced by Dexamethasone (P<0.05). The insulin secretion was higher in DEX compared with CTL islets (P<0.05). Both secretions were reduced by wortmanin. Islets from CTL and DEX rats, treated with anti-sense anti-AS160, showed ± 80% reduction on its expression. The CTL knockdown islets secreted more insulin than CTL and the DEX knockdown secreted similar amount of insulin than DEX islets. In conclusion, these results indicated that AS160 participates in the increased insulin secretion in islets from DEX rats, and this effect seems to be dependent on the activation of the PI3K/Akt pathway. The increase in insulin secretion also depends on the dissociation between Rab27a and AS160
Mestrado
Fisiologia
Mestre em Biologia Funcional e Molecular
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Singh, Indu, and indu singh@rmit edu au. "The influence of antioxidants on thrombotic risk factors in healthy population." RMIT University. Medical Sciences, 2008. http://adt.lib.rmit.edu.au/adt/public/adt-VIT20081205.121719.

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Oxidative damage has been suggested to play a key role in the pathogenesis of atherosclerosis and other cardiovascular disease. Increased free radical production induced by oxidative stress can oxidise low density lipoproteins, activates platelets, induces endothelial dysfunction and disturbs glucose transport by consuming endogenous antioxidants. Using a combination, of in vitro and in vivo experimental models, the primary aims of the studies undertaken for this thesis were to examine whether different antioxidants could negate risk factors leading to thrombosis, atherosclerosis and other cardiovascular diseases. The studies utilised the mechanisms involved in platelet activity and glucose uptake by skeletal muscle myotubes. The first study determined if olive leaf extract would attenuate platelet activity in healthy human subjects. Blood samples (n=11) were treated with five different concentrations of extract of Olea europaea L. leaves ranging from 5.4£gg/mL to 54£gg/mL. A significant reduction in platelet activity (pless than0.001) and ATP release from platelets (p=0.02) was observed with 54£gg/mL olive leaf extract. The next crossover study compared the effect of exercise and antioxidant supplementation on platelet function between trained and sedentary individuals. An acute bout of 1 hour exercise (sub maximal cycling at 70% of VO2max) was used to induce oxidative stress in 8 trained and 8 sedentary male subjects, before and after one week supplementation with 236 mg/day of cocoa polyphenols. Baseline platelet count and ATP release increased significantly (pless than0.05) after exercise in all subjects. Baseline platelet numbers in the trained were higher than in the sedentary (235¡Ó37 vs. 208¡Ó34 x109/L, p less than 0.05), whereas platelet activation in trained subjects was lower than sedentary individuals (51¡Ó6 vs. 59¡Ó5%, p less than0.05). Seven days of cocoa polyphenol supplementation did not change platelet activity compared to the placebo group. The third study determined the effect of 5 weeks of either 100mg/day £^-Tocopherol (n=14), 200mg/d £^-Tocopherol (n=13) or placebo (n=12) on platelet function, lipid profile and the inflammatory marker C-reactive protein. Blood £^-tocopherol concentrations increased significantly (pless than0.05) relative to dose. Both doses attenuated platelet activation (pless than0.05). LDL cholesterol, platelet aggregation and mean platelet volume were decreased by 100mg/d £^-tocopherol (all pless than0.05). The final study determined the effect of glucose oxidase induced oxidative stress and £^-tocopherol treatment on glucose transport and insulin signalling in cultured rat L6 muscle cells. One hour treatment with 100mU/mL glucose oxidase significantly decreased glucose uptake both with and without 100nM insulin stimulation (pless than0.05). Pre-treatment with 100ƒÝM and 200ƒÝM £^-tocopherol partially protected cells from the effect of glucose oxidase, whereas 200ƒÝM £^-tocopherol restored both basal and insulin stimulated glucose transport to control levels. Glucose oxidase-induced oxidative stress did not impair basal or insulin stimulated phosphorylation of Akt or AS160, but 200ƒÝM £^-tocopherol improved insulin-stimulated phosphorylation of these proteins. In summary, the results from the studies undertaken for this thesis provide evidence that antioxidant supplementation maintains normal platelet function, exerts a positive effect on blood lipid profile and improves glucose uptake in normal healthy asymptomatic population as well as under conditions of induced oxidative stress. Antioxidants including foods rich in cocoa, olive and gamma tocopherol have the potential to combat oxidative stress induced risk factors leading to cardiovascular diseases.
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Bruss, Matthew D. "Effects of insulin and contraction on AS160 phosphorylation in isolated rat epitrochlearis muscle." 2004. http://catalog.hathitrust.org/api/volumes/oclc/56131097.html.

