Academic literature on the topic 'Facilitative Glucose Transport Proteins'
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Journal articles on the topic "Facilitative Glucose Transport Proteins"
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Hoffman, Brenda B., and Fuad N. Ziyadeh. "Facilitative glucose transport proteins and sodium-glucose co-transporters in the kidney." Current Opinion in Nephrology and Hypertension 4, no. 5 (September 1995): 406–12. http://dx.doi.org/10.1097/00041552-199509000-00006.
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Liu, K., S. Zhao, B. Liu, B. Fan, C. Li, and M. Yu. "Assignment of solute carrier family 2 (facilitated glucose transporter), members <i>SLC2A2</i>, <i>SLC2A3</i>, <i>SLC2A5</i>, <i>SLC2A8</i> and <i>SLC2A12</i> to porcine chromosomes by somatic cell and radiation hybrid panel mapping (Brief report)." Archives Animal Breeding 50, no. 1 (October 10, 2007): 114–15. http://dx.doi.org/10.5194/aab-50-114-2007.
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Abstract. The transport of glucose plays an important role in cellular glucose homeostasis and metabolism [1]. Due to the hydrophilic character of glucose, the transport of glucose in and out of cells requires specific carrier proteins. The mammalian facilitative glucose transport family, which contains the energy-independent transporters (gene symbol SLC2A, protein symbol GLUT), catalyzes the entry of glucose into mammalian cells by facilitative diffusion down a concentration gradient. Thirteen members of mammalian GLUT family have been now characterized [1]. In swine, the chromosomal locations for the five genes (SLC2A2, SLC2A3, SLC2A5, SLC2A8 and SLC2A12) have not yet been determined. In this study, as the first step to better understand of the roles of these GLUTs in pigs which could subsequently be beneficial for pig production, we report the mapping of the five genes using both porcine somatic cell hybrid panel (INRA-SCHP) and radiation hybrid panel (IMpRH).
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Wood, I. Stuart, and Paul Trayhurn. "Glucose transporters (GLUT and SGLT): expanded families of sugar transport proteins." British Journal of Nutrition 89, no. 1 (January 2003): 3–9. http://dx.doi.org/10.1079/bjn2002763.
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The number of known glucose transporters has expanded considerably over the past 2 years. At least three, and up to six, Na+-dependent glucose transporters (SGLT1–SGLT6; gene name SLC5A) have been identified. Similarly, thirteen members of the family of facilitative sugar transporters (GLUT1–GLUT12 and HMIT; gene name SLC2A) are now recognised. These various transporters exhibit different substrate specificities, kinetic properties and tissue expression profiles. The number of distinct gene products, together with the presence of several different transporters in certain tissues and cells (for example, GLUT1, GLUT4, GLUT5, GLUT8, GLUT12 and HMIT in white adipose tissue), indicates that glucose delivery into cells is a process of considerable complexity.
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Waddell, I. D., A. G. Zomerschoe, M. W. Voice, and A. Burchell. "Cloning and expression of a hepatic microsomal glucose transport protein. Comparison with liver plasma-membrane glucose-transport protein GLUT 2." Biochemical Journal 286, no. 1 (August 15, 1992): 173–77. http://dx.doi.org/10.1042/bj2860173.
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Antibodies raised against a 52 kDa rat liver microsomal glucose-transport protein were used to screen a rat liver cDNA library. Six positive clones were isolated. Two clones were found to be identical with the liver plasma-membrane glucose-transport protein termed GLUT 2. The sequence of the four remaining clones indicates that they encode a unique microsomal facilitative glucose-transport protein which we have termed GLUT 7. Sequence analysis revealed that the largest GLUT 7 clone was 2161 bp in length and encodes a protein of 528 amino acids. The deduced amino acid sequence of GLUT 7 shows 68% identity with the deduced amino acid sequence of rat liver GLUT 2. The GLUT 7 sequence is six amino acids longer than rat liver GLUT 2, and the extra six amino acids at the C-terminal end contain a consensus motif for retention of membrane-spanning proteins in the endoplasmic reticulum. When the largest GLUT 7 clone was transfected into COS 7 cells the expressed protein was found in the endoplasmic reticulum and nuclear membrane, but not in the plasma membrane. Microsomes isolated from the transfected COS 7 cells demonstrated an increase in their microsomal glucose-transport capacity, demonstrating that the GLUT 7 clone encodes a functional endoplasmic-reticulum glucose-transport protein.
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Olson, Ann Louise, and Kenneth Humphries. "Recent advances in understanding glucose transport and glucose disposal." F1000Research 9 (June 24, 2020): 639. http://dx.doi.org/10.12688/f1000research.22237.1.
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Deficient glucose transport and glucose disposal are key pathologies leading to impaired glucose tolerance and risk of type 2 diabetes. The cloning and identification of the family of facilitative glucose transporters have helped to identify that underlying mechanisms behind impaired glucose disposal, particularly in muscle and adipose tissue. There is much more than just transporter protein concentration that is needed to regulate whole body glucose uptake and disposal. The purpose of this review is to discuss recent findings in whole body glucose disposal. We hypothesize that impaired glucose uptake and disposal is a consequence of mismatched energy input and energy output. Decreasing the former while increasing the latter is key to normalizing glucose homeostasis.
