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Human monocyte interactions with non-enzymatically glycated collagen
1Department of Pathology, Vanderbilt University, Nashville, Tennessee.
Diabetologia
|February 1, 1992
Summary
Activated human monocytes, expressing receptors for advanced glycation end products, show increased adhesion to glycated collagen. This suggests a role in counterbalancing impaired binding and potentially contributing to pathological changes.
Area of Science:
- Immunology
- Biochemistry
- Cell Biology
Background:
- Receptors for advanced glycation end products (RAGE) are expressed on activated human monocytes.
- Non-enzymatic glycation of extracellular matrix proteins can alter cell interactions.
Purpose of the Study:
- To investigate the role of RAGE in monocyte adhesion and matrix interaction with glycated substrates.
- To determine if RAGE expression on activated monocytes influences their adhesion to and degradation of glycated collagen, fibronectin, and endothelial cell matrix proteins.
Main Methods:
- Assessing monocyte adhesion to non-enzymatically glycated collagen, fibronectin, and endothelial cell matrix substrates.
- Utilizing competitive inhibition assays with glycated albumin.
- Measuring the degradation of 125I-labelled non-enzymatically glycated collagen by activated human monocytes.
Main Results:
- Activated monocytes showed significantly increased adhesion to glycated collagen (+32%), which was inhibited by glycated albumin.
- Non-activated monocytes exhibited decreased adhesion (-16%) to glycated substrates.
- Activated monocytes demonstrated enhanced degradation of glycated collagen over 2-4 hours.
Conclusions:
- RAGE on activated monocytes may counterbalance reduced adherence to glycated matrix proteins.
- Overcompensation by RAGE could lead to pathological changes.
- These receptors may also facilitate monocyte-mediated remodeling of glycated matrix proteins.