Intracellular detection of laminin α2 chain in skin by electron microscopy immunocytochemistry: Comparison between normal and laminin α2 chain deficient subjects

S. Squarzoni, M. Villanova, P. Sabatelli, A. Malandrini, P. Toti, A. Pini, L. Merlini, G. C. Guazzi, N. M. Maraldi

Research output: Contribution to journalArticle


The aim of this study is to localize the α2 laminin chain in normal human skin. The methods used were immune-gold cytochemistry on cryo-ultramicrotomy sections and thin-section-fracture-label, together with electron microscopy observation. Results were compared with light microscopy peroxidase immune-staining. Both normal skin samples and skin biopsies from laminin α2 chain deficient congenital muscular dystrophy affected patients were studied. The results show that, in normal skin, the laminin α2 chain is spread throughout the cytoplasm of basal keratinocytes, while it appears associated with desmosomal tonofilaments in the spinous and granular epidermal layers; in skin samples from dystrophic patients the laminin α2 chain was not detectable, These data suggest that the function of the laminin α2 chain is different in the epidermis as compared to that in muscle and peripheral nerve, where it is localized in the basement membrane.

Original languageEnglish
Pages (from-to)91-98
Number of pages8
JournalNeuromuscular Disorders
Issue number2
Publication statusPublished - Mar 1997



  • Cytoskeleton
  • Electron microscopy immunocytochemistry
  • Extracellular matrix
  • Laminin 2
  • Signalling
  • Thin section fracture label

ASJC Scopus subject areas

  • Clinical Neurology
  • Pediatrics, Perinatology, and Child Health
  • Developmental Neuroscience
  • Neurology

Cite this