PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 33713326-6 2021 High glucose induced the activation of the phosphorylated protein kinase B (pAkt)/GSK-3beta signaling pathway and a significant increase in the expression of beta-site beta APP cleaving enzyme (BACE1), presenilin1 (PS1) and Abeta42. Glucose 5-12 protein tyrosine kinase 2 beta Homo sapiens 58-74 31752432-7 2019 We observed that siRNA silencing of the glucose-regulated protein (GRP78) receptor and pharmacological inhibitors of mitogen-activated kinase (MAP3/1/ERK1/2), Janus kinase (STAT3) and protein kinase B (AKT) blocked the ability of vaspin cell proliferation and enhanced caspase-3/7 activities. Glucose 40-47 protein tyrosine kinase 2 beta Homo sapiens 184-200 33716662-2 2021 Available studies pointed to a network in which the activation of the nutrient-sensing (glucose, fatty acid, and amino acid) systems would result in AMP-activated protein kinase (AMPK) inhibition and activation of protein kinase B (Akt) and mechanistic target of rapamycin (mTOR). Glucose 88-95 protein tyrosine kinase 2 beta Homo sapiens 214-230 33382998-5 2021 While insulin-activated IRS/PI3K/PKB pathway cascades are primarily known to reduce glucose production, it was recently discovered to increase the Hh signaling pathway"s stability, thereby activating the PI3K/PKB/mammalian target of rapamycin complex 2 (mTORC2) signaling pathway. Glucose 84-91 protein tyrosine kinase 2 beta Homo sapiens 33-36 32878322-3 2020 Targeting 786-O cells by SH-859 inhibited cell growth and affected the protein kinase B/mechanistic target of rapamycin 1 pathway, which in turn downregulated the expression of glycolytic enzymes, including lactate dehydrogenase A and glucose transporter-1, as well as other signaling proteins. Glucose 235-242 protein tyrosine kinase 2 beta Homo sapiens 71-87 30150922-1 2018 Background: Augmenting glucose utilization in skeletal muscle via the phosphatidylinositol-3 kinase (PI3 kinase)/protein kinase B (Akt) pathway or the adenosine monophosphate (AMP)-activated protein kinase (AMPK) pathway is necessary to regulate hyperglycemia in patients with type 2 diabetes mellitus. Glucose 23-30 protein tyrosine kinase 2 beta Homo sapiens 113-129 30315968-3 2018 Indeed, prominent pathways involved in glucose metabolism such as phosphatidylinositol 3-kinase/ protein kinase B (PI3-K/AKT) and 5" AMP-activated protein kinase (AMPK) are impaired in an insulin resistant state. Glucose 39-46 protein tyrosine kinase 2 beta Homo sapiens 97-113 29484683-3 2018 Protein kinase B (AKT) plays an important role in overall skeletal muscle health and glucose uptake into the muscle. Glucose 85-92 protein tyrosine kinase 2 beta Homo sapiens 0-16 25158671-10 2015 Silencing Nox4 significantly normalized the levels of reactive oxygen species in glucose-treated cells; 20 mM glucose obviously upregulated Nox4, PTEN, phosphor-PTEN, and Bax levels, but significantly reduced integrin-linked kinase (ILK) activity, Bcl-2 (B cell lymphoma 2) expression, and protein kinase B (Akt) phosphorylation at serine 473. Glucose 81-88 protein tyrosine kinase 2 beta Homo sapiens 290-306 25158671-10 2015 Silencing Nox4 significantly normalized the levels of reactive oxygen species in glucose-treated cells; 20 mM glucose obviously upregulated Nox4, PTEN, phosphor-PTEN, and Bax levels, but significantly reduced integrin-linked kinase (ILK) activity, Bcl-2 (B cell lymphoma 2) expression, and protein kinase B (Akt) phosphorylation at serine 473. Glucose 110-117 protein tyrosine kinase 2 beta Homo sapiens 290-306 23880101-1 2013 The phosphatidylinositol 3 kinase/protein kinase B (PI3K/Akt) pathway mediates the high-glucose-induced lipid accumulation in the renal tubular cells in diabetes. Glucose 88-95 protein tyrosine kinase 2 beta Homo sapiens 34-50 22512570-1 2013 Protein kinase B (PKB, also known as Akt) plays a critical role in the multiple cellular processes including glucose metabolism, cell growth, survival, apoptosis, transcription, and cell migration. Glucose 109-116 