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Selectins

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...

Intracellular Signaling Affects Focal Adhesions

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.
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Immunoglobulin-like Cell Adhesion Molecules

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Immunoglobulin-like cell adhesion molecules or Ig-CAMs are a versatile group of cell surface glycoproteins belonging to the immunoglobulin protein superfamily. Ig-CAMs possess the characteristic immunoglobulin protein domains and other domains such as the fibronectin type III domain. The Ig domains are glycosylated to varying degrees in different Ig-CAMs.
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Cell Adhesion Molecules - Types and Functions

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Invadosome is a broad category of cell surface structures with proteolytic activity that degrades the extracellular matrix (ECM). Invadosomes are present in normal cell types, including macrophages, endothelial cells, and neurons, as well as tumor cells. Although the macrophage podosomes and tumor cell invadopodia are classified as invadosomes, they have different structures, molecular pathways, and functions. Podosomes are short structures that last for a few minutes. However, invadopodia can...

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Related Experiment Video

Updated: May 21, 2026

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

Published on: June 13, 2014

LRP-1--CD44, a new cell surface complex regulating tumor cell adhesion.

Gwenn Perrot¹, Benoit Langlois, Jérôme Devy

¹Université de Reims Champagne-Ardenne, Unité MEDyC, CNRS FRE 3481, Laboratoire SiRMa, Campus Moulin de la Housse, Reims, France.

Molecular and Cellular Biology

|June 20, 2012

Summary

Low-density lipoprotein receptor-related protein 1 (LRP-1) regulates CD44 cell surface levels. LRP-1 blockade increases CD44, promoting tumor cell adhesion, critical for cancer progression.

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Static Adhesion Assay for the Study of Integrin Activation in T Lymphocytes

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Area of Science:

Cell Biology
Molecular Biology
Cancer Research

Background:

Low-density lipoprotein receptor-related protein 1 (LRP-1) is an endocytic receptor involved in extracellular matrix clearance.
Initially linked to antitumor effects, LRP-1's role in cancer progression is now being re-evaluated, particularly its influence on cell adhesion.

Purpose of the Study:

To investigate the relationship between LRP-1 and CD44 in tumor cells.
To elucidate the mechanism of LRP-1-mediated CD44 internalization and its impact on tumor cell adhesion.

Main Methods:

LRP-1 silencing and receptor-associated protein (RAP) treatment to observe CD44 cell surface accumulation.
Co-immunoprecipitation to study LRP-1 and CD44 interaction.
Analysis of CD44 trafficking using EEA1 and LAMP-1 labeling.
Assessment of internalization pathways (clathrin-coated pits, lipid rafts) and effect of hyperosmotic conditions and cholesterol depletion.
CD44 silencing to evaluate its role in RAP-induced tumor cell attachment.

Main Results:

LRP-1 silencing or RAP treatment caused CD44 accumulation on tumor cell surfaces.
A direct interaction between LRP-1 and CD44 was confirmed, with the fourth ligand-binding cluster of LRP-1 being crucial for binding.
Internalized CD44 is trafficked via early endosomes to lysosomes in an LRP-1-dependent manner, primarily through clathrin-coated pits.
CD44 accumulation on the cell surface upon LRP-1 blockade was responsible for increased tumor cell adhesion.

Conclusions:

LRP-1 plays a critical role in regulating CD44 internalization and cell surface expression.
LRP-1-mediated CD44 trafficking is essential for controlling tumor cell adhesion properties.
Targeting the LRP-1-CD44 interaction may offer a novel strategy for modulating cancer cell adhesion and progression.