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Biological Chemistry

Editor-in-Chief: Brüne, Bernhard

Editorial Board: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Thomas, Douglas D. / Turk, Boris / Wittinghofer, Alfred


IMPACT FACTOR 2018: 3.014
5-year IMPACT FACTOR: 3.162

CiteScore 2018: 3.09

SCImago Journal Rank (SJR) 2018: 1.482
Source Normalized Impact per Paper (SNIP) 2018: 0.820

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1437-4315
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Volume 389, Issue 6

Issues

Human tissue kallikreins as promiscuous modulators of homeostatic skin barrier functions

Azza Eissa
  • 1Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto M5G 1L5, ON, Canada and Department of Pathology and Laboratory Medicine, Mount Sinai Hospital, Toronto M5T 3L9, ON, Canada
  • Other articles by this author:
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/ Eleftherios P. Diamandis
  • 2Department of Laboratory Medicine and Pathobiology, University of Toronto, Toronto M5G 1L5, ON, Canada and Department of Pathology and Laboratory Medicine, Mount Sinai Hospital, Toronto M5T 3L9, ON, Canada and Department of Clinical Biochemistry, University Health Network and Toronto Medical Laboratories, Toronto M5G 1X5, ON, Canada
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Published Online: 2008-05-15 | DOI: https://doi.org/10.1515/BC.2008.079

Abstract

Human tissue kallikreins (KLKs) are the largest family of secreted serine protease endopeptidases encoded by 15 genes clustered on chromosome 19q13.4. Multiple KLK enzymes are co-localized in the upper stratum granulosum and stratum corneum of human epidermis, and in associated appendages such as hair follicle epithelia and sweat glands. Until recently, kallikrein proteolytic activity in the skin was exclusively attributed to KLK5 and KLK7. However, wider cutaneous roles of kallikreins became evident in recent years as the proposal of KLK proteolytic activation cascades emerged. We postulate that these proteolytic enzymes may serve as promiscuous mediators of different skin barrier functions, since they are capable of proteolysing different substrates that govern skin desquamation, antimicrobial defense, and lipid permeability. Growing evidence now attests to potential kallikrein involvement in skin inflammation, pigmentation, and tumor suppression via their ability to target proteinase-activated receptor signaling pathways. Current knowledge on kallikrein roles in skin physiology and pathobiology is described in this review.

Keywords: activation cascade; corneodesmosomes; proteinase-activated receptors; serine protease inhibitors; skin diseases; stratum corneum

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Published Online: 2008-05-15

Published in Print: 2008-06-01


Citation Information: Biological Chemistry, Volume 389, Issue 6, Pages 669–680, ISSN (Online) 14374315, ISSN (Print) 1431-6730, DOI: https://doi.org/10.1515/BC.2008.079.

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