protein tyrosine kinase 2 beta Homo sapiens 0-16 23578643-2 2013 Our results demonstrated that high glucose-induced oxidative stress in HUVECs was mainly mediated through activation of reactive oxygen species (ROS), Jun N-kinase 2/3 (JNK2/3) and plasma interleukin-8 (IL-8), and inactivation of phosphorylated protein kinase B (P-Akt). Glucose 35-42 protein tyrosine kinase 2 beta Homo sapiens 245-261 22512570-1 2013 Protein kinase B (PKB, also known as Akt) plays a critical role in the multiple cellular processes including glucose metabolism, cell growth, survival, apoptosis, transcription, and cell migration. Glucose 109-116 protein tyrosine kinase 2 beta Homo sapiens 18-21 18669636-0 2008 Use of Akt inhibitor and a drug-resistant mutant validates a critical role for protein kinase B/Akt in the insulin-dependent regulation of glucose and system A amino acid uptake. Glucose 139-146 protein tyrosine kinase 2 beta Homo sapiens 79-95 23514176-4 2013 In many cell systems, mTORC1 couples PI3K (phosphoinositide 3-kinase) and PKB (protein kinase B), also known as Akt, with the control of glucose uptake and glycolysis. Glucose 137-144 protein tyrosine kinase 2 beta Homo sapiens 74-77 23514176-4 2013 In many cell systems, mTORC1 couples PI3K (phosphoinositide 3-kinase) and PKB (protein kinase B), also known as Akt, with the control of glucose uptake and glycolysis. Glucose 137-144 protein tyrosine kinase 2 beta Homo sapiens 79-95 23333242-6 2013 C1P-stimulated glucose uptake was blocked by selective inhibitors of phosphatidylinositol 3-kinase (PI3K) or Akt, also known as protein kinase B (PKB), and by specific siRNAs to silence the genes encoding for these kinases. Glucose 15-22 protein tyrosine kinase 2 beta Homo sapiens 128-144 23333242-6 2013 C1P-stimulated glucose uptake was blocked by selective inhibitors of phosphatidylinositol 3-kinase (PI3K) or Akt, also known as protein kinase B (PKB), and by specific siRNAs to silence the genes encoding for these kinases. Glucose 15-22 protein tyrosine kinase 2 beta Homo sapiens 146-149 22891069-6 2012 Initial research described a critical role for PI3K signaling through Akt (also called protein kinase B) for the increased glucose uptake and glycolysis that accompanies T cell activation. Glucose 123-130 protein tyrosine kinase 2 beta Homo sapiens 87-103 21602475-6 2011 The stimulation of glucose uptake by AMPK activators and insulin correlated with AMPK and protein kinase B (PKB/Akt) activation, respectively. Glucose 19-26 protein tyrosine kinase 2 beta Homo sapiens 90-106 19639221-5 2009 Since PKB is instrumental in mediating the effects of insulin on glucose transport, glycogen synthesis and gluconeogenesis, it is reasonable to suggest that activation of this pathway by BMOV serves as a mechanism for its insulin-like effects. Glucose 65-72 protein tyrosine kinase 2 beta Homo sapiens 6-9 18669636-1 2008 Protein kinase B (PKB)/Akt has been strongly implicated in the insulin-dependent stimulation of GLUT4 translocation and glucose transport in skeletal muscle and fat cells. Glucose 120-127 protein tyrosine kinase 2 beta Homo sapiens 0-16 17570343-3 2007 As shown recently, the stimulating effect of protein kinase B on the glucose carrier GLUT4 involves the mammalian phosphatidylinositol-3-phosphate-5-kinase PIKfyve (PIP5K3). Glucose 69-76 protein tyrosine kinase 2 beta Homo sapiens 45-61 17095927-5 2006 Protein kinase B/Akt can both activate protein synthesis and decrease protein breakdown, thus leading to hypertrophy, and AMP-activated protein kinase can increase mitochondrial protein, glucose transport, and a number of other factors that result in an endurance phenotype. Glucose 187-194 protein tyrosine kinase 2 beta Homo sapiens 0-16 17311546-7 2007 These pathways are ultimately linked to protein kinase B (Akt) and the insulin signaling pathways that determine the initial onset of glucose intolerance and the subsequent course to apoptotic cell injury. Glucose 134-141 protein tyrosine kinase 2 beta Homo sapiens 40-56 16489105-0 2006 AMPK activation