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Thorens, Bernard, and Mike Mueckler. "Glucose transporters in the 21st Century." American Journal of Physiology-Endocrinology and Metabolism 298, no. 2 (February 2010): E141—E145. http://dx.doi.org/10.1152/ajpendo.00712.2009.
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The ability to take up and metabolize glucose at the cellular level is a property shared by the vast majority of existing organisms. Most mammalian cells import glucose by a process of facilitative diffusion mediated by members of the Glut (SLC2A) family of membrane transport proteins. Fourteen Glut proteins are expressed in the human and they include transporters for substrates other than glucose, including fructose, myoinositol, and urate. The primary physiological substrates for at least half of the 14 Glut proteins are either uncertain or unknown. The well-established glucose transporter isoforms, Gluts 1–4, are known to have distinct regulatory and/or kinetic properties that reflect their specific roles in cellular and whole body glucose homeostasis. Separate review articles on many of the Glut proteins have recently appeared in this journal. Here, we provide a very brief summary of the known properties of the 14 Glut proteins and suggest some avenues of future investigation in this area.
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Vannucci, Susan J., Lisa B. Seaman, and Robert C. Vannucci. "Effects of Hypoxia-Ischemia on GLUT1 and GLUT3 Glucose Transporters in Immature Rat Brain." Journal of Cerebral Blood Flow & Metabolism 16, no. 1 (January 1996): 77–81. http://dx.doi.org/10.1097/00004647-199601000-00009.
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Cerebral hypoxia-ischemia produces major alterations in energy metabolism and glucose utilization in brain. The facilitative glucose transporter proteins mediate the transport of glucose across the blood–brain barrier (BBB) (55 kDa GLUT1) and into the neurons and glia (GLUT3 and 45 kDa GLUT1). Glucose uptake and utilization are low in the immature rat brain, as are the levels of the glucose transporter proteins. This study investigated the effect of cerebral hypoxia-ischemia in a model of unilateral brain damage on the expression of GLUT 1 and GLUT3 in the ipsilateral (damaged, hypoxic-ischemic) and contralateral (undamaged, hypoxic) hemispheres of perinatal rat brain. Early in the recovery period, both hemispheres exhibited increased expression of BBB GLUT1 and GLUT3, consistent with increased glucose transport and utilization. Further into recovery, BBB GLUT1 increased and neuronal GLUT3 decreased in the damaged hemisphere only, commensurate with neuronal loss.
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Lee, W. J., D. R. Peterson, E. J. Sukowski, and R. A. Hawkins. "Glucose transport by isolated plasma membranes of the bovine blood-brain barrier." American Journal of Physiology-Cell Physiology 272, no. 5 (May 1, 1997): C1552—C1557. http://dx.doi.org/10.1152/ajpcell.1997.272.5.c1552.
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Luminal and abluminal endothelial plasma membrane vesicles were isolated from bovine cerebral microvessels, the site of the blood-brain barrier. Glucose transport across each membrane was measured using a rapid-filtration technique. Glucose transport into luminal vesicles occurred by a stereospecific energy-independent transporter [Michaelis-Menten constant (K(m)) = 10.3 +/- 2.8 (SE) mM and maximal velocity (Vmax) = 8.6 +/- 2.0 nmol.mg protein(-1).min-1]. Kinetic analysis of abluminal vesicles also showed a transport system with characteristics similar to the luminal transporter (K(m) = 12.5 +/- 2.3 mM and Vmax = 10.0 +/- 1.0 nmol.mg protein-1.min-1). These functional, facilitative glucose transporters were symmetrically distributed between the luminal and abluminal membrane domains, providing a mechanism for glucose movement between blood and brain. The studies also revealed a Na-dependent transporter on the abluminal membrane with a higher affinity and lower capacity than the facilitative transporters (K(m) = 130 +/- 20 microM and Vmax = 1.59 +/- 0.44 nmol.mg protein-1.min-1. The abluminal Na-dependent glucose transporter is in a position to transport glucose from the brain extracellular fluid into the endothelial cells of the blood-brain barrier. The functional significance of its presence there remains to be determined.
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Reisser, Christoph, Kai Eichhorn, Christel Herold-Mende, Antonio I. Born, and Peter Bannasch. "Expression of facilitative glucose transport proteins during development of squamous cell carcinomas of the head and neck." International Journal of Cancer 80, no. 2 (January 18, 1999): 194–98. http://dx.doi.org/10.1002/(sici)1097-0215(19990118)80:2<194::aid-ijc6>3.0.co;2-m.
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Hay, WW. "Regulation of placental metabolism by glucose supply." Reproduction, Fertility and Development 7, no. 3 (1995): 365. http://dx.doi.org/10.1071/rd9950365.
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Glucose is supplied to the placenta and fetus from the maternal plasma according to concentration-dependent mechanisms exhibiting saturation kinetics that are mediated by facilitative transporter proteins on both the maternal-facing microvillus and fetal-facing basal trophoblast membranes. Placental glucose transport to the fetus requires a net maternal-to-fetal plasma glucose concentration gradient that is determined by placental as well as fetal glucose consumption. Fetal plasma glucose concentration, independent of maternal glucose concentration, regulates the partition of placental glucose uptake into transfer to the fetus and consumption by the placenta. Placental transport capacity increases with advancing gestation, probably by an increased number of transporter proteins as surface area increases. Placental glucose consumption contributes to most or all of placental lactate and fructose production and other less well defined non-oxidative pathways of carbon metabolism. Placental glucose consumption accounts for at least 50% of placental oxygen consumption which remains independent of short-term or long-term changes in placental glucose supply, thus requiring varying amounts of other carbon substrates. Placental glucose supply, therefore, plays a key role in regulating placental glucose metabolism and placental carbon balance, and interacts reciprocally with other carbon substrates to maintain placental oxidative metabolism.
