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Human blood monocytes interact with type I collagen through alpha x beta 2 integrin (CD11c-CD18, gp150-95)
R Garnotel1, L Rittié, S Poitevin
1Laboratoire de Biochimie Médicale et Biologie Moléculaire, Centre National de la Recherche Scientifique, UPRESA 6021, Institut Fedératif de Recherche 53-Biomolécules, Faculté de Médecine, Université de Reims Champagne-Ardenne, Reims, France.
Journal of Immunology (Baltimore, Md. : 1950)
|May 23, 2000
Summary
Human monocytes use CD11c-CD18 integrins to adhere to and activate on type I collagen, a key step in inflammation and wound healing. Specific collagen domains are crucial for monocyte activation.
Area of Science:
- Immunology
- Cell Biology
- Biochemistry
Background:
- Human blood monocytes migrate into tissues during inflammation and wound healing.
- Monocytes interact with extracellular matrix proteins like collagen.
Purpose of the Study:
- To investigate the effects of type I collagen on human monocyte adhesion and superoxide anion production.
- To identify the specific molecular mechanisms underlying monocyte-collagen interactions.
Main Methods:
- Used elutriated human monocytes and rat tail tendon type I collagen.
- Assessed monocyte adhesion and superoxide production.
- Employed monoclonal antibodies (mAbs) against integrin subunits CD11c and CD18.
- Utilized affinity chromatography and Western blotting.
Main Results:
- Both acid-soluble and pepsin-digested type I collagens promoted monocyte adhesion.
- Only acid-soluble collagen with intact telopeptides induced superoxide production.
- Monocyte adhesion and activation on type I collagen were mediated by CD11c-CD18 (αxβ2) integrins.
- Specific domains of type I collagen telopeptides were necessary for monocyte activation.
Conclusions:
- Monocytes interact with type I collagen via CD11c-CD18 integrins, facilitating adhesion and activation.
- Telopeptide domains of type I collagen are essential for monocyte activation.
- These monocyte-collagen interactions are likely significant in early inflammatory processes.