Skin surface proteolytic activity. Partial characterization and identification
Wormser, U.; Brodsky, B.; Moor, E.V.; Eldad, A.; Gal, R.; Nyska, A.; Kohen, R.
Advances in Experimental Medicine and Biology 436: 207-212
1998
ISSN/ISBN: 0065-2598 PMID: 9561221 Document Number: 486595
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.