Dissertations / Theses on the topic "Facilitative Glucose Transport Proteins"
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Graybill, Christopher A. "Biophysical Analysis of the Human Erythrocyte Glucose Transporter: a Dissertation." eScholarship@UMMS, 2005. https://escholarship.umassmed.edu/gsbs_diss/207.
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Hydrodynamic analysis and electron microscopy of GLUT1/lipid/detergent micelles and freeze fracture electron microscopy of GLUT1 proteoliposomes support the hypothesis that the glucose transporter is a multimeric (probably tetrameric) complex of GLUT1 proteins. Some detergents (e.g. octylglucoside) maintain the multimeric complex while other detergents (e.g. CHAPS and dodecylmaltoside) promote the dissociation of GLUT1 oligomers into smaller aggregation states (dimers or monomers). GLUT1 does not appear to exchange rapidly between protein/lipid/detergent micelles but is able to self-associate in the plane of the lipid bilayer. Quantitatively deglycosylated GLUT1 displays aberrant electrophoretic mobility, but each protein band contains full-length GLUT1 and the less mobile species, when treated with additional detergent and reductant, converts to the more mobile species. Preliminary structural analysis suggests that denaturing detergent- and thiol chemistry-related changes of α-helical content may mirror mobility shifts. Limited proteolysis of membrane-resident GLUT1 (± ligands) releases membrane-spanning α-helical domains suggesting that (i) some bilayer-resident helices are highly solvent exposed; (ii) membrane-spanning domains 1, 2, & 4 and 7, 8, & 10 are destabilized upon ligand binding; and (iii) helix packing compares well with high-resolution structures of prokaryotic transporters from the same superfamily. Results are consistent with a central, hydrophilic, translocation pathway comprised of amphipathic, membrane-spanning domains that alter associations upon ligand/substrate binding. We have resolved technical difficulties (heterogeneity, lipid/detergent removal, glycosylation, small molecule contamination) associated with GLUT1 analysis by mass spectrometry; and we map global conformational changes between sugar uptake and sugar efflux.
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Graybill, Christopher A. "Biophysical Analysis of the Human Erythrocyte Glucose Transporter: a Dissertation." eScholarship@UMMS, 2010. http://escholarship.umassmed.edu/gsbs_diss/207.
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Hydrodynamic analysis and electron microscopy of GLUT1/lipid/detergent micelles and freeze fracture electron microscopy of GLUT1 proteoliposomes support the hypothesis that the glucose transporter is a multimeric (probably tetrameric) complex of GLUT1 proteins. Some detergents (e.g. octylglucoside) maintain the multimeric complex while other detergents (e.g. CHAPS and dodecylmaltoside) promote the dissociation of GLUT1 oligomers into smaller aggregation states (dimers or monomers). GLUT1 does not appear to exchange rapidly between protein/lipid/detergent micelles but is able to self-associate in the plane of the lipid bilayer. Quantitatively deglycosylated GLUT1 displays aberrant electrophoretic mobility, but each protein band contains full-length GLUT1 and the less mobile species, when treated with additional detergent and reductant, converts to the more mobile species. Preliminary structural analysis suggests that denaturing detergent- and thiol chemistry-related changes of α-helical content may mirror mobility shifts. Limited proteolysis of membrane-resident GLUT1 (± ligands) releases membrane-spanning α-helical domains suggesting that (i) some bilayer-resident helices are highly solvent exposed; (ii) membrane-spanning domains 1, 2, & 4 and 7, 8, & 10 are destabilized upon ligand binding; and (iii) helix packing compares well with high-resolution structures of prokaryotic transporters from the same superfamily. Results are consistent with a central, hydrophilic, translocation pathway comprised of amphipathic, membrane-spanning domains that alter associations upon ligand/substrate binding. We have resolved technical difficulties (heterogeneity, lipid/detergent removal, glycosylation, small molecule contamination) associated with GLUT1 analysis by mass spectrometry; and we map global conformational changes between sugar uptake and sugar efflux.
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Danai, Laura V. "Role of Protein Kinase Map4k4 in Energy Metabolism: A Dissertation." eScholarship@UMMS, 2015. https://escholarship.umassmed.edu/gsbs_diss/791.
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Systemic glucose regulation is essential for human survival as low or chronically high glucose levels can be detrimental to the health of an individual. Glucose levels are highly regulated via inter-organ communication networks that alter metabolic function to maintain euglycemia. For example, when nutrient levels are low, pancreatic α-cells secrete glucagon, which signals to the liver to promote glycogen breakdown and glucose production. In times of excess nutrient intake, pancreatic β-cells release insulin. Insulin signals to the liver to suppress hepatic glucose production, and signals to the adipose tissue and the skeletal muscle to take up excess glucose via insulin-regulated glucose transporters. Defects in this inter-organ communication network including insulin resistance can result in glucose deregulation and ultimately the onset of type-2 diabetes (T2D).
