Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 403-9 |
| Number of pages | 7 |
| Journal | British Journal of Dermatology |
| Volume | 124 |
| Issue number | 5 |
| DOIs | |
| Publication status | Published - 1991 |
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