title: Skin surface proteolytic activity. Partial characterization and identification.
abstract: Skin surface proteolytic activity in the living animal was determined by a sensitive, non-invasive methodology developed in our laboratory. A non-leaky well was constructed on the shaved back of an anesthetized guinea pig. The well contained the reaction mixture including the substrate 125I-S-carboxymethylated insulin B-chain (ICMI). The proteolytic activity was shown to be time-dependent. The activity was strongly inhibited by pepstatin A, indicating the involvement of aspartic proteinase(s) such as cathepsin D and/or E. Pretreatment of the skin with propylene glycol blocked the proteolytic activity. The present study demonstrates the presence of proteolytic activity located on skin surface using a unique, non-invasive method for in situ proteinase determination in the living animal.
authors.affiliation: Department of Pharmacology, School of Pharmacy, Faculty of Medicine, Hebrew University, Israel. wormser@yam-suff.cc.huji.ac.il
authors.forename: U
authors.initials: U
authors.lastname: Wormser
authors.forename: B
authors.initials: B
authors.lastname: Brodsky
authors.forename: E V
authors.initials: EV
authors.lastname: Moor
authors.forename: A
authors.initials: A
authors.lastname: Eldad
authors.forename: R
authors.initials: R
authors.lastname: Gal
authors.forename: A
authors.initials: A
authors.lastname: Nyska
authors.forename: R
authors.initials: R
authors.lastname: Kohen
mesh_terms: D000818:Animals; D010450:Endopeptidases / Q000378:metabolism*; D006168:Guinea Pigs; D012867:Skin / Q000201:enzymology*
chemical_list: D010450:Endopeptidases