To identify novel regulators of insulin-mediated glucose transport, our laboratory performed an siRNA-mediated gene-silencing screen in cultured adipocytes and measured insulin-mediated glucose transport. Gene silencing of Mitogen-activated protein kinase kinase kinase kinase 4 (Map4k4), a Sterile-20-related serine/threonine protein kinase, enhanced insulin-stimulated glucose transport, suggesting Map4k4 inhibits insulin action and glucose transport. Thus, for the first part of my thesis, I explore the role of Map4k4 in cultured adipose cells and show that Map4k4 also represses lipid synthesis independent of its effects on glucose transport. Map4k4 inhibits lipid synthesis in a Mechanistic target of rapamycin complex 1 (mTORC1)- and Sterol regulatory element-binding transcription factor 1 (Srebp-1)-dependent mechanism and not via a c-Jun NH2-terminal kinase (Jnk)-dependent mechanism. For the second part of my thesis, I explore the metabolic function of Map4k4 in vivo. Using mice with loxP sites flanking the Map4k4 allele and a ubiquitously expressed tamoxifen-activated Cre, we inducibly ablated Map4k4 expression in adult mice and found significant improvements in metabolic health indicated by improved fasting glucose and whole-body insulin action. To assess the role of Map4k4 in specific metabolic tissues responsible for systemic glucose regulation, we employed tissue-specific knockout mice to deplete Map4k4 in adipose tissue using an adiponectin-cre transgene, liver using an albumin-cre transgene, and skeletal muscle using a Myf5-cre transgene. Ablation of Map4k4 expression in adipose tissue or liver had no impact on whole body glucose homeostasis or insulin resistance. However, we surprisingly found that Map4k4 depletion in Myf5-positive tissues, which include skeletal muscles, largely recapitulates the metabolic phenotypes observed in systemic Map4k4 knockout mice, restoring obesity-induced glucose intolerance and insulin resistance. Furthermore these metabolic changes were associated with enhanced insulin signaling to Akt in the visceral adipose tissue, a tissue that is nearly devoid of Myf5-positive cells and does not display changes in Map4k4 expression. Thus, these results indicate that Map4k4 in Myf5-positive cells, most likely skeletal muscle cells, inhibits whole-body insulin action and these effects may be mediated via an indirect effect on the visceral adipose tissue. The results presented here provide evidence for Map4k4 as a potential therapeutic target for the treatment of insulin resistance and T2D.
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Danai, Laura V. "Role of Protein Kinase Map4k4 in Energy Metabolism: A Dissertation." eScholarship@UMMS, 2004. http://escholarship.umassmed.edu/gsbs_diss/791.
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Systemic glucose regulation is essential for human survival as low or chronically high glucose levels can be detrimental to the health of an individual. Glucose levels are highly regulated via inter-organ communication networks that alter metabolic function to maintain euglycemia. For example, when nutrient levels are low, pancreatic α-cells secrete glucagon, which signals to the liver to promote glycogen breakdown and glucose production. In times of excess nutrient intake, pancreatic β-cells release insulin. Insulin signals to the liver to suppress hepatic glucose production, and signals to the adipose tissue and the skeletal muscle to take up excess glucose via insulin-regulated glucose transporters. Defects in this inter-organ communication network including insulin resistance can result in glucose deregulation and ultimately the onset of type-2 diabetes (T2D).
To identify novel regulators of insulin-mediated glucose transport, our laboratory performed an siRNA-mediated gene-silencing screen in cultured adipocytes and measured insulin-mediated glucose transport. Gene silencing of Mitogen-activated protein kinase kinase kinase kinase 4 (Map4k4), a Sterile-20-related serine/threonine protein kinase, enhanced insulin-stimulated glucose transport, suggesting Map4k4 inhibits insulin action and glucose transport. Thus, for the first part of my thesis, I explore the role of Map4k4 in cultured adipose cells and show that Map4k4 also represses lipid synthesis independent of its effects on glucose transport. Map4k4 inhibits lipid synthesis in a Mechanistic target of rapamycin complex 1 (mTORC1)- and Sterol regulatory element-binding transcription factor 1 (Srebp-1)-dependent mechanism and not via a c-Jun NH2-terminal kinase (Jnk)-dependent mechanism. For the second part of my thesis, I explore the metabolic function of Map4k4 in vivo. Using mice with loxP sites flanking the Map4k4 allele and a ubiquitously expressed tamoxifen-activated Cre, we inducibly ablated Map4k4 expression in adult mice and found significant improvements in metabolic health indicated by improved fasting glucose and whole-body insulin action. To assess the role of Map4k4 in specific metabolic tissues responsible for systemic glucose regulation, we employed tissue-specific knockout mice to deplete Map4k4 in adipose tissue using an adiponectin-cre transgene, liver using an albumin-cre transgene, and skeletal muscle using a Myf5-cre transgene. Ablation of Map4k4 expression in adipose tissue or liver had no impact on whole body glucose homeostasis or insulin resistance. However, we surprisingly found that Map4k4 depletion in Myf5-positive tissues, which include skeletal muscles, largely recapitulates the metabolic phenotypes observed in systemic Map4k4 knockout mice, restoring obesity-induced glucose intolerance and insulin resistance. Furthermore these metabolic changes were associated with enhanced insulin signaling to Akt in the visceral adipose tissue, a tissue that is nearly devoid of Myf5-positive cells and does not display changes in Map4k4 expression. Thus, these results indicate that Map4k4 in Myf5-positive cells, most likely skeletal muscle cells, inhibits whole-body insulin action and these effects may be mediated via an indirect effect on the visceral adipose tissue. The results presented here provide evidence for Map4k4 as a potential therapeutic target for the treatment of insulin resistance and T2D.
