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Related Concept Videos

The Extracellular Matrix01:42

The Extracellular Matrix

In order to maintain tissue organization, many animal cells are surrounded by structural molecules that make up the extracellular matrix (ECM). Together, the molecules in the ECM maintain the structural integrity of tissue as well as the remarkable specific properties of certain tissues.Composition of the Extracellular MatrixThe extracellular matrix (ECM) is commonly composed of ground substance, a gel-like fluid, fibrous components, and many structurally and functionally diverse molecules.
The Extracellular Matrix01:29

The Extracellular Matrix

Overview
In order to maintain tissue organization, many animal cells are surrounded by structural molecules that make up the extracellular matrix (ECM). Together, the molecules in the ECM maintain the structural integrity of tissue as well as the remarkable specific properties of certain tissues.
Composition of the Extracellular Matrix
The extracellular matrix (ECM) is commonly composed of ground substance, a gel-like fluid, fibrous components, and many structurally and functionally diverse...
Matrix Proteoglycans and Glycoproteins01:21

Matrix Proteoglycans and Glycoproteins

Proteoglycans are extensively glycosylated proteins, commonly found in the extracellular matrix, interwoven with collagen fibers. Hyaline cartilage, the most common type of cartilage in the body, consists of short and dispersed collagen fibers associated with large amounts of proteoglycans. These proteoglycans have long negative charges that attract cations, which in turn attract water molecules. This influx of ions and water molecules swells up the proteoglycan like a water-soaked gel that can...
Fibronectins Connect Cells with ECM01:25

Fibronectins Connect Cells with ECM

Fibronectin is an adhesive glycoprotein present in the extracellular matrix of embryogenic and adult tissue. These molecules primarily aid in regulating cell motility and attachment. A fibronectin molecule is composed of two identical polypeptide chains attached to each other by a pair of disulfide bonds at the C-terminal.
Both proteoglycans and collagen are attached to fibronectin proteins, which, in turn, are attached to integrin proteins. These integrin proteins interact with transmembrane...
Overview of Cell-Matrix Interactions01:24

Overview of Cell-Matrix Interactions

The extracellular matrix or ECM holds cells together to form a tissue and allows the cells within the tissue to communicate. ECM comprises proteins such as fibronectin, collagen, laminin, etc. The most abundant protein in this space is collagen. Collagen fibers are interwoven with carbohydrate-containing protein molecules called proteoglycans. ECM allows cell migration and provides a structural scaffold at cell adhesion that anchors the cell when the extracellular matrix proteins interact with...
Protein Diffusion in the Membrane01:24

Protein Diffusion in the Membrane

Proteins show rotational as well as lateral diffusion across the membrane. The lateral diffusion of proteins was confirmed through the cell fusion experiment where mouse and human cells were fused, resulting in hybrid cells. When the human and mouse cells fused, the specific membrane proteins on human and mouse cells were marked with the red and green-fluorescent markers, respectively. Initially, the red and green fluorescence was located on the respective hemisphere of the cell. As time...

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FGF9 monomer-dimer equilibrium regulates extracellular matrix affinity and tissue diffusion.

Masayo Harada1, Hirotaka Murakami, Akihiko Okawa

  • 1RIKEN Research Center for Allergy and Immunology, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama, Kanagawa 230-0045, Japan.

Nature Genetics
|February 17, 2009
PubMed
Summary
This summary is machine-generated.

A mutation in the Fibroblast Growth Factor 9 (FGF9) gene causes Elbow knee synostosis (Eks) in mice, leading to joint and cranial suture fusion. This FGF9 mutation disrupts protein function, causing developmental defects.

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Area of Science:

  • Developmental Biology
  • Genetics
  • Molecular Biology

Background:

  • The Elbow knee synostosis (Eks) mouse mutant exhibits joint and cranial suture fusion.
  • Understanding the genetic basis of synostosis is crucial for developmental research.

Purpose of the Study:

  • To identify the genetic cause of the Eks mutation.
  • To elucidate the molecular mechanisms underlying FGF9 signaling in joint and suture development.

Main Methods:

  • Genetic analysis to identify the causative mutation in the Fgf9 gene.
  • Biochemical assays to assess FGF9 protein homodimerization and heparin binding.
  • Analysis of FGF9(Eks) protein diffusion and signaling in developing tissues.

Main Results:

  • A missense mutation in the Fgf9 gene was identified as the cause of the Eks phenotype.
  • The Eks mutation impairs FGF9 protein homodimerization and reduces heparin binding affinity.
  • Altered FGF9(Eks) protein exhibits increased diffusion, leading to ectopic signaling and repressed joint/suture development.

Conclusions:

  • FGF9 protein homodimerization and heparan sulfate proteoglycan binding are critical for limiting FGF9 signaling range.
  • Disruption of these interactions leads to developmental abnormalities like synostosis.
  • This study reveals a novel regulatory mechanism for FGF9 signaling in embryonic development.