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Skin surface proteolytic activity. Partial characterization and identification

U Wormser1, B Brodsky, E V Moor

  • 1Department of Pharmacology, School of Pharmacy, Faculty of Medicine, Hebrew University, Israel. wormser@yam-suff.cc.huji.ac.il

Advances in Experimental Medicine and Biology
|April 30, 1998
PubMed
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Researchers developed a novel, non-invasive method to measure skin surface proteolytic activity in living animals. This technique identified aspartic proteinases on the skin, offering new insights into skin physiology.

Area of Science:

  • Biochemistry
  • Dermatology
  • Enzymology

Background:

  • Proteolytic activity on the skin surface plays a role in various physiological and pathological processes.
  • Existing methods for assessing skin proteinase activity are often invasive or indirect.

Purpose of the Study:

  • To develop and validate a sensitive, non-invasive method for determining skin surface proteolytic activity in vivo.
  • To characterize the nature of the identified skin surface proteinases.

Main Methods:

  • A novel methodology using a constructed well on anesthetized guinea pig skin.
  • Incubation of 125I-S-carboxymethylated insulin B-chain (ICMI) as a substrate within the well.
  • Assessment of time-dependent activity and inhibition by pepstatin A and propylene glycol.

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Main Results:

  • Demonstrated time-dependent proteolytic activity on the skin surface of living guinea pigs.
  • Showed strong inhibition by pepstatin A, suggesting the involvement of aspartic proteinases (e.g., cathepsin D/E).
  • Confirmed blockage of activity by propylene glycol pretreatment.

Conclusions:

  • The study successfully established a non-invasive method for in situ proteinase determination on living animal skin.
  • This method revealed the presence of active aspartic proteinases on the skin surface.
  • The findings open avenues for further research into skin surface proteinase functions and modulation.