Статті в журналах з теми "Sodium-galactose transporter"
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1
Abramson, Jeff. "Deciphering ligand-induced conformational changes in the sodium galactose transporter." Acta Crystallographica Section A Foundations and Advances 73, a2 (December 1, 2017): C150. http://dx.doi.org/10.1107/s2053273317094232.
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2
Alruwaili, Nawaf W., and Fahad Alshdayed. "Fructose Metabolism and Its Effect on Glucose-Galactose Malabsorption Patients: A Literature Review." Diagnostics 13, no. 2 (January 12, 2023): 294. http://dx.doi.org/10.3390/diagnostics13020294.
Повний текст джерелаАнотація:
Glucose-galactose malabsorption is a rare inherited autosomal recessive genetic defect. A mutation in the glucose sodium-dependent transporter-1 gene will alter the transportation and absorption of glucose and galactose in the intestine. The defect in the SGLT-1 leads to unabsorbed galactose, glucose, and sodium, which stay in the intestine, leading to dehydration and hyperosmotic diarrhea. Often, glucose-galactose malabsorption patients are highly dependent on fructose, their primary source of carbohydrates. This study aims to investigate all published studies on congenital glucose-galactose malabsorption and fructose malabsorption. One hundred published studies were assessed for eligibility in this study, and thirteen studies were identified and reviewed. Studies showed that high fructose consumption has many health effects and could generate life-threatening complications. None of the published studies included in this review discussed or specified the side effects of fructose consumption as a primary source of carbohydrates in congenital glucose-galactose malabsorption patients.
3
Ohta, T., K. J. Isselbacher, and D. B. Rhoads. "Regulation of glucose transporters in LLC-PK1 cells: effects of D-glucose and monosaccharides." Molecular and Cellular Biology 10, no. 12 (December 1990): 6491–99. http://dx.doi.org/10.1128/mcb.10.12.6491-6499.1990.
Повний текст джерелаАнотація:
Regulation of D-glucose transport in the porcine kidney epithelial cell line LLC-PK1 was examined. To identify the sodium-coupled glucose transporter (SGLT), we cloned and sequenced several partial cDNAs homologous to SGLT1 from rabbit small intestine (M. A. Hediger, M. J. Coady, T. S. Ikeda, and E. M. Wright, Nature (London) 330:379-381, 1987). The extensive homology of the two sequences leads us to suggest that the high-affinity SGLT expressed by LLC-PK1 cells is SGLT1. SGLT1 mRNA levels were highest when the D-glucose concentration in the culture medium was 5 to 10 mM. Addition of D-mannose or D-fructose, but not D-galactose, in the presence of 5 mM D-glucose suppressed SGLT1 mRNA levels. SGLT1 activity, measured by methyl alpha-D-glucopyranoside uptake, paralleled message levels except in cultures containing D-galactose. Therefore, SGLT1 gene expression may respond either to the cellular energy status or to the concentration of a hexose metabolite(s). By isolating several cDNAs homologous to rat GLUT-1, we identified the facilitated glucose transporter in LLC-PK1 cells as the erythroid/brain type GLUT-1. High-stringency hybridization of a single mRNA transcript to the rat GLUT-1 cDNA probe and failure to observe additional transcripts hybridizing either to GLUT-1 or to GLUT-2 probes at low stringency provide evidence that GLUT-1 is the major facilitated glucose transporter in this cell line. LLC-PK1 GLUT-1 mRNAs were highest at medium D-glucose concentrations of less than or equal to 2 mM. D-Fructose, D-mannose, and to a lesser extent D-galactose all suppressed GLUT-1 mRNA levels. Since the pattern of SGLT1 and GLUT-1 expression differed, particularly in low D-glucose or in the presence of D-galactose, we suggest that the two transporters are regulated independently.
4
Ohta, T., K. J. Isselbacher, and D. B. Rhoads. "Regulation of glucose transporters in LLC-PK1 cells: effects of D-glucose and monosaccharides." Molecular and Cellular Biology 10, no. 12 (December 1990): 6491–99. http://dx.doi.org/10.1128/mcb.10.12.6491.
Повний текст джерелаАнотація:
Regulation of D-glucose transport in the porcine kidney epithelial cell line LLC-PK1 was examined. To identify the sodium-coupled glucose transporter (SGLT), we cloned and sequenced several partial cDNAs homologous to SGLT1 from rabbit small intestine (M. A. Hediger, M. J. Coady, T. S. Ikeda, and E. M. Wright, Nature (London) 330:379-381, 1987). The extensive homology of the two sequences leads us to suggest that the high-affinity SGLT expressed by LLC-PK1 cells is SGLT1. SGLT1 mRNA levels were highest when the D-glucose concentration in the culture medium was 5 to 10 mM. Addition of D-mannose or D-fructose, but not D-galactose, in the presence of 5 mM D-glucose suppressed SGLT1 mRNA levels. SGLT1 activity, measured by methyl alpha-D-glucopyranoside uptake, paralleled message levels except in cultures containing D-galactose. Therefore, SGLT1 gene expression may respond either to the cellular energy status or to the concentration of a hexose metabolite(s). By isolating several cDNAs homologous to rat GLUT-1, we identified the facilitated glucose transporter in LLC-PK1 cells as the erythroid/brain type GLUT-1. High-stringency hybridization of a single mRNA transcript to the rat GLUT-1 cDNA probe and failure to observe additional transcripts hybridizing either to GLUT-1 or to GLUT-2 probes at low stringency provide evidence that GLUT-1 is the major facilitated glucose transporter in this cell line. LLC-PK1 GLUT-1 mRNAs were highest at medium D-glucose concentrations of less than or equal to 2 mM. D-Fructose, D-mannose, and to a lesser extent D-galactose all suppressed GLUT-1 mRNA levels. Since the pattern of SGLT1 and GLUT-1 expression differed, particularly in low D-glucose or in the presence of D-galactose, we suggest that the two transporters are regulated independently.
