Expression of tenascin in perifollicular connective tissue: comparison of normal scalp and alopecia areata.
Tenascin, a recently discovered extracellular matrix protein, was demonstrated in perifollicular connective tissue of normal human scalp using immunohistochemistry. Its localization was different from other well-known extracellular matrix components, like fibronectin, laminin and heparan sulphate proteoglycan. A comparison between alopecia areata and normal scalps did not reveal major qualitative differences, except for an increased expression near heavily infiltrated follicles.
van Baar
H M
HM
Department of Dermatology, University Nijmegen, The Netherlands.
Perret
C M
CM
van Vlijmen-Willems
I M
IM
Cleutjens
J P
JP
Mackie
E J
EJ
Happle
R
R
Schalkwijk
J
J
D000506:Alopecia Areata / Q000378:metabolism* / Q000473:pathology; D015816:Cell Adhesion Molecules, Neuronal / Q000378:metabolism*; D003238:Connective Tissue / Q000378:metabolism*; D016326:Extracellular Matrix Proteins / Q000378:metabolism*; D005353:Fibronectins / Q000378:metabolism; D006197:Hair / Q000166:cytology / Q000378:metabolism* / Q000473:pathology; D006497:Heparan Sulfate / Q000378:metabolism; D006801:Humans; D007150:Immunohistochemistry; D007797:Laminin / Q000378:metabolism; D012535:Scalp / Q000166:cytology / Q000378:metabolism*; D019063:Tenascin
D015816:Cell Adhesion Molecules, Neuronal; D016326:Extracellular Matrix Proteins; D005353:Fibronectins; D006497:Heparan Sulfate; D007797:Laminin; D019063:Tenascin