Schalkwijk J, de Roo C, de Jongh G J
Department of Dermatology, Academic Hospital Nijmegen, The Netherlands.
Biochim Biophys Acta. 1991 Feb 22;1096(2):148-54. doi: 10.1016/0925-4439(91)90053-c.
Recently we reported a preliminary characterization of anti-elastase activity which is found in cultured keratinocytes and in epidermis from psoriasis patients, but not in normal human epidermis. Here we present evidence that this inhibitory activity is derived from a cationic protein with a molecular mass of 18 kDa. In psoriatic scales the inhibitor is mainly present as a biologically active 11 kDa fragment. Inhibition of human leukocyte elastase is strong (Ki = 2 x 10(11) M) and fast (kon = 10(7) M-1.s-1). Using chromatofocusing, affinity chromatography and gel-permeation FPLC, the 11 kDa fragment was purified from psoriatic scales. This preparation was reduced and carboxymethylated, blotted onto poly(vinylidene difluoride) membrane and subjected to N-terminal gas-phase sequencing. Within a stretch of 16 amino acids a 40% homology was found with the active site of antileukoproteinase (ALP) a known serine proteinase inhibitor present in mucous secretions. We therefore propose the acronym SKALP (skin-derived antileukoproteinase) as a name for this elastase inhibitor.
