Biochemical changes in desmosomes of bovine muzzle epidermis during differentiation.
Biochemical changes taking place in desmosomes during differentiation have been studied. Bovine muzzle epidermis was sliced horizontally into 6 layers, 0.2 mm thick, and desmosomes were isolated from each layer. These were then analyzed by polyacrylamide gel electrophoresis. The electrophoretic patterns of desmosomal proteins from the 6 layers were found to be qualitatively similar to each other, but there was an increase in the ratio of the amount of 150 kD glycoprotein (desmoglein I) relative to 240 and 210 kD proteins (desmoplakins) in the upper layers of the epidermis. This finding was supported by the similar increase observed in electrophoretic patterns of proteins extracted directly from each layer of the epidermis in electrophoretic sample buffer. In order to study the fate of desmosomal components in the stratum corneum, serial skin surface biopsies were stained with antisera against desmosomal components using indirect immunofluorescence techniques. This experiment showed that desmosomal proteins and glycoproteins persist in the stratum corneum but quantitatively decrease in the outer layers. This decrease may play a significant role in desquamation.
Konohana
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Department of Medicine (Dermatology), University of Wales College of Medicine, Cardiff, U.K.
Konohana
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Roberts
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Marks
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D000818:Animals; D002417:Cattle; D002454:Cell Differentiation; D003598:Cytoskeletal Proteins; D051183:Desmoglein 1; D051182:Desmogleins; D051180:Desmoplakins; D003896:Desmosomes / Q000378:metabolism* / Q000648:ultrastructure; D000078404:Epidermal Cells; D004817:Epidermis / Q000648:ultrastructure; D005455:Fluorescent Antibody Technique; D006023:Glycoproteins / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000378:metabolism; D008970:Molecular Weight
D003598:Cytoskeletal Proteins; D051183:Desmoglein 1; D051182:Desmogleins; D051180:Desmoplakins; D006023:Glycoproteins; D008562:Membrane Glycoproteins