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Silva, Filho Tiago Jo?o da. "Express?o imunoistoqu?mica de GLUT-1 e marcadores de prolifera??o e apoptose em anomalias vasculares orais." Universidade Federal do Rio Grande do Norte, 2014. http://repositorio.ufrn.br:8080/jspui/handle/123456789/17131.
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Vascular anomalies constitute a distinct group of lesions, but they may present similar clinical and histopatological characteristics, which can lead to diagnostic mistakes. This study aimed by histopathology and immunohistochemical expression of human glucose transporter protein (GLUT-1), correctly identify and classify oral vascular anomalies, besides analyzing the immunoexpression of markers proliferation and apoptosis (Ki-67 and Bcl-2). All cases diagnosed as "oral hemangiomas" belonging to the archives of the Service of Pathological Anatomy from the subject of Oral Pathology of the Department of Dentistry (DOD), of the Federal University of Rio Grande do Norte (UFRN) were reviewed, totalizing 77 cases. Immunohistochemical analysis for GLUT-1 showed that only 26 (33.8%) of the specimens were true infantile hemangiomas (IHs). The 51 (66.2%%) GLUT-1 negative specimens were then reclassified as pyogenic granulomas (PGs) and vascular malformations (VMs) from their histopathologic characteristics,totalizing 26 (33.8%) cases of IHs, 20 (26.0%) of PGs and 31 (40.2) cases of oral VMs. The cases analyzed by the marker Ki-67 showed different median IH (13,85), PG (33,70) and VM (4.55) with statistically significant differences between them (p <0.001). In relation to the protein Bcl-2, the groups also showed different median of the established scores IH (1.00), PG (1.50), VMs (0.0) demonstrating statistically significant differences between them (p<0,001). No statistically significant correlation between the indexes of positivity for Ki-67 and the scores of immunoexpression of Bcl-2 were observed in any group. Thus, we can conclude that it is necessary a careful and parameterized review of cases of vascular anomalies making use of auxiliary tools such as GLUT-1, since the histopathological findings alone, sometimes, are not sufficient to differentiate some anomalies. Furthermore, analysis of the expressions of markers involved in the levels of proliferation of lesions is important for a better understanding of its biological behavior aspect
As anomalias vasculares constituem um grupo de les?es distintas, mas que podem apresentar caracter?sticas cl?nicas e histopatol?gicas semelhantes, que podem levar a equ?vocos diagn?sticos.Este estudo objetivou por meio da histopatologia e da express?o imuno-histoqu?mica daprote?na humana transportadora de glicose (GLUT-1), identificar e classificar corretamente as anomalias vasculares orais, al?m de analisar a imunoexpress?o de marcadores de prolifera??o e apoptose (Ki-67 e Bcl-2).Todos os casos diagnosticados como hemangiomas orais pertencentes aos arquivos do Servi?o de Anatomia Patol?gica da disciplina de Patologia Oral do Departamento de Odontologia (DOD) da Universidade Federal do Rio Grande do Norte (UFRN) foram revisados, totalizando 77 casos. A an?lise imuno-histoqu?mica para GLUT-1 revelou que apenas 26 (33,8%) dos esp?cimes tratavam-se de hemangiomas da inf?ncia (HIs) verdadeiros. Os 51 (66,2%%)esp?cimes GLUT-1 negativos foram ent?o reclassificados em granulomas piog?nicos (GPs) e malforma??es vasculares (MVs) a partir de suas caracter?sticas histopatol?gicas, totalizando 26 (33,8%) casos de HIs, 20 (26,0%) de GPs e 31 (40,2) casos de MVs orais. Os casos submetidos ? an?lise do marcador Ki-67 apresentaram medianas diferentes HI (13,85), GP (33,70) e MV (4,55) com diferen?as estatisticamente significantes entre elas (p<0,001). Em rela??o ? prote?na Bcl-2, os grupos tamb?m apresentaram diferentes medianas dos escores estabelecidos HI (1,00), GP (1,50), MVs (0,0), demonstrando diferen?as estatisticamente significantes entre elas (p<0,001). N?o foi observada correla??o estatisticamente significante entre os ?ndices de positividade para o Ki-67 e os escores de imunoexpress?o de Bcl-2 em nenhum grupo.Dessa maneira, podemos concluir que se faz necess?rio uma revis?o criteriosa e parametrizada dos casos de anomalias vasculares utilizando ferramentas auxiliares, como a GLUT-1, uma vez que os achados histopatol?gicos sozinhos, ?s vezes, n?o s?o suficientes para diferenciar algumas anomalias. Al?m disso, a an?lise das express?es de marcadores envolvidos nos n?veis de prolifera??o das les?es ? um aspecto importante para o melhor entendimento do seu comportamento biol?gico
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Martineau, Louis C. "Myocardial glucose transport system related proteins, the effects of aging and exercise in old mice." Thesis, National Library of Canada = Bibliothèque nationale du Canada, 1997. http://www.collectionscanada.ca/obj/s4/f2/dsk2/ftp04/mq24205.pdf.
