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Related Concept Videos

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...
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...
Cell-matrix's Response to Mechanical Forces01:13

Cell-matrix's Response to Mechanical Forces

In animal cells, the extracellular matrix allows cells within tissues to withstand external stresses and transmits signals from the outside of the cell to the inside. The extracellular matrix is extensive, and its composition varies between different types of tissues. For example, the reticular fibers and ground substance make up the ECM in loose connective tissue, while collagen and bone minerals make up the ECM of bone tissue. 
Anchoring junctions mechanically attach a cell to the...
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...
Immunoglobulin-like Cell Adhesion Molecules01:31

Immunoglobulin-like Cell Adhesion Molecules

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.
Ig-CAMs exhibit either homophilic binding (to other Ig-CAMs) or heterophilic binding (to other ligands such as integrins). While most Ig-CAMs...
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,...

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Preparation of 3D Collagen Gels and Microchannels for the Study of 3D Interactions In Vivo
10:24

Preparation of 3D Collagen Gels and Microchannels for the Study of 3D Interactions In Vivo

Published on: May 9, 2016

Evolution of collagen-based adhesion systems.

Jyrki Heino1, Mikko Huhtala, Jarmo Käpylä

  • 1Department of Biochemistry and Food Chemistry, University of Turku, FI-20014 Turku, Finland. jyrki.heino@utu.fi

The International Journal of Biochemistry & Cell Biology
|September 16, 2008
PubMed
Summary
This summary is machine-generated.

Collagens are ancient proteins crucial for metazoan evolution. Early animals may have used collagen-binding glycoproteins for cell adhesion before specialized integrin receptors evolved in vertebrates.

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Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
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Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides

Published on: January 31, 2014

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Preparation of 3D Collagen Gels and Microchannels for the Study of 3D Interactions In Vivo
10:24

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Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides
07:03

Imaging Denatured Collagen Strands In vivo and Ex vivo via Photo-triggered Hybridization of Caged Collagen Mimetic Peptides

Published on: January 31, 2014

Area of Science:

  • Evolutionary Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Collagens are essential triple-helical proteins forming extracellular matrix structures.
  • Cell adhesion receptors like integrins are ancient, but direct collagen binding by integrins is vertebrate-specific.
  • Early metazoans likely used alternative receptors for collagen recognition.

Purpose of the Study:

  • To explore the evolutionary origins and roles of collagen receptors.
  • To investigate the potential involvement of integrins and discoidin domain receptors (DDRs) in early metazoan evolution.
  • To understand the differential recognition of fibrillar and non-fibrillar collagens by receptor families.

Main Methods:

  • Comparative analysis of collagen receptor families (integrins, DDRs) across metazoan phyla.
  • Review of existing literature on collagen structure and function.
  • Hypothesizing receptor-ligand interactions based on evolutionary timelines.

Main Results:

  • Collagens and integrins co-evolved early in metazoan history.
  • Vertebrate-specific integrins directly bind collagens, suggesting indirect binding in invertebrates.
  • Discoidin domain receptors (DDRs) are present in invertebrates, but their collagen-binding function is unconfirmed.
  • Both fibrillar and non-fibrillar collagens exist in primitive metazoans like sponges.

Conclusions:

  • Specialized collagen receptors, including integrins and potentially DDRs, were instrumental in the evolution of complex metazoan systems.
  • The evolution of direct collagen binding by integrins may have facilitated the development of bone, cartilage, and circulatory systems.
  • Further research is needed to elucidate the collagen-binding capabilities of invertebrate DDRs.