Reddish, scaly, and itchy: how proteases and their inhibitors contribute to inflammatory skin diseases.

Full Abstract

The skin protects us from water loss and mechanical damage. The surface-exposed epidermis, a self-renewing stratified squamous epithelium composed of several layers of keratinocytes, is most important in the barrier defense against these challenges. Endogenous and exogenous proteases such as kallikreins, matriptase, caspases, cathepsins, and proteases derived from microorganisms are important in the desquamation process of the stratum corneum and are able to activate and inactivate defense molecules in human epidermis. Protease inhibitors such as like LEKTI, elafin, SLPI, SERPINs, and cystatins regulate their proteolytic activity and contribute to the integrity and protective barrier function of the skin. Changes in the proteolytic balance of the skin can result in inflammation, which leads to the typical clinical signs of redness, scaling, and itching. This review summarizes the current knowledge of how proteases, their inhibitors, and their target proteins, including filaggrin, protease-activated receptors, and corneodesmosin, contribute to the pathophysiology of inflammation of the skin and highlight their role in common inflammatory skin diseases such as atopic dermatitis, rosacea, and psoriasis.

Author information

Author/s: Meyer-Hoffert, Ulf (U);

Affiliation: Department of Dermatology, University Hospital Schleswig-Holstein, D-24105, Kiel, Germany. umeyerhoffert(-atsign-)dermatology.uni-kiel.de

Journal and publication information

Publication Type: Journal Article; Research Support, Non-U.S. Gov't; Review

Journal: Archivum immunologiae et therapiae experimentalis (Arch Immunol Ther Exp (Warsz)), published in Switzerland. (Language: eng)

Reference: -2009 Sep-Oct; vol 57 (issue 5) : pp 345-54

Dates: Created 2009/08/26; Completed 2009/10/21;

PMID: 19688185, status: MEDLINE (last retrieval date: 10/21/2009, IMS Date: )

Sourced from the National Library of Medicine. Abstract text and other information may be subject to copyright.

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MeSH headings (categories)

This article was linked to the MESH Headings shown below.

Animals
Antimicrobial Cationic Peptides - metabolism
Caspase 14 - metabolism
Cathepsin D - metabolism
Cystatins - metabolism
Dipeptidyl Peptidase I - metabolism
Elafin - metabolism
Glycoproteins - metabolism
Humans
Inflammation - metabolism; pathology

Intermediate Filament Proteins - metabolism
Kallikreins - metabolism
Peptide Hydrolases - metabolism
Protease Inhibitors - metabolism
Proteinase Inhibitory Proteins, Secretory - metabolism
Pruritus - metabolism; pathology
Receptors, Proteinase-Activated - metabolism
Serine Endopeptidases - metabolism
Skin - metabolism; pathology
Skin Diseases - metabolism; pathology

Associated Chemicals: Antimicrobial Cationic Peptides (0) ; CDSN protein, human (0) ; Cystatins (0) ; Elafin (0) ; Glycoproteins (0) ; Intermediate Filament Proteins (0) ; PI3 protein, human (0) ; Protease Inhibitors (0) ; Proteinase Inhibitory Proteins, Secretory (0) ; Receptors, Proteinase-Activated (0) ; SPINK5 protein, human (0) ; filaggrin (0) ; Peptide Hydrolases (EC 3.4.-) ; Dipeptidyl Peptidase I (EC 3.4.14.1) ; Kallikreins (EC 3.4.21.-) ; Serine Endopeptidases (EC 3.4.21.-) ; matriptase (EC 3.4.21.-) ; prostasin (EC 3.4.21.-) ; Caspase 14 (EC 3.4.22.-) ; Cathepsin D (EC 3.4.23.5)

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