Related Experiment Video

Updated: Jun 6, 2026

A Mouse Model to Investigate the Role of Cancer-Associated Fibroblasts in Tumor Growth
06:35

A Mouse Model to Investigate the Role of Cancer-Associated Fibroblasts in Tumor Growth

Published on: December 22, 2020

Galectin-1 sensitizes carcinoma cells to anoikis via the fibronectin receptor α5β1-integrin

H Sanchez-Ruderisch1, K M Detjen, M Welzel

  • 1Medizinische Klinik m.S. Hepatologie und Gastroenterologie, Charité-Universitätsmedizin Berlin, Campus Virchow-Klinikum, Berlin, Germany.

Cell Death and Differentiation
|November 30, 2010
PubMed

Insights

Endogenous lectin galectin-1 (Gal-1) induces apoptosis in anoikis-resistant carcinoma cells by binding to the fibronectin receptor α(5)β(1)-integrin. This interaction is glycan-dependent, with sialylation acting as a negative regulator.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Cancer Research

Background:

  • Anoikis resistance is a key characteristic of transformed epithelial cells.
  • Galectin-1 (Gal-1) is an endogenous lectin involved in various cellular processes.
  • Integrins, such as α(5)β(1)-integrin, play crucial roles in cell adhesion and signaling.

Purpose of the Study:

  • To investigate the role of galectin-1 in promoting apoptosis in anoikis-resistant carcinoma cells.
  • To elucidate the specific molecular interactions involved in Gal-1-induced anoikis.
  • To understand the influence of cell surface glycans on Gal-1 function.

Main Methods:

  • Treatment of carcinoma cell lines with galectin-1.
  • Analysis of α(5)β(1)-integrin expression and binding.
  • Co-precipitation assays to study protein interactions.
  • Glycan analysis and desialylation treatments.
  • Inhibition studies using filipin and caspase-8 inhibitors.

Main Results:

  • Galectin-1 treatment promoted apoptosis in anoikis-resistant cells via interaction with α(5)β(1)-integrin.
  • Gal-1 binding and anoikis stimulation correlated with α(5)β(1)-integrin expression.
  • The interaction was dependent on cell surface glycans, with α2,6-sialylation acting as an inhibitory signal.
  • Desialylation enhanced Gal-1 binding and anoikis induction.
  • Gal-1-induced anoikis was dependent on α(5)β(1)-integrin internalization via cholesterol-enriched microdomains and caspase-8 activation.

Conclusions:

  • Galectin-1/α(5)β(1)-integrin interaction is a critical mechanism for inducing apoptosis in anoikis-resistant carcinoma cells.
  • Integrin sialylation represents a potential mechanism for carcinoma cells to evade Gal-1-mediated apoptosis and maintain epithelial integrity.
  • Targeting the Gal-1/α(5)β(1)-integrin pathway or modulating integrin sialylation may offer therapeutic strategies for cancer treatment.

Related Concept Videos

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...
Activation of Integrins01:15

Activation of Integrins

Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
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...
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.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Mitogens and the Cell Cycle02:38

Mitogens and the Cell Cycle

Mitogens and their receptors play a crucial role in controlling the progression of the cell cycle. However, the loss of mitogenic control over cell division leads to tumor formation. Therefore, mitogens and mitogen receptors play an important role in cancer research. For instance, the epidermal growth factor (EGF) - a type of mitogen and its transmembrane receptor (EGFR), decides the fate of the cell's proliferation. When EGF binds to EGFR, a member of the ErbB family of tyrosine kinase...
Adaptive Mechanisms in Cancer Cells02:53

Adaptive Mechanisms in Cancer Cells

Cancer cells accumulate genetic changes at an abnormally rapid rate due to the defects in the DNA repair mechanisms. From an evolutionary perspective, such genetic instability is advantageous for cancer development. Mutant cell lines accumulate a series of beneficial mutations that contribute to their progression into cancer.
Some of the advantages that cancer cells have on normal cells include - enhanced ability to divide without terminally differentiating, induce new blood vessel formation,...