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Thesis (M.S.)--University of Wisconsin--Madison, 2004.
Typescript. eContent provider-neutral record in process. Description based on print version record. Includes bibliographical references (leaves 36-38).
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Kramer, Henning Fritz. "The role of the Akt Substrate of 160 kDa (AS160) on skeletal muscle glucose uptake." 2007. http://www.etda.libraries.psu.edu/theses/approved/WorldWideIndex/ETD-1825/index.html.

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Kleinert, Maximilian. "An amino acid mixture enhances insulin-stimulated glucose uptake in isolated epitrochlearis muscle." Thesis, 2010. http://hdl.handle.net/2152/ETD-UT-2010-08-1809.

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Amino acids are important modulators of skeletal muscle metabolism, but their impact on glucose uptake by skeletal muscle remains unclear. To address the effect of an amino acid (AA) mixture consisting predominately of isoleucine on glucose uptake we first conducted a dose-response experiment, investigating how different concentrations of the AA mixture affect glucose uptake by isolated rat epitrochlearis muscle. In a subsequent experiment we examined how the AA mixture affects insulin-stimulated glucose uptake by isolated rat epitrochlearis muscle. It was found that the AA mixture with as little as 0.5 mM Ile increases [H3]2-deoxy-D-glucose (2-DG) uptake by 76% compared to basal glucose uptake. The AA mixtures with 1, 2 or 4 mM Ile provided no significant additional effect. Next we combined the AA mixture consisting of 2 mM Ile, 0.012 mM Cys, 0.006 mM Val and 0.014 mM Leu with physiological levels (75 μU/ml, sINS) and maximally-stimulating levels (2 mU/ml, mINS) of insulin. The AA mixture only, sINS and mINS significantly increased 2-DG uptake compared to basal by 63, 79 and 298%, respectively. When the AA mixture was combined with sINS and mINS 2-DG uptake was further increased significantly by 26 and 14%, respectively. Western blotting analysis revealed that compared to basal the AA mixture increased AS160 phosphorylation, while phosphorylation of Akt and mTOR did not change. Combining the AA mixture with sINS resulted in no additional phosphorylation compared to sINS alone. Interestingly, addition of the AA mixture to mINS resulted in increased phosphorylation of mTOR, Akt and AS160 compared to mINS alone. Our results suggest that certain AAs (1) increase glucose uptake in the absence of insulin and (2) augment insulin-stimulated glucose uptake in an additive manner. These effects on glucose uptake appear to be mediated via a molecular pathway that is partially independent from the canonical insulin signaling cascade.
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盧建智. "The study on the grinding of P/M high speed steel ASP60." Thesis, 1997. http://ndltd.ncl.edu.tw/handle/15661987931448997341.

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Book chapters on the topic "AS160"

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Tsui, David T., Rebecca A. Clewell, J. Eric Eldridge, and David R. Mattie. "Perchlorate Analysis with the AS16 Separation Column." In Perchlorate in the Environment, 59–80. Boston, MA: Springer US, 2000. http://dx.doi.org/10.1007/978-1-4615-4303-9_7.

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"Emergency Department Treatment." In Manual of Clinical Psychopharmacology. American Psychiatric Publishing, 2015. http://dx.doi.org/10.1176/appi.books.9781615370047.as10.

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Rosenbaum, Jerrold, and Dawn Ionescu. "Fluoxetine." In The American Psychiatric Association Publishing Textbook of Psychopharmacology. American Psychiatric Association Publishing, 2017. http://dx.doi.org/10.1176/appi.books.9781615371624.as10.