5
Adelman, Joshua L., Ying Sheng, Seungho Choe, Jeff Abramson, Ernest M. Wright, John M. Rosenberg, and Michael Grabe. "Structural Determinants of Water Permeation through the Sodium-Galactose Transporter vSGLT." Biophysical Journal 106, no. 6 (March 2014): 1280–89. http://dx.doi.org/10.1016/j.bpj.2014.01.006.
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Henriquez, Tania, Larissa Wirtz, Dan Su, and Heinrich Jung. "Prokaryotic Solute/Sodium Symporters: Versatile Functions and Mechanisms of a Transporter Family." International Journal of Molecular Sciences 22, no. 4 (February 13, 2021): 1880. http://dx.doi.org/10.3390/ijms22041880.
Повний текст джерелаАнотація:
The solute/sodium symporter family (SSS family; TC 2.A.21; SLC5) consists of integral membrane proteins that use an existing sodium gradient to drive the uphill transport of various solutes, such as sugars, amino acids, vitamins, or ions across the membrane. This large family has representatives in all three kingdoms of life. The human sodium/iodide symporter (NIS) and the sodium/glucose transporter (SGLT1) are involved in diseases such as iodide transport defect or glucose-galactose malabsorption. Moreover, the bacterial sodium/proline symporter PutP and the sodium/sialic acid symporter SiaT play important roles in bacteria–host interactions. This review focuses on the physiological significance and structural and functional features of prokaryotic members of the SSS family. Special emphasis will be given to the roles and properties of proteins containing an SSS family domain fused to domains typically found in bacterial sensor kinases.
7
Post, Deborah M. B., Rachna Mungur, Bradford W. Gibson, and Robert S. Munson. "Identification of a Novel Sialic Acid Transporter in Haemophilus ducreyi." Infection and Immunity 73, no. 10 (October 2005): 6727–35. http://dx.doi.org/10.1128/iai.73.10.6727-6735.2005.
Повний текст джерелаАнотація:
ABSTRACT Haemophilus ducreyi, the causative agent of chancroid, produces a lipooligosaccharide (LOS) which terminates in N-acetyllactosamine. This glycoform can be further extended by the addition of a single sialic acid residue to the terminal galactose moiety. H. ducreyi does not synthesize sialic acid, which must be acquired from the host during infection or from the culture medium when the bacteria are grown in vitro. However, H. ducreyi does not have genes that are highly homologous to the genes encoding known bacterial sialic acid transporters. In this study, we identified the sialic acid transporter by screening strains in a library of random transposon mutants for those mutants that were unable to add sialic acid to N-acetyllactosamine-containing LOS. Mutants that reacted with the monoclonal antibody 3F11, which recognizes the terminal lactosamine structure, and lacked reactivity with the lectin Maackia amurensis agglutinin, which recognizes α2,3-linked sialic acid, were further characterized to demonstrate that they produced a N-acetyllactosamine-containing LOS by silver-stained sodium dodecyl sulfate-polyacrylamide gel electrophoresis and mass spectrometric analyses. The genes interrupted in these mutants were mapped to a four-gene cluster with similarity to genes encoding bacterial ABC transporters. Uptake assays using radiolabeled sialic acid confirmed that the mutants were unable to transport sialic acid. This study is the first report of bacteria using an ABC transporter for sialic acid uptake.
8
Bisha, Ina, Alex Rodriguez, Jacopo Sgrignani, Alessandra Magistrato, and Alessandro Laio. "Sodium-Galactose Transporter: The First Steps of the Transport Mechanism Investigated by Molecular Dynamics." Biophysical Journal 106, no. 2 (January 2014): 365a—366a. http://dx.doi.org/10.1016/j.bpj.2013.11.2073.
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Charon, J. P., J. McCormick, A. Mehta, and P. J. Kemp. "Characterization of sodium-dependent glucose transport in sheep tracheal epithelium." American Journal of Physiology-Lung Cellular and Molecular Physiology 267, no. 4 (October 1, 1994): L390—L397. http://dx.doi.org/10.1152/ajplung.1994.267.4.l390.
Повний текст джерелаАнотація:
The nonmetabolizable glucose analogue methyl(alpha-D-[U-14C]gluco)pyranoside ([14C]AMG) was used to study sodium-dependent glucose transport in two preparations: 1) discs punched from strips of sheep tracheal epithelium, and 2) freshly enzyme-isolated sheep tracheal epithelial cells. In discs, cellular accumulation of [14C]AMG was saturable and exhibited a Michaelis-Menten constant (Km) for AMG of 0.63 +/- 0.15 mM. Uptake was linear over 30 min and was inhibited maximally by 100 microM phlorizin [inhibition constant (Ki) approximately 20 nM], by replacement of external sodium with choline or by addition of 10 mM D-glucose (Ki = 0.19 +/- 0.02 mM). Accumulative uptake was activated, in a concentration-dependent manner, by external sodium [affinity constant (Ka) approximately 23 mM] with a Hill coefficient of greater than one but was abolished on depolarizing with high external potassium. In the presence of sodium, D-galactose and AMG both inhibited uptake of [14C]AMG, whereas L-glucose, D-fructose, and D-mannose were ineffective. In isolated cells, [14C]AMG accumulated only in the presence of external sodium and uptake was inhibited by the addition of D-glucose (Ki approximately 0.2 mM), D-galactose, and AMG but not by L-glucose or D-xylose. We conclude that sheep tracheal epithelium exhibits sodium-dependent glucose uptake with a very high affinity for phlorizin, which indicates the presence of a novel isoform of the transporter.
