Home Human tissue kallikreins as promiscuous modulators of homeostatic skin barrier functions
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Human tissue kallikreins as promiscuous modulators of homeostatic skin barrier functions

  • Azza Eissa and Eleftherios P. Diamandis
Published/Copyright: May 15, 2008
Biological Chemistry
From the journal Volume 389 Issue 6

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.


Corresponding author

Published Online: 2008-05-15
Published in Print: 2008-06-01

©2008 by Walter de Gruyter Berlin New York

Articles in the same Issue

  1. Editorial
  2. Kallikreins and kallikrein-related peptidases
  3. Guest Editorial
  4. The 2nd International Symposium on Kallikreins and Kallikrein-Related Peptidases (ISK 2007) and the Commemorative Gold Medal of the E.K. Frey–E. Werle Foundation of the Henning L. Voigt Family
  5. Highlight: Kallikrein, kinins and kallikrein-related peptidases
  6. Structures and specificity of the human kallikrein-related peptidases KLK 4, 5, 6, and 7
  7. Development of peptides specifically modulating the activity of KLK2 and KLK3
  8. Kallikreins and proteinase-mediated signaling: proteinase-activated receptors (PARs) and the pathophysiology of inflammatory diseases and cancer
  9. Prostatic trypsin-like kallikrein-related peptidases (KLKs) and other prostate-expressed tryptic proteinases as regulators of signalling via proteinase-activated receptors (PARs)
  10. Human tissue kallikreins as promiscuous modulators of homeostatic skin barrier functions
  11. A potential role for tissue kallikrein-related peptidases in human cervico-vaginal physiology
  12. microRNAs: a new frontier in kallikrein research
  13. Functions of KLK4 and MMP-20 in dental enamel formation
  14. Genetic deficiency in tissue kallikrein activity in mouse and man: effect on arteries, heart and kidney
  15. Development of diabetic cardiomyopathy and the kallikrein-kinin system – new insights from B1 and B2 receptor signaling
  16. Doxorubicin cardiomyopathy-induced inflammation and apoptosis are attenuated by gene deletion of the kinin B1 receptor
  17. Attenuation of left ventricular dysfunction by an ACE inhibitor after myocardial infarction in a kininogen-deficient rat model
  18. Tissue kallikrein and kinin infusion promotes neovascularization in limb ischemia
  19. Kallikreins as microRNA targets: an in silico and experimental-based analysis
  20. Kallikreins are associated with secondary progressive multiple sclerosis and promote neurodegeneration
  21. Immunofluorometric activity-based probe analysis of active KLK6 in biological fluids
  22. Kallikrein 6 is a mediator of K-RAS-dependent migration of colon carcinoma cells
  23. Gene expression changes associated with the anti-angiogenic activity of kallikrein-related peptidase 3 (KLK3) on human umbilical vein endothelial cells
  24. An AKT activity threshold regulates androgen-dependent and androgen-independent PSA expression in prostate cancer cell lines
  25. Quantitative RT-PCR analysis and immunohistochemical localization of the kallikrein-related peptidases 13 and 14 in lung
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