Related Experiment Video

Updated: Jun 7, 2026

Efficient Retroviral Transduction and Competitive Homing for Investigating GPCR-Mediated T-Cell Localization in Diverse Tissue Microenvironments
09:12

Efficient Retroviral Transduction and Competitive Homing for Investigating GPCR-Mediated T-Cell Localization in Diverse Tissue Microenvironments

Published on: March 28, 2025

Intercellular transfer regulation of the paracrine activity of GPI-anchored Cripto-1 as a Nodal co-receptor

Kazuhide Watanabe1, David S Salomon

  • 1Mammary Biology & Tumorigenesis Laboratory, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.

Biochemical and Biophysical Research Communications
|November 9, 2010
PubMed

Insights

Cripto-1 (CR-1), a co-receptor for Nodal, transfers between cells in its membrane-bound form. This intercellular transfer enhances cell adhesion and may explain CR-1's paracrine signaling activity.

Area of Science:

  • Cell Biology
  • Developmental Biology
  • Glycoprotein Signaling

Background:

  • Cripto-1 (CR-1) is a GPI-anchored glycoprotein essential for Nodal signaling.
  • CR-1's paracrine function is mediated by a poorly understood cellular mechanism.
  • Paracrine activity requires membrane-bound CR-1, but not soluble forms.

Purpose of the Study:

  • To elucidate the cellular mechanism behind CR-1's paracrine activity.
  • To investigate the differences between membrane-bound and soluble CR-1.
  • To determine how CR-1 expression affects cell surface properties and intercellular communication.

Main Methods:

  • Comparative analysis of post-translational modifications between membrane-bound and soluble CR-1.
  • Flow cytometry to assess intercellular transfer of CR-1.
  • Microscopy to observe cell morphology, membrane extensions, and fragment generation.
  • Cell adhesion assays.

Main Results:

  • Minimal biochemical differences were found between membrane-bound and soluble CR-1.
  • Flow cytometry confirmed intercellular transfer of membrane-bound CR-1.
  • CR-1-expressing cells showed increased membrane extensions, fragment release, and cellular adhesion.
  • CR-1 expression alters plasma membrane physiochemical properties.

Conclusions:

  • Intercellular transfer of membrane-bound CR-1 is a key mechanism for its paracrine activity.
  • CR-1 expression enhances cell adhesion and membrane dynamics.
  • Altered membrane properties facilitate the transfer of signaling components, explaining CR-1's paracrine function.

More Related Videos

Characterizing Modulators of Protease-Activated Receptors with a Calcium Mobilization Assay Using a Plate Reader07:13

Characterizing Modulators of Protease-Activated Receptors with a Calcium Mobilization Assay Using a Plate Reader

Published on: May 24, 2024

A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators07:41

A Kinetic Fluorescence-based Ca2+ Mobilization Assay to Identify G Protein-coupled Receptor Agonists, Antagonists, and Allosteric Modulators

Published on: February 20, 2018

Related Concept Videos

IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and produces two-second...
GPI Anchoring of Proteins in the ER Membrane01:29

GPI Anchoring of Proteins in the ER Membrane

GPI-anchoring is a post-translational, reversible protein modification that is ubiquitous in eukaryotes. Such proteins are primarily present on the exoplasmic leaflet of the plasma membrane.
GPI-anchor structure
A sequence of 11 enzymatic reactions results in the synthesis of the complete GPI anchor consisting of a hydrophobic and a hydrophilic portion. The hydrophobic portion comprises phosphatidylinositol, while the hydrophilic part comprises polar groups like phosphoethanolamine,...
GPCRs Regulate Adenylyl Cylase Activity01:09

GPCRs Regulate Adenylyl Cylase Activity

Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of cells.
Two...
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...
G-protein Coupled Receptors01:21

G-protein Coupled Receptors

G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.
G-protein Coupled Receptors01:21

G-protein Coupled Receptors

G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.