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Vitronectin shows complement-independent binding to isolated keratin filament aggregates.
H Hintner1, U Stanzl, K Dahlbäck
1Department of Dermatology, University of Innsbruck, Austria.
The Journal of Investigative Dermatology
|November 1, 1989
Summary
Vitronectin binds to keratin intermediate filaments, potentially aiding in the clearance of keratin bodies. This interaction may limit complement-mediated damage and facilitate fibroblast or macrophage removal of these structures.
Area of Science:
- Biochemistry
- Cell Biology
- Dermatology
Background:
- Keratinocyte cell death can form dermal keratin bodies from keratin intermediate filament aggregates.
- Vitronectin, a glycoprotein, is found associated with keratin bodies in vivo.
- Vitronectin's known functions include inhibiting complement and promoting cell attachment.
Purpose of the Study:
- To investigate the interaction between vitronectin and keratin intermediate filaments.
- To explore vitronectin's potential role in the removal of keratin bodies.
- To determine if vitronectin binding to keratin bodies is complement-dependent.
Main Methods:
- Immunofluorescence staining of human skin sections and Hep-2 cells.
- Immunoblotting of keratin intermediate filament aggregates.
- Studies using normal human serum, heat-inactivated serum, and C4-deficient serum.
- Experiments with purified vitronectin and amyloid P component.
Main Results:
- Vitronectin binding to keratin intermediate filaments was observed in skin and Hep-2 cells.
- Vitronectin directly bound to isolated keratin intermediate filament aggregates.
- Binding was independent of complement activation and amyloid P component.
- Purified vitronectin demonstrated binding to keratin aggregates.
Conclusions:
- Vitronectin interacts with keratin intermediate filaments.
- Vitronectin binding to keratin bodies may limit complement-mediated damage.
- This interaction could facilitate the clearance of keratin bodies by phagocytic cells.