Abstract
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.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Alopecia Areata / metabolism*
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Alopecia Areata / pathology
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Cell Adhesion Molecules, Neuronal / metabolism*
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Connective Tissue / metabolism*
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Extracellular Matrix Proteins / metabolism*
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Fibronectins / metabolism
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Hair / cytology
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Hair / metabolism*
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Hair / pathology
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Heparitin Sulfate / metabolism
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Humans
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Immunohistochemistry
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Laminin / metabolism
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Scalp / cytology
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Scalp / metabolism*
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Tenascin
Substances
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Cell Adhesion Molecules, Neuronal
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Extracellular Matrix Proteins
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Fibronectins
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Laminin
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Tenascin
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Heparitin Sulfate