10
Faham, S., A. Watanabe, G. M. Besserer, D. Cascio, A. Specht, B. A. Hirayama, E. M. Wright, and J. Abramson. "The Crystal Structure of a Sodium Galactose Transporter Reveals Mechanistic Insights into Na+/Sugar Symport." Science 321, no. 5890 (August 8, 2008): 810–14. http://dx.doi.org/10.1126/science.1160406.
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11
Aljure, Oscar, and Ana Díez-Sampedro. "Functional characterization of mouse sodium/glucose transporter type 3b." American Journal of Physiology-Cell Physiology 299, no. 1 (July 2010): C58—C65. http://dx.doi.org/10.1152/ajpcell.00030.2010.
Повний текст джерелаАнотація:
Despite belonging to a family of sugar cotransporters, human sodium/glucose transporter type 3 (hSGLT3) does not transport sugar, but it depolarizes the cell in the presence of extracellular sugar, and thus it has been suggested to work as a sugar sensor. In the human genome there is one SGLT3 gene, yet in mouse there are two. In this study we cloned one of them, mouse SGLT3b (mSGLT3b) and characterized the protein. We found that mSGLT3b has low affinity for sugars, as does hSGLT3, but surprisingly, mSGLT3b transports sugar, although the sugar transport is not as tightly coupled to cations as in SGLT1. Moreover, the sugar specificity of mSGLT3b has characteristics reminiscent of both SGLT1 and hSGLT3: mSGLT3b does not respond to galactose, similar to hSGLT3, but neither does it respond to 1-deoxynojirimycin, unlike hSGLT3 but similar to SGLT1. mSGLT3b has low apparent affinities for sugar and Na+ and, furthermore, displays pre-steady-state currents, which in SGLT1 report on conformational changes in the protein. Finally, phlorizin, the typical inhibitor of SGLT proteins, also inhibits mSGLT3b. In summary, although mSGLT3b has some characteristics that resemble SGLT1 and others that are similar to hSGLT3, its low sugar affinity and uncoupled sugar transport lead us to conclude that mSGLT3b likely functions as a physiological glucose sensor similar to hSGLT3.
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Pavić, Mirela, Marija Ljubojević, Ivona Žura Žaja, Ivana Prakatur, Manuela Grčević, Suzana Milnković-Tur, Hrvoje Brzica, and Marcela Šperanda. "Transepithelial glucose transport in the small intestine." Veterinarska stanica 51, no. 6 (July 1, 2020): 673–86. http://dx.doi.org/10.46419/vs.51.6.1.
Повний текст джерелаАнотація:
The duodenum, jejunum and ileum are parts of the small intestine and the sites of the terminal stages of enzymatic digestion, and the majority of nutrient, electrolyte and water absorption. The apical, luminal membrane of the enterocyte is built of numerous microvilli that increase the absorptive surface of the cell. Carbohydrates, in the form of monosaccharides, oligosaccharides and especially polysaccharides, make up the largest quantitative and energetic part of the diet of most animals, including humans. Galactose, fructose and glucose, the final degradation products of polysaccharide and oligosaccharide enzymatic digestion, can be absorbed by enterocytes either by active transport or by facilitated diffusion. In the small intestine, the transepithelial transport of glucose, the most abundant monosaccharide after carbohydrate digestion and the main source of energy, is performed by a specific membrane transporter located in the brush border membrane of the enterocyte, the sodiumglucose cotransporter 1 (SGLT1). While SGLT1 transports glucose across the brush border membrane, a specific basolateral membrane glucose transporter, the sodium-independent glucose transporter 2 (GLUT2), transfers glucose out of the enterocyte down the concentration gradient. The sodium-potassium pump (Na/KATPase), as a sodium and potassium ion transporter, is functionally closely related to the sodium-dependent SGLT1. Na/KATPase is responsible for maintaining the electrochemical gradient of sodium ions, as the driving force for glucose transport via SGLT1. Transepithelial transport of glucose in the small intestine and the differentiation of enterocytes occurs relatively early during the foetal period, allowing glucose to be absorbed from ingested amniotic fluid. Nutrient transport is possible along the whole villus-crypt axis during intrauterine development, while transport shifts toward the villus tip in the mature small intestine. With maturation, glucose transport rates change not only across the villus-crypt axis, but also along the proximodistal axis in the small intestine. The glucose absorption rate shows differences between subunits of the small intestine depending on the age and type of ingested carbohydrates, where complex carbohydrates replace less complex carbohydrates or disaccharides.
