Basement membrane proteins, interstitial collagens, and fibronectin in neurofibroma

Abstract

The distribution and nature of extracellular matrix proteins in neurofibroma tissue was studied by indirect immunofluorescence, immunoelectron microscopy, immunoblotting, and rotary shadowing. The most striking feature was an extensive network of basement membranes localized mainly around Schwann cells and small blood vessels. The major components, collagen IV, laminin, and nidogen, were mainly deposited in the lamina densa. Some laminin and nidogen could be extracted with 0.5 M NaCl and were shown by electrophoresis to have the characteristic chain and fragment patterns described previously for these proteins isolated from the mouse Engelbreth-Holm-Swarm (EHS) sarcoma. Fragments of collagen IV and collagen VI were solubilized by limited proteolytic digestion and identified after rotary shadowing. The more remote interstitial regions of the tumor contained cross-striated collagen fibrils which were composed of collagen III (diameter, 20-30 nm) or collagen I (diameter, 40-50 nm). Collagen fibrils thicker than 80 nm were not found. The interstitial regions also contained collagen VI as a fine filamentous network near cells and between collagen fibrils. Deposits of fibronectin were rather small and showed a scattered distribution. The data indicate that Schwann cells contribute considerably to matrix production in neurofibroma which may therefore be a suitable model for studying basement membranes of neuroectodermal origin.