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Updated: Jul 18, 2026
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
Mammalian collagen receptors
Birgit Leitinger1, Erhard Hohenester
1National Heart and Lung Institute, Imperial College London, London SW7 2AZ, UK.
Summary
Mammalian tissues rely on collagen for mechanical stability and cell behavior control. This review details collagen
Area of Science:
- Biochemistry and Cell Biology
- Extracellular Matrix Research
Background:
- Collagens are crucial structural proteins in mammalian tissues, providing mechanical stability.
- They also play vital roles in regulating cell behavior and tissue function.
- The characteristic triple helix structure of collagen, formed by glycine-X-Y repeats, is key to its function.
Purpose of the Study:
- To review the structure and function of cell surface receptors that recognize triple-helical collagen.
- To elucidate the principles governing collagen recognition by these diverse receptors.
Main Methods:
- Literature review of studies on collagen structure and cell surface receptors.
- Analysis of the molecular mechanisms underlying collagen-receptor interactions.
- Comparative examination of different collagen-binding receptor families.
Main Results:
- Identified five major families of cell surface receptors that bind to triple-helical collagen: integrins, discoidin domain receptors (DDRs), glycoprotein VI (GPVI), leukocyte-associated IG-like receptor-1 (LAIR-1), and mannose receptor family members.
- Highlighted the structural diversity among these receptors, despite their common ligand.
- Emphasized the functional implications of collagen recognition in various physiological and pathological processes.
Conclusions:
- Multiple distinct receptor families have evolved to recognize collagen's triple helix.
- Understanding these collagen recognition principles is essential for deciphering tissue mechanics and cell signaling.
- Further research into these interactions may reveal therapeutic targets for collagen-related diseases.
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