13
Titgemeyer, Fritz, Johannes Amon, Stephan Parche, Maysa Mahfoud, Johannes Bail, Maximilian Schlicht, Nadine Rehm, et al. "A Genomic View of Sugar Transport in Mycobacterium smegmatis and Mycobacterium tuberculosis." Journal of Bacteriology 189, no. 16 (June 8, 2007): 5903–15. http://dx.doi.org/10.1128/jb.00257-07.
Повний текст джерелаАнотація:
ABSTRACT We present a comprehensive analysis of carbohydrate uptake systems of the soil bacterium Mycobacterium smegmatis and the human pathogen Mycobacterium tuberculosis. Our results show that M. smegmatis has 28 putative carbohydrate transporters. The majority of sugar transport systems (19/28) in M. smegmatis belong to the ATP-binding cassette (ABC) transporter family. In contrast to previous reports, we identified genes encoding all components of the phosphotransferase system (PTS), including permeases for fructose, glucose, and dihydroxyacetone, in M. smegmatis. It is anticipated that the PTS of M. smegmatis plays an important role in the global control of carbon metabolism similar to those of other bacteria. M. smegmatis further possesses one putative glycerol facilitator of the major intrinsic protein family, four sugar permeases of the major facilitator superfamily, one of which was assigned as a glucose transporter, and one galactose permease of the sodium solute superfamily. Our predictions were validated by gene expression, growth, and sugar transport analyses. Strikingly, we detected only five sugar permeases in the slow-growing species M. tuberculosis, two of which occur in M. smegmatis. Genes for a PTS are missing in M. tuberculosis. Our analysis thus brings the diversity of carbohydrate uptake systems of fast- and a slow-growing mycobacteria to light, which reflects the lifestyles of M. smegmatis and M. tuberculosis in their natural habitats, the soil and the human body, respectively.
14
Scholtka, B., F. Stümpel, and K. Jungermann. "Acute increase, stimulated by prostaglandin E2, in glucose absorption via the sodium dependent glucose transporter-1 in rat intestine." Gut 44, no. 4 (April 1, 1999): 490–96. http://dx.doi.org/10.1136/gut.44.4.490.
Повний текст джерелаАнотація:
BACKGROUND/AIMSAcute stimulation by cAMP of the sodium dependent glucose cotransporter SGLT1 has previously been shown. As prostaglandin E2(PGE2) increases intracellular cAMP concentrations via its receptor subtypes EP2R and EP4R, it was investigated whether PGE2 could enhance intestinal glucose absorption.METHODSThe action of PGE2 on carbohydrate absorption in the ex situ perfused rat small intestine and on 3-O-[14C]methylglucose uptake in isolated villus tip enterocytes was determined. Expression of mRNA for the PGE2 receptor subtypes 1–4 was assayed in enterocytes by reverse transcriptase polymerase chain reaction (RT-PCR).RESULTSIn the perfused small intestine, PGE2 acutely increased absorption of glucose and galactose, but not fructose (which is not a substrate for SGLT1); in isolated enterocytes it stimulated 3-O-[14C]methylglucose uptake. The 3-O-[14C]methylglucose uptake could be inhibited by the cAMP antagonist RpcAMPS and the specific inhibitor of SGLT1, phlorizin. High levels of EP2R mRNA and EP4R mRNA were detected in villus tip enterocytes.CONCLUSIONPGE2acutely increased glucose and galactose absorption by the small intestine via the SGLT1, with cAMP serving as the second messenger. PGE2 acted directly on the enterocytes, as the stimulation was still observed in isolated enterocytes and RT-PCR detected mRNA for the cAMP-increasing PGE2 receptors EP2R and EP4R.
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Choe, Seungho, Joshua L. Adelman, John M. Rosenberg, Ernest M. Wright, Jeff Abramson, and Michael Grabe. "Understanding Substrate Unbinding from the Sodium-Galactose Co-Transporter vSGLT based on 16 Microseconds of Molecular Simulation." Biophysical Journal 102, no. 3 (January 2012): 661a. http://dx.doi.org/10.1016/j.bpj.2011.11.3603.
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Adelman, Joshua L., Ying Sheng, Seungho Choe, Jeff Abramson, Ernest M. Wright, and Michael Grabe. "Insight into the Mechanism of Water Permeation through the Sodium-Galactose Transporter vSGLT from Long Molecular Dynamics Simulations." Biophysical Journal 106, no. 2 (January 2014): 365a. http://dx.doi.org/10.1016/j.bpj.2013.11.2071.
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Liu, Yaqun, Liguo Shang, Yuhua Zhan, Min Lin, Zhu Liu, and Yongliang Yan. "Genome-Wide Analysis of Sugar Transporters Identifies the gtsA Gene for Glucose Transportation in Pseudomonas stutzeri A1501." Microorganisms 8, no. 4 (April 19, 2020): 592. http://dx.doi.org/10.3390/microorganisms8040592.
