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Related Concept Videos

Glucose Transporters01:27

Glucose Transporters

Glucose transporters facilitate the transport of glucose across the cell membrane. In addition to glucose, some glucose transporters can also aid the movement of other hexoses such as fructose, mannose, and galactose.
Facilitated diffusion-glucose transporters (GLUTs) are encoded by the solute-linked carrier (SLC) family 2, subfamily A gene family, or SLC2A. The 14 GLUT protein members are distributed into three classes:
Oligosaccharide Assembly01:24

Oligosaccharide Assembly

Protein glycosylation starts in the ER lumen and continues in the Golgi apparatus. Glycosyltransferases catalyze the addition of sugar molecules or glycosylation of proteins. Usually, these enzymes add sugars to the hydroxyl groups of selected serine or threonine residues to form O-linked glycans or the amino groups of asparagine residues to form N-linked glycans. Different positions on the same polypeptide chain can contain differently linked glycans.
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Glucose Absorption Into the Small Intestine01:26

Glucose Absorption Into the Small Intestine

Complex carbohydrates consumed cannot be absorbed into the small intestine in their original form. First, they must be hydrolyzed to a monosaccharide form such as glucose or galactose. These monosaccharides are then transported across the intestinal membrane and into the blood via transcellular transport. The intestinal epithelial cells allow the movement of these monosaccharides with a defined 'entry' through membrane transporter proteins present on their apical membrane and 'exit' via the...
Protein Glycosylation01:25

Protein Glycosylation

Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
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Bioinformatics Resources for the Study of Glycan-Mediated Protein Interactions
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Galectin 3-β-galactobiose interactions.

A P Gunning1, C Pin, V J Morris

  • 1Institute of Food Research, Norwich Research Park, Norwich NR4 7 UA, UK.

Carbohydrate Polymers
|December 11, 2012
PubMed
Summary
This summary is machine-generated.

Modified citrus pectin inhibits cancer metastasis by targeting the pro-metastatic protein galectin-3 (Gal3). This study quanties the specific binding interactions between Gal3 and pectin components, revealing potential therapeutic mechanisms.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cancer Research

Background:

  • Galectin-3 (Gal3) is a protein implicated in promoting cancer metastasis.
  • Understanding the molecular interactions of Gal3 is crucial for developing anti-metastatic therapies.

Purpose of the Study:

  • To investigate the specific binding interactions between the disaccharide β-galactobiose and galectin-3 (Gal3) using force spectroscopy.
  • To provide insights into the mechanism by which modified citrus pectin may inhibit cancer metastasis by targeting Gal3.

Main Methods:

  • Utilized force spectroscopy to probe the interaction between β-galactobiose and Gal3.
  • Quantified key interaction parameters such as off-rate dissociation constant (k(off)) and interaction distance (x).

Main Results:

  • Specific interactions between β-galactobiose and Gal3 were characterized.
  • An off-rate dissociation constant (k(off)) of 0.33 s⁻¹ and an interaction distance (x) of 0.2 nm at zero applied force were determined.
  • These parameters suggest an interaction lifetime of approximately 3.0 seconds.

Conclusions:

  • The findings support the hypothesis that modified citrus pectin inhibits cancer metastasis by interfering with Gal3 function.
  • Pectin-derived galactan sidechains likely facilitate binding to Gal3, thereby inhibiting its pro-metastatic roles.