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Related Concept Videos

Lipids as Anchors01:32

Lipids as Anchors

In the plasma membrane, the lipids forming the bilayer can also act as an anchor to tether proteins to the membrane. The three main types of lipid anchors found in eukaryotes are – prenyl groups, fatty acyl groups, and glycosylphosphatidylinositol or GPI groups. Prenyl and fatty acyl groups act as anchors on the cytosolic surface of the membrane, whereas GPI anchors proteins on the extracellular side.
The carboxy-terminal of most of the prenylated proteins, such as Ras proteins, contains the...
Integrins01:10

Integrins

Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
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Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Anchoring Junctions01:03

Anchoring Junctions

Anchoring junctions are multiprotein complexes that help cells connect to other cells and the extracellular matrix. Anchoring junctions are present on the lateral and basal surfaces of cells, providing strong and flexible connections. Focal adhesions are often formed due to cell interactions with the ECM substrata, which initiate signal transduction via kinase cascades and other mechanisms. Together, they provide stability and tissue integrity. There are three types of anchoring junctions:...
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
The Integrin family of proteins is primarily  involved in a...
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...

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Updated: Jul 17, 2026

Analysis of Physiologic E-Selectin-Mediated Leukocyte Rolling on Microvascular Endothelium
14:16

Analysis of Physiologic E-Selectin-Mediated Leukocyte Rolling on Microvascular Endothelium

Published on: February 11, 2009

Glycolipids support E-selectin-specific strong cell tethering under flow.

M M Burdick1, B S Bochner, B E Collins

  • 1Department of Chemical Engineering, Johns Hopkins University, Baltimore, Maryland 21218, USA.

Biochemical and Biophysical Research Communications
|May 26, 2001
PubMed
Summary

Glycosphingolipids with specific structures act as ligands for E-selectin, mediating cell rolling. However, they do not bind to P-selectin, indicating selective interactions in cell adhesion.

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Last Updated: Jul 17, 2026

Analysis of Physiologic E-Selectin-Mediated Leukocyte Rolling on Microvascular Endothelium
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Analysis of Physiologic E-Selectin-Mediated Leukocyte Rolling on Microvascular Endothelium

Published on: February 11, 2009

Ligand Nano-cluster Arrays in a Supported Lipid Bilayer
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Published on: April 23, 2017

Imaging Molecular Adhesion in Cell Rolling by Adhesion Footprint Assay
08:24

Imaging Molecular Adhesion in Cell Rolling by Adhesion Footprint Assay

Published on: September 27, 2021

Area of Science:

  • Cellular Biology
  • Biochemistry
  • Immunology

Background:

  • Selectins are cell adhesion molecules crucial for immune cell trafficking.
  • Glycosphingolipids are complex lipids involved in cell surface recognition.
  • Understanding selectin-ligand interactions is vital for studying inflammatory diseases.

Purpose of the Study:

  • To investigate the role of glycosphingolipids as ligands for E-selectin and P-selectin.
  • To determine the functional differences in cell adhesion mediated by these selectins.

Main Methods:

  • Perfusion of Chinese hamster ovary (CHO) cells expressing E-selectin (CHO-E) or P-selectin (CHO-P) over immobilized alpha2,3-sialyl Lewis X (alpha2,3-sLe(x)) glycosphingolipids.
  • Analysis of cell tethering and rolling interactions under varying shear stress, selectin, and ligand densities.
  • Application of a stochastic model to quantify cell rolling parameters.
  • Detachment assays to assess adhesive strengths.

Main Results:

  • CHO-E cells exhibited extensive tethering and stable rolling on alpha2,3-sLe(x) glycosphingolipids, but not on alpha2,6-sLe(x).
  • CHO-P cells showed limited, fast rolling on alpha2,3-sLe(x) glycosphingolipids.
  • Stochastic modeling revealed differences in bond release dynamics between CHO-E and CHO-P cells.
  • Detachment assays confirmed stronger adhesion of CHO-E cells to the glycosphingolipid ligand.

Conclusions:

  • Glycosphingolipids expressing alpha2,3-sialyl Lewis X are functional ligands for E-selectin, mediating significant cell tethering and rolling.
  • P-selectin interacts weakly with these glycosphingolipids, supporting only limited cell rolling.
  • These findings highlight the selectivity of E-selectin and P-selectin binding to specific glycosphingolipid structures.