Повний текст джерелаАнотація:
Pseudomonas stutzeri A1501 possesses an extraordinary number of transporters which confer this rhizosphere bacterium with the sophisticated ability to metabolize various carbon sources. However, sugars are not a preferred carbon source for P. stutzeri A1501. The P. stutzeri A1501 genome has been sequenced, allowing for the homology-based in silico identification of genes potentially encoding sugar-transport systems by using established microbial sugar transporters as a template sequence. Genomic analysis revealed that there were 10 sugar transporters in P. stutzeri A1501, most of which belong to the ATP-binding cassette (ABC) family (5/10); the others belong to the phosphotransferase system (PTS), major intrinsic protein (MIP) family, major facilitator superfamily (MFS) and the sodium solute superfamily (SSS). These systems might serve for the import of glucose, galactose, fructose and other types of sugar. Growth analysis showed that the only effective medium was glucose and its corresponding metabolic system was relatively complete. Notably, the loci of glucose metabolism regulatory systems HexR, GltR/GtrS, and GntR were adjacent to the transporters ABCMalEFGK, ABCGtsABCD, and ABCMtlEFGK, respectively. Only the ABCGtsABCD expression was significantly upregulated under both glucose-sufficient and -limited conditions. The predicted structure and mutant phenotype data of the key protein GtsA provided biochemical evidence that P. stutzeri A1501 predominantly utilized the ABCGtsABCD transporter for glucose uptake. We speculate that gene absence and gene diversity in P. stutzeri A1501 was caused by sugar-deficient environmental factors and hope that this report can provide guidance for further analysis of similar bacterial lifestyles.
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Sanguinetti, Manuel, Sotiris Amillis, Sergio Pantano, Claudio Scazzocchio, and Ana Ramón. "Modelling and mutational analysis of Aspergillus nidulans UreA, a member of the subfamily of urea/H + transporters in fungi and plants." Open Biology 4, no. 6 (June 2014): 140070. http://dx.doi.org/10.1098/rsob.140070.
Повний текст джерелаАнотація:
We present the first account of the structure–function relationships of a protein of the subfamily of urea/H + membrane transporters of fungi and plants, using Aspergillus nidulans UreA as a study model. Based on the crystal structures of the Vibrio parahaemolyticus sodium/galactose symporter (vSGLT) and of the Nucleobase-Cation-Symport-1 benzylhydantoin transporter from Microbacterium liquefaciens (Mhp1), we constructed a three-dimensional model of UreA which, combined with site-directed and classical random mutagenesis, led to the identification of amino acids important for UreA function. Our approach allowed us to suggest roles for these residues in the binding, recognition and translocation of urea, and in the sorting of UreA to the membrane. Residues W82, Y106, A110, T133, N275, D286, Y388, Y437 and S446, located in transmembrane helixes 2, 3, 7 and 11, were found to be involved in the binding, recognition and/or translocation of urea and the sorting of UreA to the membrane. Y106, A110, T133 and Y437 seem to play a role in substrate selectivity, while S446 is necessary for proper sorting of UreA to the membrane. Other amino acids identified by random classical mutagenesis (G99, R141, A163, G168 and P639) may be important for the basic transporter's structure, its proper folding or its correct traffic to the membrane.
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Verdile, Nicole, Rolando Pasquariello, Tiziana A. L. Brevini, and Fulvio Gandolfi. "The 3D Pattern of the Rainbow Trout (Oncorhynchus mykiss) Enterocytes and Intestinal Stem Cells." International Journal of Molecular Sciences 21, no. 23 (December 2, 2020): 9192. http://dx.doi.org/10.3390/ijms21239192.
Повний текст джерелаАнотація:
We previously showed that, according to the frequency and distribution of specific cell types, the rainbow trout (RT) intestinal mucosa can be divided in two regions that form a complex nonlinear three-dimensional (3D) pattern and have a different renewal rate. This work had two aims. First, we investigated whether the unusual distribution of cell populations reflects a similar distribution of functional activities. To this end, we determined the protein expression pattern of three well-defined enterocytes functional markers: peptide transporter 1 (PepT1), sodium–glucose/galactose transporter 1 (SGLT-1), and fatty-acid-binding protein 2 (Fabp2). Second, we characterized the structure of RT intestinal stem-cell (ISC) niche and determined whether the different proliferative is accompanied by a different organization and/or extension of the stem-cell population. We studied the expression and localization of well-characterized mammal ISC markers: LGR5, HOPX, SOX9, NOTCH1, DLL1, and WNT3A. Our results indicate that morphological similarity is associated with similar function only between the first portion of the mid-intestine and the apical part of the complex folds in the second portion. Mammal ISC markers are all expressed in RT, but their localization is completely different, suggesting also substantial functional differences. Lastly, higher renewal rates are supported by a more abundant ISC population.
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Liu, Tiemin, Bryan Lo, Pam Speight, and Mel Silverman. "Transmembrane IV of the high-affinity sodium-glucose cotransporter participates in sugar binding." American Journal of Physiology-Cell Physiology 295, no. 1 (July 2008): C64—C72. http://dx.doi.org/10.1152/ajpcell.90602.2007.
Повний текст джерелаАнотація:
Investigation of the structure/function relationships of the sodium-glucose transporter (SGLT1) is crucial to understanding the cotransporter mechanism. In the present study, we used cysteine-scanning mutagenesis and chemical modification by methanethiosulfonate (MTS) derivatives to test whether predicted transmembrane IV participates in sugar binding. Five charged and polar residues (K139, Q142, T156, K157, and D161) and two glucose/galactose malabsorption missense mutations (I147 and S159) were replaced with cysteine. Mutants I147C, T156C, and K157C exhibited sufficient expression to be studied in detail using the two-electrode voltage-clamp method in Xenopus laevis oocytes and COS-7 cells. I147C was similar in function to wild-type and was not studied further. Mutation of lysine-157 to cysteine (K157C) causes loss of phloridzin and α-methyl-d-glucopyranoside (αMG) binding. These functions are restored by chemical modification with positively charged (2-aminoethyl) methanethiosulfonate hydrobromide (MTSEA). Mutation of threonine-156 to cysteine (T156C) reduces the affinity of αMG and phloridzin for T156C by ∼5-fold and ∼20-fold, respectively. In addition, phloridzin protects cysteine-156 in T156C from alkylation by MTSEA. Therefore, the presence of a positive charge or a polar residue at 157 and 156, respectively, affects sugar binding and sugar-induced Na+ currents.
