Recognition of galactan components of pectin by galectin-3

A Patrick Gunning1, Roy J M Bongaerts, Victor J Morris

  • 1Institute of Food Research, Norwich Research Park, Colney, Norwich NR4 7UA, UK. patrick.gunning@bbsrc.ac.uk

Insights

Modified pectin fragments show anticancer potential by inhibiting galectin 3 (Gal3). Researchers identified specific pectin galactan binding to Gal3, suggesting neutral sugar side chains hold bioactivity for cancer therapy development.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Carbohydrate Chemistry

Background:

  • Modified pectin exhibits anticancer properties, potentially by targeting galectin 3 (Gal3).
  • The precise structural elements of pectin responsible for this bioactivity remain unclear.
  • Galectin 3 plays a critical role in cancer progression and metastasis.

Purpose of the Study:

  • To elucidate the structural basis of pectin's anticancer activity.
  • To demonstrate direct binding between pectin components and galectin 3.
  • To identify specific pectin structures that can be optimized for therapeutic use.

Main Methods:

  • Utilized fluorescence microscopy to visualize interactions.
  • Employed flow cytometry for quantitative analysis.
  • Applied force spectroscopy to probe binding mechanics.

Main Results:

  • Confirmed specific binding between a pectin galactan and recombinant human galectin 3.
  • Provided the first direct evidence of this molecular interaction.
  • Indicated that neutral sugar side chains of pectin are key to bioactivity.

Conclusions:

  • Pectin's anticancer activity is linked to the binding of its neutral sugar side chains to galectin 3.
  • These specific side chains represent a promising target for developing novel anticancer agents.
  • Isolation and modification of these pectin components could enhance therapeutic efficacy.

Related Concept Videos

Cellulose and Pectic Polysaccharides01:15

Cellulose and Pectic Polysaccharides

Every plant cell has a cell wall that protects the cell, provides structural support, and gives the cell shape. Cellulose, the main structural component of the plant cell wall, makes up over 30% of plant matter. It is the most abundant organic compound on earth.  Cellulose is an unbranched polysaccharide composed of linear chains of glucose molecules linked by β (1→4) glycosidic bonds.
As a cell matures, its cell wall specializes according to its type. For example, the parenchyma cells of...
Cell Adhesion in Plants01:14

Cell Adhesion in Plants

Plants have rigid cell walls that are made up of cell wall polysaccharides that mediate cell-cell adhesion. The primary cell walls of plants consist of two independent and interacting polysaccharide networks: a pectin matrix that embeds the second network comprising cellulose and hemicelluloses.
Pectins are complex heteropolymers mainly composed of negatively-charged α-D-glucopyranosyl uronic acid and some neutral glycosyl residues such as α-L-rhamnopyranose, α-L-arabinofuranose, and...
Proteoglycans01:05

Proteoglycans

Glycans, a class of complex heterogeneous molecules, can be covalently attached to proteins to form glycosylated proteins that regulate various physiological and pathological processes. Glycosylated proteins or glycoproteins comprise N-linked and O-linked oligosaccharides. O-glycosylation is the most common type of protein glycosylation. Here, glycans attach to the oxygen atom of the hydroxyl groups of Serine or Threonine residues. O-linked glycosylation occurs later in protein processing,...
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.
Multiple sugar molecules that may or may...
Selectins01:25

Selectins

Cell adhesion is  an essential aspect of multicellularity. While stable cell interactions usually occur between cells of the same type, transient cell interactions occur between cells of different tissue types, such as between neutrophils and endothelial cells. Selectins are one class of cell adhesion molecules (CAMs) that bind carbohydrate ligands to form transient cell adhesion. They are rod-like proteins with a long extracellular part of variable length ending with the lectin domain, which...
Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...