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Type I and type III collagen interactions during fibrillogenesis
R Fleischmajer1, J S Perlish, R E Burgeson
1Department of Dermatology, Mount Sinai School of Medicine, New York, New York 10029.
Annals of the New York Academy of Sciences
|January 1, 1990
Summary
Type I and type III collagens coexist within the same fibrils, as demonstrated by immunoelectron microscopy. The aminopropeptide of type III procollagen coats mature type I collagen fibrils in human skin.
Area of Science:
- Biochemistry
- Cell Biology
- Dermatology
Background:
- Type I and type III collagens are major structural proteins in human skin.
- Previous studies suggested potential co-localization of type I and type III collagens within fibrils.
Purpose of the Study:
- To investigate the co-localization of type I and type III collagens within the same fibrils.
- To examine the distribution and presence of procollagen aminopropeptides in embryonic and adult human skin.
Main Methods:
- Double labeling immunofluorescence and immunoelectron microscopy using antibodies against collagen molecules and procollagen aminopropeptides.
- Immunoblotting of skin extracts.
- Utilized 5- and 15-nm gold particles for ultrastructural visualization.
Main Results:
- Identical immunofluorescence patterns for type I and type III collagen molecules in fetal and adult skin.
- Type III procollagen aminopropeptide present throughout fetal and adult dermis.
- Type I procollagen aminopropeptide present in embryonic dermis, reduced in adult dermis except at the epidermo-dermal junction.
- Immunoelectron microscopy confirmed type I and type III collagens on the same thin fibrils in fetal skin.
- Large type I fibrils coated with type III collagen and its aminopropeptide in fetal skin.
Conclusions:
- Type I and type III collagens coexist within the same fibrils in human skin.
- Type III procollagen aminopropeptide is found on mature type I collagen fibrils.
- Differential distribution of type I procollagen aminopropeptide suggests developmental changes in collagen processing.