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Roberts, Dennis A. "Design and Synthesis of Stable Glucose Uptake Inhibitors." Ohio University / OhioLINK, 2016. http://rave.ohiolink.edu/etdc/view?acc_num=ohiou14791141897033.
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Cura, Anthony J. "Acute Modulation of Endothelial Cell Glucose Transport: A Dissertation." eScholarship@UMMS, 2010. http://escholarship.umassmed.edu/gsbs_diss/507.
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Studies have demonstrated that under conditions of chronic metabolic stress, GLUT1-mediated sugar transport is upregulated at the blood-brain barrier by a number of mechanisms. Although acute metabolic stress has also been shown to increase GLUT1-mediated transport, the mechanisms underlying this regulation remain unclear. This work attempts to explain how GLUT1-mediated sugar uptake is increased during acute metabolic stress, as well as explore the factors involved in this modulation of sugar transport in blood-brain barrier endothelial cells. Glucose depletion, KCN and FCCP were applied to brain microvascular endothelial cell line bEnd.3 in order to induce acute metabolic stress by ATP depletion. Kinetic sugar uptake measurements in combination with qPCR, whole cell lysate western blots, and cell-surface biotinylation were employed to probe for changes in GLUT1-mediated sugar uptake, GLUT1 expression levels, and GLUT1 localization during metabolic stress. Finally, the role of AMP-activated kinase (AMPK) in the bEnd.3 cell response to acute stress was examined using the specific AMPK activator AICAR and inhibitor Compound C.
The data presented in this thesis supports the following two conclusions: 1. GLUT1-mediated sugar transport in bEnd.3 cells during acute metabolic stress is increased 3-7 fold due to translocation of intracellular GLUT1 to the plasma membrane, with no change in expression of total GLUT1 protein, and 2. AMPK plays a direct role in modulating increases in GLUT1-mediated sugar transport in bEnd.3 cells during acute metabolic stress by regulating trafficking of GLUT1 to the plasma membrane.
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Levine, Kara B. "Identification of the Human Erythrocyte Glucose Transporter (GLUT1) ATP Binding Domain: A Dissertation." eScholarship@UMMS, 1999. https://escholarship.umassmed.edu/gsbs_diss/247.
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The human erythrocyte glucose transport protein (GLUT1) interacts with, and is regulated by, cytosolic ATP. This study asks the following questions concerning ATP modulation of GLUT1 mediated sugar transport. 1) Which region(s) of GLUT1 form the adenine nucleotide-binding domain? 2) What factors influence ATP modulation of sugar transport? 3) Is ATP interaction with GLUT1 sufficient for sugar transport regulation?
The first question was addressed through peptide mapping, n-terminal sequencing, and alanine scanning mutagenesis of GLUT1 using [32P]-azidoATP, a photoactivatable ATP analog. We then used a combination of transport measurements and photolabeling strategies to examine how glycolytic intermediates, pH, and transporter oligomeric structure affect ATP regulation of sugar transport. Finally, GLUT1 was reconstituted into proteoliposomes to determine whether ATP is sufficient for the modulation of GLUT1 function in-vitro.
This thesis presents data supporting the hypothesis that residues 332-335 contribute to the efficiency of adenine nucleotide binding to GLUT1. In addition, we show that AMP, acidification, and conversion of the transporter to its dimeric form antagonize ATP regulation of sugar transport. Finally, we present results that support the proposal that ATP interaction with GLUT1 is sufficient for transport modulation.
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Blodgett, David M. "Human Erythrocyte Glucose Transporter (GLUT1) Structure, Function, and Regulation: A Dissertation." eScholarship@UMMS, 2007. https://escholarship.umassmed.edu/gsbs_diss/326.
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The structure-function relationship explains how the human erythrocyte glucose transport protein (GLUT1) catalyzes sugar transport across the plasma membrane. This work investigates the glucose transport mechanism, the structural arrangement and dynamics of GLUT1 membrane-spanning α-helices, the molecular basis for glucose transport regulation by ATP, and how cysteine accessibility contributes to GLUT1 structure.
A rapid kinetics approach was applied to examine the conformational changes GLUT1 undergoes during the transport cycle. To transition from a global to molecular focus, a novel mass spectrometry technique was developed to resolve GLUT1 sequence that is associated either with membrane embedded GLUT1 subdomains or with water exposed domains. By studying accessibility changes of specific amino acids to covalent modification by a Sulfo-NHS-LC-Biotin probe, specific protein regions associated with glucose transport modulation by ATP were identified. Finally, mass spectrometry was applied to examine cysteine residue accessibility under native and reducing conditions.
This thesis presents data supporting the isolation of an intermediate, occluded GLUT1 conformational state that temporally bridges import and export configurations during glucose translocation. Our results confirm that amphipathic α-helices line the translocation pathway and promote interactions with the aqueous environment and substrate. In addition, we show that GLUT1 is conformationally dynamic, undergoes reorganization in the cytoplasmic region in response to ATP modulation, and that GLUT1 contains differentially exposed cysteine residues that affect its folding.