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Blier, Pierre. "Vortioxetine." In The American Psychiatric Association Publishing Textbook of Psychopharmacology. American Psychiatric Association Publishing, 2017. http://dx.doi.org/10.1176/appi.books.9781615371624.as16.

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Haroon, Ebrahim, Giuseppe Pagnoni, Christine Heim, Gregory Berns, and Helen Mayberg. "Brain Imaging in Psychopharmacology." In The American Psychiatric Publishing Textbook of Psychopharmacology. American Psychiatric Publishing, 2009. http://dx.doi.org/10.1176/appi.books.9781585623860.as10.

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Aboujaoude, Elias, and Lorrin Koran. "Fluvoxamine." In The American Psychiatric Publishing Textbook of Psychopharmacology. American Psychiatric Publishing, 2009. http://dx.doi.org/10.1176/appi.books.9781585623860.as16.

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Reite, Martin. "Treatment of Insomnia." In The American Psychiatric Publishing Textbook of Psychopharmacology. American Psychiatric Publishing, 2009. http://dx.doi.org/10.1176/appi.books.9781585623860.as60.

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"Emergency Department Treatment." In Schatzberg’s Manual of Psychopharmacology. American Psychiatric Association Publishing, 2019. http://dx.doi.org/10.1176/appi.books.9781615372300.as10.

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"Emergency Department Treatment." In Schatzberg’s Manual of Psychopharmacology. American Psychiatric Association Publishing, 2019. http://dx.doi.org/10.1176/appi.books.9781615372997.as10.

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Languet, Hubert. "Hubert Languet to Sidney, Vienna, 15 January 1574 (AS10)." In The Correspondence of Sir Philip Sidney, Vol. 1, edited by Roger Kuin, 86–89. Oxford University Press, 2012. http://dx.doi.org/10.1093/oseo/instance.00027057.

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Conference papers on the topic "AS160"

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Binsch, C., D. Barbosa, K. Jeruschke, J. Weiß, M. Hubert, G. Hansen, SM Hodge, et al. "Absence of TBC1D4/AS160 impairs cardiac substrate metabolism and increases ischemia/reperfusion-induced myocardial damage." In Diabetes Kongress 2019 – 54. Jahrestagung der DDG. Georg Thieme Verlag KG, 2019. http://dx.doi.org/10.1055/s-0039-1688288.

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Binsch, C., D. Barbosa, K. Jeruschke, J. Weiß, M. Hubert, G. Hansen, S. Gorressen, et al. "Deletion von TBC1D4/AS160 erhöht den Myokardschaden nach Ischämie/Reperfusion und verschlechtert den kardialen Substratmetabolismus." In Diabetes Kongress 2018 – 53. Jahrestagung der DDG. Georg Thieme Verlag KG, 2018. http://dx.doi.org/10.1055/s-0038-1641777.

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"Session AS16: Presented at Asilomar 2016." In 2017 51st Asilomar Conference on Signals, Systems, and Computers. IEEE, 2017. http://dx.doi.org/10.1109/acssc.2017.8335728.

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Yang-Hartwich, Yang. "Abstract AS16: Ovulation and extraovarian origin of ovarian cancer." In Abstracts: 10th Biennial Ovarian Cancer Research Symposium; September 8-9, 2014; Seattle, WA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1557-3265.ovcasymp14-as16.

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Iovu, Maria A., Mihail S. Iovu, Diana V. Harea, Eduard P. Colomeico, and Valeriu G. Ciorba. "Light induced phenomena in amorphous As100-xSx and As40Se60:Sn thin films." In SPIE Proceedings, edited by Ovidiu Iancu, Adrian Manea, and Paul Schiopu. SPIE, 2007. http://dx.doi.org/10.1117/12.741870.

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Tworoger, Shelley S., Elizabeth M. Poole, Alan A. Arslan, Lesley M. Butler, Victoria Kirsh, James V. Lacey, I.-Min Lee, et al. "Abstract AS10: Ovarian cancer risk factor associations by tumor aggressiveness in the ovarian cancer cohort consortium (OC3)." In Abstracts: 10th Biennial Ovarian Cancer Research Symposium; September 8-9, 2014; Seattle, WA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1557-3265.ovcasymp14-as10.

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