restores the stimulation of glucose uptake in an in vitro model of insulin-resistant cardiomyocytes via the activation of protein kinase B. Glucose 44-51 protein tyrosine kinase 2 beta Homo sapiens 138-154 16489105-6 2006 Stimulation of glucose uptake by insulin or biguanides was correlated to protein kinase B (PKB) or AMPK activation, respectively, and were additive. Glucose 15-22 protein tyrosine kinase 2 beta Homo sapiens 73-89 16489105-6 2006 Stimulation of glucose uptake by insulin or biguanides was correlated to protein kinase B (PKB) or AMPK activation, respectively, and were additive. Glucose 15-22 protein tyrosine kinase 2 beta Homo sapiens 91-94 16611685-10 2006 The siRNA-mediated down-regulation of ILK expression inhibited the elevation of PKB/Akt phosphorylation induced by high glucose treatment. Glucose 120-127 protein tyrosine kinase 2 beta Homo sapiens 80-83 16489105-10 2006 We concluded that AMPK activators, like biguanides and oligomycin, are able to restore glucose uptake stimulation, in the absence of insulin, in insulin-resistant cardiomyocytes via the additive activation of AMPK and PKB. Glucose 87-94 protein tyrosine kinase 2 beta Homo sapiens 218-221 16193290-3 2005 The present study was designed to elucidate the role of protein kinase B (Akt/PKB) in glucose-induced fibronectin mRNA expression and protein production in vascular endothelial cells. Glucose 86-93 protein tyrosine kinase 2 beta Homo sapiens 56-72 16049004-0 2005 Glucose uptake via glucose transporter 3 by human platelets is regulated by protein kinase B. Glucose 0-7 protein tyrosine kinase 2 beta Homo sapiens 76-92 16049004-1 2005 In insulin-responsive tissues, insulin is a potent activator of protein kinase B (PKB)-mediated glucose uptake through the facilitative glucose transporter GLUT4. Glucose 96-103 protein tyrosine kinase 2 beta Homo sapiens 64-80 16049004-1 2005 In insulin-responsive tissues, insulin is a potent activator of protein kinase B (PKB)-mediated glucose uptake through the facilitative glucose transporter GLUT4. Glucose 96-103 protein tyrosine kinase 2 beta Homo sapiens 82-85 16049004-3 2005 Here we report the PKB-mediated glucose uptake by platelets by agents that do (thrombin) or do not (insulin) induce alpha-granule translocation to the plasma membrane. Glucose 32-39 protein tyrosine kinase 2 beta Homo sapiens 19-22 16049004-5 2005 Inhibition of PKB by the pharmacological inhibitor ML-9 decreases thrombin-induced alpha-granule release and thrombin- and insulin-induced glucose uptake. Glucose 139-146 protein tyrosine kinase 2 beta Homo sapiens 14-17 16049004-8 2005 We conclude that in platelets glucose transport through GLUT3 is regulated by changes in surface expression and affinity modulation, which are both under control of PKB. Glucose 30-37 protein tyrosine kinase 2 beta Homo sapiens 165-168 15504741-1 2004 Although a number of studies and approaches have indicated that activation of the Ser/Thr kinase called Akt/protein kinase B is critical for the insulin-stimulated increase of glucose uptake in adipocytes, other studies have indicated that this enzyme may play an ancillary role. Glucose 176-183 protein tyrosine kinase 2 beta Homo sapiens 108-124 15774472-8 2005 419, 101-109), long-chain saturated FFAs inhibited insulin stimulation of Akt/protein kinase B, a central regulator of glucose uptake and anabolic metabolism. Glucose 119-126 protein tyrosine kinase 2 beta Homo sapiens 78-94 15787603-0 2005 Role of protein kinase B in insulin-regulated glucose uptake. Glucose 46-53 protein tyrosine kinase 2 beta Homo sapiens 8-24 15787603-1 2005 The activation of protein kinase B (or Akt) plays a central role in the stimulation of glucose uptake by insulin. Glucose 87-94 protein tyrosine kinase 2 beta Homo sapiens 18-34 15573143-4 2004 As a result, they promote an increase in protein tyrosine phosphorylation of several key components of the insulin signaling pathway, leading to the upregulation of phosphatidylinositol 3-kinase and protein kinase B, two enzymes involved in