Books on the topic "Facilitative Glucose Transport Proteins"
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Klepper, Joerg. Glut1 Deficiency and the Ketogenic Diets. Edited by Eric H. Kossoff. Oxford University Press, 2016. http://dx.doi.org/10.1093/med/9780190497996.003.0005.
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Glucose is the essential fuel for the brain. Transport into brain is exclusively mediated by the facilitative glucose transporter Glut1. Glut1 deficiency results in a “brain energy crisis,” causing global developmental delay, epilepsy, and complex movement disorders including paroxysmal nonepileptic events. Early-onset absence epilepsy, paroxysmal exertion-induced dystonia, and stomatin-deficient cryohydrocytosis have been recognized as variants. Diagnosis is based on phenotype, isolated low CSF glucose, and mutations in the SLC2A1 gene. The condition is treated effectively by classical ketogenic diets providing ketones as an alternative fuel for the brain. The modified Atkins diet in adolescents and adults improves palatability and compliance at the expense of lower ketosis. Dietary treatment is continued into adolescence to meet the energy demand of the developing brain, raising concerns about long-term adverse effects. Current fields of research include novel compounds such as ketoesters and genetic approaches in Glut1-deficient mice as potential treatment options.
Book chapters on the topic "Facilitative Glucose Transport Proteins"
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Vyas, Nand K., Meenakshi N. Vyas, and Florante A. Quiocho. "Coordination and Stability of Calcium-Binding Site: D-Galactose/D-Glucose-Binding Protein of Bacterial Active Transport and Chemotaxis System." In Novel Calcium-Binding Proteins, 403–23. Berlin, Heidelberg: Springer Berlin Heidelberg, 1991. http://dx.doi.org/10.1007/978-3-642-76150-8_23.
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Londos, C., and I. A. Simpson. "cAMP-Independent Regulation of Adipocyte Glucose Transport Activity and Other Metabolic Processes by a Complex of Receptors and Their Associated G-Proteins." In GTPases in Biology II, 597–609. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/978-3-642-78345-6_37.
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Burant, Charles F. "Chapter 2 Facilitative glucose transport." In Cell Chemistry and Physiology: Part III, 67–86. Elsevier, 1996. http://dx.doi.org/10.1016/s1569-2582(96)80056-0.
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Turner, Jeffrey D., Annick Delaquis, and Christiane Malo. "Culture of Mammary Tissue: Glucose Transport Processes." In Mathematical Modeling in Experimental Nutrition - Vitamins, Proteins, Methods, 207–13. Elsevier, 1996. http://dx.doi.org/10.1016/s1043-4526(08)60030-3.
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Pershadsingh, Harrihar A., Debra L. Shade, and Jay M. McDonald. "STIMULATION OF GLUCOSE TRANSPORT BY INSULIN, VANADATE, CONCANAVALIN A, HYDROGEN PEROXIDE, AND PHORBOL ESTER OCCUR BY A CALCIUM-DEPENDENT MECHANISM." In Calcium-Binding Proteins in Health and Disease, 201–3. Elsevier, 1987. http://dx.doi.org/10.1016/b978-0-12-521040-9.50039-5.
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Lachmann, Robin H., and Timothy M. Cox. "Glycogen storage diseases." In Oxford Textbook of Medicine, edited by Timothy M. Cox, 1985–93. Oxford University Press, 2020. http://dx.doi.org/10.1093/med/9780198746690.003.0227.
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Glycogen is a highly branched glucose polymer with a compacted structure found predominantly in liver and muscle. Liver glycogen is important in the maintenance of euglycaemia during fasting; muscle glycogen is an immediate source of glucose for energy production during exercise. Genetic disorders affecting proteins that regulate glycogen metabolism and transport, as well as those which catalyse its biosynthesis and breakdown, cause marked accumulation of glycogen in diverse tissues, and pathological glycogen often has an abnormal macromolecular structure. Depending on the enzyme system involved, diseases of glycogen metabolism principally affect liver and muscle. Clinical features are related to pathological glycogen in tissues and/or failure to release glucose. Glycogen storage is associated with organomegaly and tissue injury. Fasting hypoglycaemia occurs where hepatic breakdown of glycogen is impaired. Glycogen diseases that affect muscle usually present with rhabdomyolysis, exercise intolerance, and muscle pain or weakness. Formerly, diseases of glycogen metabolism were diagnosed by showing excess storage of glycogen in the tissue of interest, accompanied by reduced activity of particular glycogen-metabolizing enzymes. Currently, where available, molecular analysis of genomic DNA is the preferred method for providing a definitive diagnosis. The mainstay of treatment of glycogen diseases affecting the liver is dietary, including pre-emptive management of hypoglycaemia that is readily provoked by fasting. Dietary interventions may also ameliorate some of the glycogen diseases that affect muscle, and weakness and pain after exertion can be improved by graduated exercise programmes in some patients.
Conference papers on the topic "Facilitative Glucose Transport Proteins"
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Jewel, Yead, Prashanta Dutta, and Jin Liu. "Coarse-Grained Molecular Dynamics Simulations of Sugar Transport Across Lactose Permease." In ASME 2015 International Mechanical Engineering Congress and Exposition. American Society of Mechanical Engineers, 2015. http://dx.doi.org/10.1115/imece2015-52337.