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Cottrell, J. J., B. Stoll, R. K. Buddington, J. E. Stephens, L. Cui, X. Chang, and D. G. Burrin. "Glucagon-like peptide-2 protects against TPN-induced intestinal hexose malabsorption in enterally refed piglets." American Journal of Physiology-Gastrointestinal and Liver Physiology 290, no. 2 (February 2006): G293—G300. http://dx.doi.org/10.1152/ajpgi.00275.2005.
Повний текст джерелаАнотація:
Premature infants receiving chronic total parenteral nutrition (TPN) due to feeding intolerance develop intestinal atrophy and reduced nutrient absorption. Although providing the intestinal trophic hormone glucagon-like peptide-2 (GLP-2) during chronic TPN improves intestinal growth and morphology, it is uncertain whether GLP-2 enhances absorptive function. We placed catheters in the carotid artery, jugular and portal veins, duodenum, and a portal vein flow probe in piglets before providing either enteral formula (ENT), TPN or a coinfusion of TPN plus GLP-2 for 6 days. On postoperative day 7, all piglets were fed enterally and digestive functions were evaluated in vivo using dual infusion of enteral (13C) and intravenous (2H) glucose, in vitro by measuring mucosal lactase activity and rates of apical glucose transport, and by assessing the abundances of sodium glucose transporter-1 (SGLT-1) and glucose transporter-2 (GLUT2). Both ENT and GLP-2 pigs had larger intestine weights, longer villi, and higher lactose digestive capacity and in vivo net glucose and galactose absorption compared with TPN alone. These endpoints were similar in ENT and GLP-2 pigs except for a lower intestinal weight and net glucose absorption in GLP-2 compared with ENT pigs. The enhanced hexose absorption in GLP-2 compared with TPN pigs corresponded with higher lactose digestive and apical glucose transport capacities, increased abundance of SGLT-1, but not GLUT-2, and lower intestinal metabolism of [13C]glucose to [13C]lactate. Our findings indicate that GLP-2 treatment during chronic TPN maintains intestinal structure and lactose digestive and hexose absorptive capacities, reduces intestinal hexose metabolism, and may facilitate the transition to enteral feeding in TPN-fed infants.
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Wright, Ernest M., Donald D. F. Loo, and Bruce A. Hirayama. "Biology of Human Sodium Glucose Transporters." Physiological Reviews 91, no. 2 (April 2011): 733–94. http://dx.doi.org/10.1152/physrev.00055.2009.
Повний текст джерелаАнотація:
There are two classes of glucose transporters involved in glucose homeostasis in the body, the facilitated transporters or uniporters (GLUTs) and the active transporters or symporters (SGLTs). The energy for active glucose transport is provided by the sodium gradient across the cell membrane, the Na+ glucose cotransport hypothesis first proposed in 1960 by Crane. Since the cloning of SGLT1 in 1987, there have been advances in the genetics, molecular biology, biochemistry, biophysics, and structure of SGLTs. There are 12 members of the human SGLT (SLC5) gene family, including cotransporters for sugars, anions, vitamins, and short-chain fatty acids. Here we give a personal review of these advances. The SGLTs belong to a structural class of membrane proteins from unrelated gene families of antiporters and Na+ and H+ symporters. This class shares a common atomic architecture and a common transport mechanism. SGLTs also function as water and urea channels, glucose sensors, and coupled-water and urea transporters. We also discuss the physiology and pathophysiology of SGLTs, e.g., glucose galactose malabsorption and familial renal glycosuria, and briefly report on targeting of SGLTs for new therapies for diabetes.
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Wright, Ernest M., Chiara Ghezzi, and Donald D. F. Loo. "Novel and Unexpected Functions of SGLTs." Physiology 32, no. 6 (November 2017): 435–43. http://dx.doi.org/10.1152/physiol.00021.2017.
Повний текст джерелаАнотація:
It has been 30 years since the intestinal sodium glucose cotransporter SGLT1 was cloned, and, in the intervening years, there have been many advances that have influenced physiology and medicine. Among the first was that SGLT1 is the founding member of the human gene family SLC5, containing 11 diverse transporters and a glucose sensor. Equally surprising was that SGLTs are members of a structural family of cotransporters and exchangers in different gene families. This led to the conclusion that these proteins operate by a mechanism where transport involves the opening and closing of external and internal gates. The mechanism is shared by a wide variety of transporters in different structural families, e.g., the human facilitated glucose transporters (SLC2) in the huge major facilitator superfamily (MFS). Not surprising is the finding that mutations in Sglt genes cause the rare diseases glucose-galactose-malabsorption (GGM) and familial renal glucosuria (FRG). However, it was not envisaged that SGLT inhibitors would be used to treat diabetes mellitus, and these drugs may be able to treat cancer. Finally, in 2017, we have just learned that SGLT1 may be required to resist infection and to avoid recurrent pregnancy loss.
