Phenotypical and Molecular Profiling of the Extraneuronal Cholinergic System of the Skin

We present molecular and protein profiling of all acetylcholine receptors (ACh-R) in human scalp skin using PCR, in situ hybridization and double-labeling immunofluorescence. Within the epidermis, the nicotinic (n)ACh-R subunits, α3, α5, β2, and β4 were expressed in the basal cell layer (BCL) and in...

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Veröffentlicht in:Journal of investigative dermatology 2004-11, Vol.123 (5), p.937-949
Hauptverfasser: Kurzen, Hjalmar, Berger, Hans, Jäger, Claudia, Hartschuh, Wolfgang, Näher, Helmut, Gratchev, Alexei, Goerdt, Sergij, Deichmann, Martin
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Sprache:eng
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Zusammenfassung:We present molecular and protein profiling of all acetylcholine receptors (ACh-R) in human scalp skin using PCR, in situ hybridization and double-labeling immunofluorescence. Within the epidermis, the nicotinic (n)ACh-R subunits, α3, α5, β2, and β4 were expressed in the basal cell layer (BCL) and in a single cell layer in the stratum granulosum; α9 was expressed in the basal and lower spinous layers. α7, α10, and β1 were preferentially detected in the upper spinous and granular layers. Of the muscarinic (m)ACh-R, m1 and m4 were found in the suprabasal layers, whereas m2, m3, and m5 remained restricted to the lower layers. In the outer root sheath of the hair follicle, all ACh-R except α9, β1, and m4 were found in the BCL whereas the α9, m4, and m5 ACh-R were restricted to the central cell layer. The α5, β1, β2, m1–m4 chains were strongly expressed in the inner root sheath. Undifferentiated sebocytes expressed the α3, α9, β4, m3–m5 ACh-R whereas α7, β2, β4, m2, and m4 were found in mature sebocytes. In sweat glands, the α3*, α7, and m2–m5 ACh-R were most prominent in the myoepithelial cells whereas α9, β2, m1, m3, and m4 ACh-R were present in the acinar cells. Taken together, our data result in a complete molecular map of the extraneuronal cholinergic system of the skin that may be translated into distinct functional reaction patterns.
ISSN:0022-202X
1523-1747
DOI:10.1111/j.0022-202X.2004.23425.x