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Related Concept Videos

Cell Adhesion Molecules - Types and Functions01:20

Cell Adhesion Molecules - Types and Functions

Cell adhesion molecules (CAMs) are pivotal to multicellularity and the coordinated functioning of tissues and organ systems. They enable physical interactions between cells and provide mechanical strength to tissues. They also function as receptors for signal transmission across the plasma membrane. The CAMs are broadly classified into four families - integrins, cadherins, selectins, and immunoglobulin-like CAMs (IgCAMs).
CAM Families
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Cell Adhesion Molecules - Types and Functions01:20

Cell Adhesion Molecules - Types and Functions

Cell adhesion molecules (CAMs) are pivotal to multicellularity and the coordinated functioning of tissues and organ systems. They enable physical interactions between cells and provide mechanical strength to tissues. They also function as receptors for signal transmission across the plasma membrane. The CAMs are broadly classified into four families - integrins, cadherins, selectins, and immunoglobulin-like CAMs (IgCAMs).
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Cadherins in Tissue Organization01:19

Cadherins in Tissue Organization

The cadherins are a superfamily of cell adhesion molecules comprising over 180 variants, with specific tissues expressing a particular combination of cadherin types. Cadherins generally exhibit homophilic binding; i.e., cadherins on one cell bind to cadherins of the same or closely related type on another cell. Thus, cells of the same type have a specific affinity to bind to each other and sort themselves into clusters to form tissues.
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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...
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,...
Structure of Cadherins01:25

Structure of Cadherins

The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This diversity of cadherins...

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Heparan sulfate chain valency controls syndecan-4 function in cell adhesion.

Sandeep Gopal1, Adam Bober, James R Whiteford

  • 1Department of Biomedical Sciences, University of Copenhagen, 2200 Copenhagen N, Denmark.

The Journal of Biological Chemistry
|February 16, 2010
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Syndecan-4 is crucial for organizing the actin cytoskeleton in fibroblasts. Its heparan sulfate chains and ligand interaction valency are key for proper alpha-smooth muscle actin bundling and cell adhesion.

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Area of Science:

  • Cell Biology
  • Biochemistry
  • Biophysics

Background:

  • Syndecan-4 is a transmembrane proteoglycan involved in cell adhesion and migration.
  • The actin cytoskeleton is essential for cell structure, movement, and mechanical force generation.
  • Alpha-smooth muscle actin (α-SMA) is a key component of the actin cytoskeleton, particularly in stress fibers.

Purpose of the Study:

  • To investigate the role of syndecan-4 in organizing the actin cytoskeleton in fibroblasts.
  • To determine the specific structural requirements of syndecan-4 for regulating alpha-smooth muscle actin organization.
  • To elucidate the contribution of heparan sulfate chains and ligand interaction valency to syndecan-4 function.

Main Methods:

  • Generation of syndecan-4 null fibroblasts.
  • Re-expression of full-length and mutant syndecan-4 constructs.
  • Analysis of actin cytoskeleton organization, specifically alpha-smooth muscle actin bundling.
  • Assessment of focal contact/adhesion size and focal adhesion kinase (FAK) phosphorylation.
  • Functional studies involving antibody-mediated clustering of syndecan-4.

Main Results:

  • Fibroblasts lacking syndecan-4 exhibit disorganized alpha-smooth muscle actin.
  • Re-expression of full-length syndecan-4 restores alpha-smooth muscle actin organization.
  • Multiple heparan sulfate chains on syndecan-4 are essential for this function.
  • The cytoplasmic V region of syndecan-4 is required, but PDZ protein interactions are not.
  • Antibody-mediated clustering of syndecan-4 with fewer chains rescues the phenotype, highlighting ligand interaction valency.
  • Reduced focal contact/adhesion size and FAK phosphorylation correlate with impaired syndecan-4 function.

Conclusions:

  • Syndecan-4 plays a critical role in regulating the actin cytoskeleton organization in fibroblasts.
  • The number of heparan sulfate chains and the valency of ligand interactions are key determinants of syndecan-4's function in actin organization.
  • Syndecan-4 influences cell adhesion dynamics and signaling pathways, including FAK phosphorylation.