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Mendelssohn, D. C., and M. Silverman. "A D-mannose transport system in renal brush-border membranes." American Journal of Physiology-Renal Physiology 257, no. 6 (December 1, 1989): F1100—F1107. http://dx.doi.org/10.1152/ajprenal.1989.257.6.f1100.
Повний текст джерелаАнотація:
Dog renal brush-border membrane vesicles (BBMV) from whole kidney cortex contain both low-affinity, high-capacity and high-affinity, low-capacity Na-dependent D-glucose cotransporters. D-Mannose is an epimer of D-glucose, differing in structure only in the axial, rather than equatorial, orientation of the hydroxyl group at the C-2 position of the pyranose ring. Uptake experiments of radioactive sugars into BBMV by standard Millipore filtration were performed to determine whether D-mannose shares either, or both, of the D-glucose carriers or if it is transported by an independent system. Transport of D-mannose occurs into an osmotically active space and is saturable and sodium dependent with a 1:1 Na:D-mannose stoichiometry, Km of 0.063 mM, Vmax of 3.6 nmol.mg-1.min-1, 25 degrees C, and pH 7.4. When an NaSCN electrochemical gradient was present, an “overshoot” was present, indicating active cotransport. Up to 50 mM D-mannose did not inhibit sodium-dependent D-glucose or alpha-methylglucoside uptake (0.01–20 mM). Sodium-dependent D-mannose uptake was inhibited by the following compounds in order of decreasing effectiveness: fructose greater than mannoheptulose greater than 2-deoxy-D-glucose greater than 2-fluoro-2-deoxy-D-glucose much greater than phloretin, cytochalasin B, galactose, 3-O-methyl-D-glucose, and L-mannose. Phlorizin also inhibited D-mannose uptake, but the high concentration required and the fact that a competitive pattern of inhibition could not be demonstrated contrasted with its effect on D-glucose transport.(ABSTRACT TRUNCATED AT 250 WORDS)
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Vichi, Joivier, Emmanuel Salazar, Verónica Jiménez Jacinto, Leticia Olvera Rodriguez, Ricardo Grande, Edgar Dantán-González, Enrique Morett, and Armando Hernández-Mendoza. "High-throughput transcriptome sequencing and comparative analysis of Escherichia coli and Schizosaccharomyces pombe in respiratory and fermentative growth." PLOS ONE 16, no. 3 (March 17, 2021): e0248513. http://dx.doi.org/10.1371/journal.pone.0248513.
Повний текст джерелаАнотація:
In spite of increased complexity in eukaryotes compared to prokaryotes, several basic metabolic and regulatory processes are conserved. Here we explored analogies in the eubacteria Escherichia coli and the unicellular fission yeast Schizosaccharomyces pombe transcriptomes under two carbon sources: 2% glucose; or a mix of 2% glycerol and 0.2% sodium acetate using the same growth media and growth phase. Overall, twelve RNA-seq libraries were constructed. A total of 593 and 860 genes were detected as differentially expressed for E. coli and S. pombe, respectively, with a log2 of the Fold Change ≥ 1 and False Discovery Rate ≤ 0.05. In aerobic glycolysis, most of the expressed genes were associated with cell proliferation in both organisms, including amino acid metabolism and glycolysis. In contrast in glycerol/acetate condition, genes related to flagellar assembly and membrane proteins were differentially expressed such as the general transcription factors fliA, flhD, flhC, and flagellum assembly genes were detected in E. coli, whereas in S. pombe genes for hexose transporters, integral membrane proteins, galactose metabolism, and ncRNAs related to cellular stress were overexpressed. In general, our study shows that a conserved "foraging behavior" response is observed in these eukaryotic and eubacterial organisms in gluconeogenic carbon sources.
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Barcelona, Stephanie, Danusa Menegaz, and Ana Díez-Sampedro. "Mouse SGLT3a generates proton-activated currents but does not transport sugar." American Journal of Physiology-Cell Physiology 302, no. 8 (April 15, 2012): C1073—C1082. http://dx.doi.org/10.1152/ajpcell.00436.2011.
Повний текст джерелаАнотація:
Sodium-glucose cotransporters (SGLTs) are secondary active transporters belonging to the SLC5 gene family. SGLT1, a well-characterized member of this family, electrogenically transports glucose and galactose. Human SGLT3 (hSGLT3), despite sharing a high amino acid identity with human SGLT1 (hSGLT1), does not transport sugar, although functions as a sugar sensor. In contrast to humans, two different genes in mice and rats code for two different SGLT3 proteins, SGLT3a and SGLT3b. We previously cloned and characterized mouse SGLT3b (mSGLT3b) and showed that, while it does transport sugar like SGLT1, it likely functions as a physiological sugar sensor like hSGLT3. In this study, we cloned mouse SGLT3a (mSGLT3a) and characterized it by expressing it in Xenopus laevis oocytes and performing electrophysiology and sugar transport assays. mSGLT3a did not transport sugar, and sugars did not induce currents at pH 7.4, though acidic pH induced inward currents that increased in the presence of sugar. Moreover, mutation of residue 457 from glutamate to glutamine resulted in a Na+-dependent transport of sugar that was inhibited by phlorizin. To corroborate our results in oocytes, we expressed and characterized mSGLT3a in mammalian cells and confirmed our findings. In addition, we cloned, expressed, and characterized rat SGLT3a in oocytes and found characteristics similar to mSGLT3a. In summary, acidic pH induces currents in mSGLT3a, and sugar-induced currents are increased at acidic pH, but wild-type SGLT3a does not transport sugar.
