Relevant bibliographies by topics / Sodium-galactose transporter

Contents

  1. Journal articles
  2. Book chapters

Academic literature on the topic 'Sodium-galactose transporter'

Author: Grafiati
Published: 14 March 2023

Create a spot-on reference in APA, MLA, Chicago, Harvard, and other styles

Select a source type:

Consult the lists of relevant articles, books, theses, conference reports, and other scholarly sources on the topic 'Sodium-galactose transporter.'

Next to every source in the list of references, there is an 'Add to bibliography' button. Press on it, and we will generate automatically the bibliographic reference to the chosen work in the citation style you need: APA, MLA, Harvard, Chicago, Vancouver, etc.

You can also download the full text of the academic publication as pdf and read online its abstract whenever available in the metadata.

Journal articles on the topic "Sodium-galactose transporter"

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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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.
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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.
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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.
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
6

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.

Full text
Abstract:
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.
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
Abstract:
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.
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
9

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.

Full text
Abstract:
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.
APA, Harvard, Vancouver, ISO, and other styles
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.

Full text
APA, Harvard, Vancouver, ISO, and other styles
More sources

Book chapters on the topic "Sodium-galactose transporter"

1

Mardones, Lorena, and Marcelo Villagrán. "Lactose Synthesis." In Lactose and Lactose Derivatives. IntechOpen, 2020. http://dx.doi.org/10.5772/intechopen.91399.

Full text
Abstract:
This chapter is related to lactose synthesis, its chemistry, regulation, and differences between species, especially in cattle. Lactose synthesis takes place in the Golgi apparatus of mammary epithelial cells (MEC) by the lactose synthase (LS) enzyme complex from two precursors, glucose and UDP-galactose. The enzyme complex is formed by galactosyltransferase, and it is associated with α-lactalbumin. Importantly, the lactose secreted determines the volume of milk produced, due to its osmotic properties. Milk contains 5% lactose and 80% water, percentages that remain constant during lactation in the different mammalian species. The low variation in milk lactose content indicates that lactose synthesis remains constant throughout the period of lactation and that is highly conserved in all mammals. Lactose synthesis is initiated during the first third of the pregnancy, increasing after birth and placenta removal. Different glucose transporters have been involved in mammary glucose uptake, mainly facilitative glucose transporters GLUT1, GLUT8, and GLUT12 and sodium-glucose transporter SGLT1, with more or less participation depending on mammal species.
APA, Harvard, Vancouver, ISO, and other styles
2

Gee, J. M., M. S. DuPont, and I. T. Johnson. "Stability of Flavonol Glycosides During Digestion and Evidence for Interaction with the Sodium Dependent Glucose/Galactose Transport Pathway." In Dietary Anticarcinogens and Antimutagens, 69–72. Elsevier, 2000. http://dx.doi.org/10.1533/9781845698188.2.69.

Full text
APA, Harvard, Vancouver, ISO, and other styles
You might also be interested in the extended bibliographies on the topic 'Sodium-galactose transporter' for particular source types:
Journal articles
We offer discounts on all premium plans for authors whose works are included in thematic literature selections. Contact us to get a unique promo code!

To the bibliography