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.
|Number of pages||7|
|Journal||British Journal of Dermatology|
|Publication status||Published - 1991|
Kelly, S. E., Hunter, J. A. A., Jones, D. B., Clark, B. R., & Fleming, S. (1991). Morphological evidence for calcium-dependent association of calgranulin with the epidermal cytoskeleton in inflammatory dermatoses. British Journal of Dermatology, 124(5), 403-9. https://doi.org/10.1111/j.1365-2133.1991.tb00616.x