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Akduman, Hasan, Dilek Dilli, and Serdar Ceylaner. "A Case of Congenital Glucose Galactose Malabsorption with a New Mutation in the SLC5A1 Gene." Journal of Pediatric Genetics, November 19, 2020. http://dx.doi.org/10.1055/s-0040-1719161.
Повний текст джерелаАнотація:
AbstractCongenital glucose-galactose malabsorption (CGGM) is an autosomal recessive disorder originating from an abnormal transporter mechanism in the intestines. It was sourced from a mutation in the SLC5A1 gene, which encodes a sodium-dependent glucose transporter. Here we report a 2-day-old girl with CGGM who presented with severe hypernatremic dehydration due to diarrhea beginning in the first hours of life. Mutation analysis revealed a novel homozygous mutation NM_000343.3 c.127G > A (p.Gly43Arg) in the SLC5A1 gene. Since CGGM can cause fatal diarrhea in the early neonatal period, timely diagnosis of the disease seems to be essential.
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Lostao, M. Pilar, Donald D. Loo, Olle Hernell, Gunnar Meeuwisse, Martin G. Martin, and Ernest M. Wright. "The Molecular Basis of Glucose Galactose Malabsorption in a Large Swedish Pedigree." Function 2, no. 5 (2021). http://dx.doi.org/10.1093/function/zqab040.
Повний текст джерелаАнотація:
Abstract Glucose-galactose malabsorption (GGM) is due to mutations in the gene coding for the intestinal sodium glucose cotransporter SGLT1 (SLC5A1). Here we identify the rare variant Gln457Arg (Q457R) in a large pedigree of patients in the Västerbotten County in Northern Sweden with the clinical phenotype of GGM. The functional effect of the Q457R mutation was determined in protein expressed in Xenopus laevis oocytes using biophysical and biochemical methods. The mutant failed to transport the specific SGLT1 sugar analog α-methyl-D-glucopyranoside (αMDG). Q457R SGLT1 was synthesized in amounts comparable to the wild-type (WT) transporter. SGLT1 charge measurements and freeze-fracture electron microscopy demonstrated that the mutant protein was inserted into the plasma membrane. Electrophysiological experiments, both steady-state and presteady-state, demonstrated that the mutant bound sugar with an affinity lower than the WT transporter. Together with our previous studies on Q457C and Q457E mutants, we established that the positive charge on Q457R prevented the translocation of sugar from the outward-facing to inward-facing conformation. This is contrary to other GGM cases where missense mutations caused defects in trafficking SGLT1 to the plasma membrane. Thirteen GGM patients are now added to the pedigree traced back to the late 17th century. The frequency of the Q457R variant in Västerbotten County genomes, 0.0067, is higher than in the general Swedish population, 0.0015, and higher than the general European population, 0.000067. This explains the high number of GGM cases in this region of Sweden.
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Bazzone, Andre, Rocco Zerlotti, Maria Barthmes, and Niels Fertig. "Functional characterization of SGLT1 using SSM-based electrophysiology: Kinetics of sugar binding and translocation." Frontiers in Physiology 14 (February 7, 2023). http://dx.doi.org/10.3389/fphys.2023.1058583.
Повний текст джерелаАнотація:
Beside the ongoing efforts to determine structural information, detailed functional studies on transporters are essential to entirely understand the underlying transport mechanisms. We recently found that solid supported membrane-based electrophysiology (SSME) enables the measurement of both sugar binding and transport in the Na+/sugar cotransporter SGLT1 (Bazzone et al, 2022a). Here, we continued with a detailed kinetic characterization of SGLT1 using SSME, determining KM and KDapp for different sugars, kobs values for sugar-induced conformational transitions and the effects of Na+, Li+, H+ and Cl− on sugar binding and transport. We found that the sugar-induced pre-steady-state (PSS) charge translocation varies with the bound ion (Na+, Li+, H+ or Cl−), but not with the sugar species, indicating that the conformational state upon sugar binding depends on the ion. Rate constants for the sugar-induced conformational transitions upon binding to the Na+-bound carrier range from 208 s−1 for D-glucose to 95 s−1 for 3-OMG. In the absence of Na+, rate constants are decreased, but all sugars bind to the empty carrier. From the steady-state transport current, we found a sequence for sugar specificity (Vmax/KM): D-glucose > MDG > D-galactose > 3-OMG > D-xylose. While KM differs 160-fold across tested substrates and plays a major role in substrate specificity, Vmax only varies by a factor of 1.9. Interestingly, D-glucose has the lowest Vmax across all tested substrates, indicating a rate limiting step in the sugar translocation pathway following the fast sugar-induced electrogenic conformational transition. SGLT1 specificity for D-glucose is achieved by optimizing two ratios: the sugar affinity of the empty carrier for D-glucose is similarly low as for all tested sugars (KD,Kapp = 210 mM). Affinity for D-glucose increases 14-fold (KD,Naapp = 15 mM) in the presence of sodium as a result of cooperativity. Apparent affinity for D-glucose during transport increases 8-fold (KM = 1.9 mM) compared to KD,Naapp due to optimized kinetics. In contrast, KM and KDapp values for 3-OMG and D-xylose are of similar magnitude. Based on our findings we propose an 11-state kinetic model, introducing a random binding order and intermediate states corresponding to the electrogenic transitions detected via SSME upon substrate binding.