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Sugar (one of the critical nutrition elements for all life forms) transport across the cell membranes play essential roles in a wide range of living organism. One of the most important active transport (against the sugar concentration) mechanisms is facilitated by the transmembrane transporter proteins, such as the Escherichia coli lactose permease (LacY) proteins. Active transport of sugar molecules with LacY proteins requires a proton gradient and a sequence of complicated protein conformational changes. However, the exact molecular mechanisms and the protein structural information involved in the transport process are largely unknown. All atom atomistic simulations are able to provide full details but are limited to relative small length and time scales due to the computational cost. The protein conformational changes during sugar transport across LacY are large scale structural reorganization and inaccessible to all atom simulations. In this work, we investigate the molecular mechanisms and conformational changes during sugar transport using coarse-grained molecular dynamics (CGMD) simulations. In our coarse-grained force field, we follow the procedures developed by Han et al. [1, 2], in which the protein model is united-atom based and each heavy atom together with the attached hydrogen atoms is represented by one site, then the protein force filed is coupled with the MARTINI [3] water and lipid force fields. This hybrid force field takes the advantage of the efficiency of MARTINI force field for the environment (water and lipid), while retaining the detailed conformational information for the proteins. Specifically, we develop the new force fields for interactions between sugar molecules and protein by matching the potential of mean force between all-atom and coarse-grained models. Then we validate our force field by comparing the potential of mean force for a glucose interaction with a carbohydrate binding protein from our new force field, with the results from all atom simulations. After validation, we implement the force field for sugar transport across LacY proteins. Through our simulations we are able to capture the formation/breakage of the important hydrogen bonds and salt bridges, which are crucial to the overall conformational changes of LacY.
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Steck, Roland, and Melissa L. Knothe Tate. "Application of Stochastic Network Models for the Study of Molecular Transport Processes in Bone." In ASME 2004 International Mechanical Engineering Congress and Exposition. ASMEDC, 2004. http://dx.doi.org/10.1115/imece2004-59746.
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Osteocytes are the most abundant cells in bone. They are entombed in lacunae within the bone matrix, but are interconnected via their processes that run within the canaliculi with other osteocytes, as well as with the osteoblasts and bone lining cells on the bone surfaces, and thus from a cellular syncytium. However, the osteocytes are not immediately connected with the vasculature of bone, which means that the transport of nutrients and hormones to the cells and the removal of waste products from the cells, as well as transport of signaling molecules between the cells, has to occur either via the pericellular fluid spaces in the lacunocanalicular network, via the matrix micropores between the collagen fibers and the apatite crystals, or via intracellular transport mechanisms. Only recently our laboratory and other research groups have started to examine the transport pathways of different molecular size substances within bone systematically, using experimental tracer methods (e.g. [1, 7]). These experiments have unveiled the molecular sieving characteristics of bone: While small tracers with molecular weights of 300 Daltons (Da, e.g. glucose and small amino acids) are found in abundance throughout the bone matrix and the lacunocanalicular network, larger molecules (e.g. cytokines and serum derived proteins) are only transported through the pericellular spaces of the lacunocanalicular network. Furthermore, the transport of these substances through the lacunocanalicular network can be enhanced by mechanical loading of bone [1]. These findings highlight the importance of the lacunocanalicular network for the survival of the osteocytes and thereby tissue health. However, the state of the osteocyte syncytium is affected by age and bone diseases. It has been shown that the number of osteocytes in cortical bone decreases with age [6]. Furthermore, a histological study of cortical bone tissue samples from donors undergoing hip replacement surgery has shown that the morphology of the lacunocanalicular network is altered in diseased bone [2].
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Kim, Sungwon S., Tom T. Huang, Timothy S. Fisher, and Michael R. Ladisch. "Effects of Carbon Nanotube Structure on Protein Adsorption." In ASME 2005 International Mechanical Engineering Congress and Exposition. ASMEDC, 2005. http://dx.doi.org/10.1115/imece2005-81395.
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Outstanding transport characteristics and high surface-to-volume ratios are several advantages that carbon nanotubes possess that make them attractive candidates for protein immobilization matrices in biosensor applications. A further advantage of using carbon nanotubes is that their structure (e.g., diameter, length, density) can potentially be controlled during synthesis. In the present study, the effects of carbon nanotube structure on enzyme immobilization onto carbon nanotube arrays are investigated. Bovine serum albumin (BSA) serves as both a blocking agent for prevention of nonspecific adsorption and as a support for anchoring bioreceptors. BSA, a globular protein having a 4 to 6 nm characteristic dimension, is stably adsorbed through mechanisms that involve hydrophobic interactions between surfaces presented by the carbon nanotubes and the spacing between the nanotubes with the protein. Protein adsorption is confirmed by fluorescence microscopy of surfaces that have been exposed to fluourescein isothiocyanate (FITC) labeled BSA. The adsorption of biotinylated BSA can be used, through a sandwich immobilization scheme, to provide an anchor for streptavidin, which in turn has at least one other adsorption site that is specific for other biotinylated proteins such as glucose oxidase that would form a biorecognition or catalytic element in a functional biosensor. Correlation between carbon nanotube structure and protein adsorption at the nano-bio interface could eventually lead to growth conditions that yield carbon nanotubes for biosensor applications with optimal protein adsorption characteristics.