Immunocytochemical localization of collagen types I, III, IV, and fibronectin in the human dermis. Modifications with ageing

The distribution of collagen types I, III, IV, and of fibronectin has been studied in the human dermis by light and electron-microscopic immunocytochemistry, using affinity purified primary antibodies and tetramethylrhodamine isothiocyanate-conjugated secondary antibodies. Type I collagen was presen...

Full description

Saved in:
Bibliographic Details
Published in:Cell and tissue research 1992-06, Vol.268 (3), p.505-511
Main Authors: Vitellaro-Zuccarello, L, Garbelli, R, Rossi, V D
Format: Article
Language:English
Subjects:
Adolescent
Adult
Aged
Aging - metabolism
Child
Child, Preschool
Collagen - analysis
Collagen - genetics
Epidermis - chemistry
Epidermis - metabolism
Epidermis - ultrastructure
Fibronectins - analysis
Fibronectins - metabolism
Humans
Immunoenzyme Techniques
Immunohistochemistry
Infant
Microscopy, Immunoelectron
Middle Aged
Citations: Items that this one cites
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The distribution of collagen types I, III, IV, and of fibronectin has been studied in the human dermis by light and electron-microscopic immunocytochemistry, using affinity purified primary antibodies and tetramethylrhodamine isothiocyanate-conjugated secondary antibodies. Type I collagen was present in all collagen fibers of both papillary and reticular dermis, but collagen fibrils, which could be resolved as discrete entities, were labeled with different intensity. Type III collagen codistributed with type I in the collagen fibers, besides being concentrated around blood vessels and skin appendages. Coexistence of type I and type III collagens in the collagen fibrils of the whole dermis was confirmed by ultrastructural double-labelling experiments using colloidal immunogold as a probe. Type IV collagen was detected in all basement membranes. Fibronectin was distributed in patches among collagen fibers and was associated with all basement membranes, while a weaker positive reaction was observed in collagen fibers. Ageing caused the thinning of collagen fibers, chiefly in the reticular dermis. The labeling pattern of both type I and III collagens did not change in skin samples from patients of up to 79 years of age, but immunoreactivity for type III collagen increased in comparison to younger skins. A loss of fibronectin, likely related to the decreased morphogenetic activity of tissues, was observed with age.
ISSN:0302-766X
1432-0878
DOI:10.1007/BF00319157