mediating GLUT-4 trans location and glucose transport. Glucose 277-284 protein tyrosine kinase 2 beta Homo sapiens 199-215 15220355-1 2004 The sphingolipid ceramide negatively regulates insulin action by inhibiting Akt/protein kinase B (PKB), a serine/threonine kinase that is a central regulator of glucose uptake and anabolic metabolism. Glucose 161-168 protein tyrosine kinase 2 beta Homo sapiens 80-96 15166230-1 2004 Insulin stimulates glucose uptake into muscle and fat cells by translocating glucose transporter 4 (GLUT4) to the cell surface, with input from phosphatidylinositol (PI) 3-kinase and its downstream effector Akt/protein kinase B. Glucose 19-26 protein tyrosine kinase 2 beta Homo sapiens 211-227 12091379-5 2002 When antisense RNA expression vector for 5"-AMP-activated protein kinase or protein kinase B/Akt was transfected into HepG2 cells, the induction of tolerance to glucose was greatly inhibited, indicating that the tolerance was dependent on 5"-AMP-activated protein kinase and protein kinase B/Akt. Glucose 161-168 protein tyrosine kinase 2 beta Homo sapiens 76-92 15094071-4 2004 IGF1 acts in an autocrine and/or paracrine manner to promote glucose utilization, using phosphatidylinositol 3 kinase (PI3K)/Akt, also known as protein kinase B (PKB)/glycogen synthase kinase 3beta (GSK3beta) pathways similar to insulin signaling in peripheral tissues. Glucose 61-68 protein tyrosine kinase 2 beta Homo sapiens 144-160 18370676-2 2004 Atypical protein kinase C and protein kinase B, operating downstream of phosphatidylinositol 3-kinase, mediate insulin effects on glucose transport, but their importance in these syndromes is poorly understood. Glucose 130-137 protein tyrosine kinase 2 beta Homo sapiens 30-46 12393870-5 2002 However, most strikingly, adenoviral mediated expression of a constitutively active PKB, but not a "kinase-dead" PKB variant, essentially prevented FFA-induced beta-cell apoptosis under all glucose/insulin-like growth factor 1 conditions. Glucose 190-197 protein tyrosine kinase 2 beta Homo sapiens 84-87 12091379-5 2002 When antisense RNA expression vector for 5"-AMP-activated protein kinase or protein kinase B/Akt was transfected into HepG2 cells, the induction of tolerance to glucose was greatly inhibited, indicating that the tolerance was dependent on 5"-AMP-activated protein kinase and protein kinase B/Akt. Glucose 161-168 protein tyrosine kinase 2 beta Homo sapiens 275-291 11007796-0 2000 Glucose activates mitogen-activated protein kinase (extracellular signal-regulated kinase) through proline-rich tyrosine kinase-2 and the Glut1 glucose transporter. Glucose 0-7 protein tyrosine kinase 2 beta Homo sapiens 99-129 11274216-0 2001 Differential activation of protein kinase B and p70(S6)K by glucose and insulin-like growth factor 1 in pancreatic beta-cells (INS-1). Glucose 60-67 protein tyrosine kinase 2 beta Homo sapiens 27-43 11257494-0 2001 Protein kinase B (PKB/Akt)--a key regulator of glucose transport? Glucose 47-54 protein tyrosine kinase 2 beta Homo sapiens 0-16 11270673-7 2001 Expression of a membrane-targetted protein kinase B led to its constitutive activation and an increase in glucose transport that was not inhibited by ceramide. Glucose 106-113 protein tyrosine kinase 2 beta Homo sapiens 35-51 11270673-8 2001 CONCLUSIONS/INTERPRETATION: These findings suggest that a defect in protein kinase B recruitment underpins the ceramide-induced loss in insulin sensitivity of key cell responses such as glucose transport and glycogen synthesis in L6 cells. Glucose 186-193 protein tyrosine kinase 2 beta Homo sapiens 68-84 11007796-6 2000 Glucose stimulated the phosphorylation of tyrosine residues 402 and 881 in PYK2 and binding of PYK2 to Myc-Glut1. Glucose 0-7 protein tyrosine kinase 2 beta Homo sapiens 75-79 11007796-6 2000 Glucose stimulated the phosphorylation of tyrosine residues 402 and 881 in PYK2 and binding of PYK2 to Myc-Glut1. Glucose 0-7 protein tyrosine kinase 2 beta Homo sapiens 95-99 11007796-7 2000 Our findings suggest that: (a) glucose