Morphological evidence for calcium-dependent association of calgranulin with the epidermal cytoskeleton in inflammatory dermatoses.
The association of calgranulins, intracellular calcium-binding proteins, with the keratinocyte cytoskeleton has been studied. These molecules are expressed in various inflammatory dermatoses and in organ-culture explants. Triton X-100 extraction in the presence of calcium or EDTA suggested that calgranulins are detergent insoluble in the presence of calcium. The molecules were localized in a plaque-like structure at the cell periphery in lesional skin and in organ-culture explants. Following induction of calgranulins in vitro there was a redistribution of the intermediate filament cytoskeleton into a perinuclear halo, although desmosomes remained intact. These various features suggest that these members of the S-100 protein family have a role in cytoskeletal changes seen in various skin diseases.
Kelly
S E
SE
Department of Dermatology, University of Edinburgh, U.K.
Hunter
J A
JA
Jones
D B
DB
Clark
B R
BR
Fleming
S
S
D015153:Blotting, Western; D002135:Calcium-Binding Proteins / Q000032:analysis*; D040501:Calgranulin A; D040502:Calgranulin B; D046508:Culture Techniques; D003599:Cytoskeleton / Q000737:chemistry* / Q000648:ultrastructure; D003872:Dermatitis / Q000378:metabolism* / Q000473:pathology; D003896:Desmosomes / Q000648:ultrastructure; D004817:Epidermis / Q000737:chemistry*; D005260:Female; D006801:Humans; D007150:Immunohistochemistry; D015603:Keratinocytes / Q000737:chemistry; D016253:Microscopy, Immunoelectron
D002135:Calcium-Binding Proteins; D040501:Calgranulin A; D040502:Calgranulin B