Barrier function, epidermal differentiation, and human beta-defensin 2 expression in tinea corporis.
Tinea corporis is a superficial mycotic infection resulting in substantial epidermal changes. We determined skin barrier function, epidermal differentiation, and human-beta-defensin 2 (hBD-2) protein expression in 10 patients with tinea corporis caused by Trichophyton rubrum (T. rubrum). We found disturbed skin barrier function as shown by a significant increase in transepidermal water loss (TEWL) and specific ultrastructural changes including disturbed formation of extracellular lipid bilayers, lamellar body extrusion, and deposit of clotted material at the stratum granulosum/stratum corneum interface. Epidermal proliferation in tinea increased several fold and accordingly, proliferation and inflammation-associated keratins K6, K16, and K17 were expressed. Expression of basal keratins K5 and K14 increased, whereas differentiation-associated K10 was reduced. Reduction of the cornified envelope proteins involucrin, loricrin, and the S100 protein filaggrin was also seen. Reduced filaggrin expression correlated with reduced skin hydration; protein breakdown products of filaggrin have been shown to be important for water binding. Surprisingly, we found pronounced epidermal protein expression of hBD-2, which may be related to disturbed epidermal differentiation and inflammation. hBD-2 showed a weak, although significant, antifungal activity against T. rubrum in the turbidimetric assay and the immunohistological staining was somewhat less pronounced in areas directly underneath fungal hyphae in the stratum corneum. Together, we describe profound changes in skin barrier structure and function, epidermal proliferation, and differentiation including pronounced protein expression of hBD-2 in tinea corporis.
Jensen
Jens-Michael
JM
Department of Dermatology, University of Kiel, Kiel, Germany.
Pfeiffer
Stephan
S
Akaki
Tatsuya
T
Schröder
Jens-Michael
JM
Kleine
Michael
M
Neumann
Claudia
C
Proksch
Ehrhardt
E
Brasch
Jochen
J
D002454:Cell Differentiation / Q000502:physiology*; D002463:Cell Membrane Permeability / Q000502:physiology*; D049109:Cell Proliferation; D003681:Dehydration / Q000503:physiopathology; D004817:Epidermis / Q000382:microbiology / Q000473:pathology* / Q000503:physiopathology; D000091344:Filaggrin Proteins; D005786:Gene Expression Regulation; D006801:Humans; D007381:Intermediate Filament Proteins / Q000235:genetics / Q000378:metabolism; D007633:Keratins / Q000235:genetics / Q000378:metabolism; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism; D011498:Protein Precursors / Q000235:genetics / Q000378:metabolism; D012879:Skin Physiological Phenomena; D014005:Tinea / Q000378:metabolism* / Q000473:pathology / Q000503:physiopathology; D014249:Trichophyton / Q000472:pathogenicity; D023083:beta-Defensins / Q000235:genetics / Q000378:metabolism*
C106641:DEFB4A protein, human; C000717249:FLG protein, human; D000091344:Filaggrin Proteins; D007381:Intermediate Filament Proteins; D008565:Membrane Proteins; D011498:Protein Precursors; D023083:beta-Defensins; C064554:loricrin; C032253:involucrin; D007633:Keratins