Expression of tenascin in perifollicular connective tissue: comparison of normal scalp and alopecia areata

Arch Dermatol Res. 1991;283(2):86-90. doi: 10.1007/BF00371614.

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

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Alopecia Areata / metabolism*
  • Alopecia Areata / pathology
  • Cell Adhesion Molecules, Neuronal / metabolism*
  • Connective Tissue / metabolism*
  • Extracellular Matrix Proteins / metabolism*
  • Fibronectins / metabolism
  • Hair / cytology
  • Hair / metabolism*
  • Hair / pathology
  • Heparitin Sulfate / metabolism
  • Humans
  • Immunohistochemistry
  • Laminin / metabolism
  • Scalp / cytology
  • Scalp / metabolism*
  • Tenascin

Substances

  • Cell Adhesion Molecules, Neuronal
  • Extracellular Matrix Proteins
  • Fibronectins
  • Laminin
  • Tenascin
  • Heparitin Sulfate