activates the GRB2/SOS/RAS/RAF/MEK1/ERK pathway by a mechanism that requires PYK2 and residues 463-468, IASGFR, in the Glut1 C terminus and (b) Glut1 serves as a sensor, transducer, and amplifier for glucose signaling to PYK2 and ERK. Glucose 31-38 protein tyrosine kinase 2 beta Homo sapiens 116-120 11007796-7 2000 Our findings suggest that: (a) glucose activates the GRB2/SOS/RAS/RAF/MEK1/ERK pathway by a mechanism that requires PYK2 and residues 463-468, IASGFR, in the Glut1 C terminus and (b) Glut1 serves as a sensor, transducer, and amplifier for glucose signaling to PYK2 and ERK. Glucose 31-38 protein tyrosine kinase 2 beta Homo sapiens 260-264 10542046-5 1999 In contrast, the nonesterified fatty acid palmitate inhibited insulin-induced signalling cascades not only at the level of IR and IRS-1 phosphorylation, but also at the level protein kinase B (PKB/Akt), which is thought to be directly involved in the insulin-induced translocation of GLUT4, and inhibited insulin-induced glucose uptake. Glucose 321-328 protein tyrosine kinase 2 beta Homo sapiens 193-196 10874027-1 2000 Protein kinase B (PKB) is a serine/threonine kinase that is activated by growth hormones and implicated in prevention of apoptosis, glycogen metabolism, and glucose uptake. Glucose 157-164 protein tyrosine kinase 2 beta Homo sapiens 0-16 10874027-1 2000 Protein kinase B (PKB) is a serine/threonine kinase that is activated by growth hormones and implicated in prevention of apoptosis, glycogen metabolism, and glucose uptake. Glucose 157-164 protein tyrosine kinase 2 beta Homo sapiens 18-21 11193829-4 2000 Insulin, IGF-1, and GLP-1 induced distinctive time dependent, dose dependent, and glucose dependent phosphorylation of PKB/Akt. Glucose 82-89 protein tyrosine kinase 2 beta Homo sapiens 119-122 10208883-1 1999 The family of protein kinases called Akt, protein kinase B (PKB), or related to A and C kinase (RAC) have been implicated in numerous biological processes including adipocyte and muscle differentiation, glycogen synthesis, glucose uptake, apoptosis and cellular proliferation. Glucose 223-230 protein tyrosine kinase 2 beta Homo sapiens 42-58 10208883-1 1999 The family of protein kinases called Akt, protein kinase B (PKB), or related to A and C kinase (RAC) have been implicated in numerous biological processes including adipocyte and muscle differentiation, glycogen synthesis, glucose uptake, apoptosis and cellular proliferation. Glucose 223-230 protein tyrosine kinase 2 beta Homo sapiens 60-63 35330934-1 2022 The serine/threonine kinase Akt, also known as protein kinase B (PKB), is one of the key factors regulating glucose and lipid energy metabolism, and is the core focus of current research on diabetes and metabolic diseases. Glucose 108-115 protein tyrosine kinase 2 beta Homo sapiens 47-63 9497382-2 1998 Protein kinase B/Akt (PKB/Akt), a member of the PKA/PKC serine/threonine kinase family, functions downstream from phosphatidylinositol 3"-kinase (PI3K) in mediating effects of insulin on glucose transport and glycogen synthesis. Glucose 187-194 protein tyrosine kinase 2 beta Homo sapiens 0-29 9478990-0 1998 Potential role of protein kinase B in insulin-induced glucose transport, glycogen synthesis, and protein synthesis. Glucose 54-61 protein tyrosine kinase 2 beta Homo sapiens 18-34 35299066-2 2022 Besides providing nitrogen substrates and carbon framework for energy homeostasis and transamination, BCAA also function as signaling molecules in the regulation of glucose, lipid, and protein synthesis via protein kinase B and as a mechanistic target of the rapamycin (AKT-mTOR) signaling pathway that is important for muscle accretion. Glucose 165-172 protein tyrosine kinase 2 beta Homo sapiens 207-223 35330934-1 2022 The serine/threonine kinase Akt, also known as protein kinase B (PKB), is one of the key factors regulating glucose and lipid energy metabolism, and is the core focus of current research on diabetes and metabolic diseases. Glucose 108-115 protein tyrosine kinase 2 beta Homo sapiens 65-68