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.
| Original language | English |
|---|---|
| Pages (from-to) | 86-90 |
| Number of pages | 5 |
| Journal | Archives of Dermatological Research |
| Volume | 283 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 1991 |
Keywords
- Alopecia Areata/metabolism
- Cell Adhesion Molecules, Neuronal/metabolism
- Connective Tissue/metabolism
- Extracellular Matrix Proteins/metabolism
- Fibronectins/metabolism
- Hair/cytology
- Heparitin Sulfate/metabolism
- Humans
- Immunohistochemistry
- Laminin/metabolism
- Scalp/cytology
- Tenascin
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