Ultrastructural changes of the skin induced by human leukocyte elastase and cathepsin G.
Human neutrophil elastase and cathepsin G at a concentration of 10(-6) M were found to attack various substrates when normal skin biopsy specimens were incubated at 37 degrees C for 1 h with either of these enzymes. Elastase damaged primarily hemidesmosomes, leading to the epidermal cleavage from the dermis, whereas cathepsin G damaged the membrane structures. Both these neutral proteinases were highly specific to basal lamina of blood vessels. This indicates that neutrophil elastase and neutrophil cathepsin G may play different roles in various skin diseases related to enhanced activity and infiltration of neutrophils.
Glinski
W
W
Department of Dermatology, Warsaw School of Medicine, Poland.
Kuligowski
M
M
Pierozynska-Dubowska
M
M
Glinska-Ferenz
M
M
Jablonska
S
S
D056649:Cathepsin G; D002403:Cathepsins / Q000494:pharmacology*; D006801:Humans; D066298:In Vitro Techniques; D009504:Neutrophils / Q000201:enzymology*; D010196:Pancreatic Elastase / Q000494:pharmacology*; D012697:Serine Endopeptidases; D012867:Skin / Q000187:drug effects* / Q000648:ultrastructure
D002403:Cathepsins; D012697:Serine Endopeptidases; C534094:CTSG protein, human; D056649:Cathepsin G; D010196:Pancreatic Elastase