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In vitroandin vivoinhibition of rat liver cathepsin L by epidermal proteinase inhibitor

Authors
Journal
Biochemical and Biophysical Research Communications
0006-291X
Publisher
Elsevier
Publication Date
Volume
93
Issue
2
Identifiers
DOI: 10.1016/0006-291x(80)91097-9
Disciplines
  • Biology

Abstract

Abstract An SH-proteinase inhibitor (EPI) purified from newborn rat epidermis was shown to inhibit casein and BAPNA hydrolytic activities of rat liver extract in vitro . The greatest inhibition was seen in the cathepsin L fraction purified by CM Sephadex C-50. Fifty percent inhibition of 1 U cathepsin L and papain were seen with 325 μg and 50 μg EPI, respectively. Intradermal injection of cathepsin L in newborn rats caused inflammatory reactions and a reduction of EPI from living epidermal cells of the skin site. The findings suggest that EPI is excreted from the epidermal cells into the dermis where SH-proteinase activity is involved in the inflammatory process.

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