TY - JOUR
T1 - Basement membrane proteins, interstitial collagens, and fibronectin in neurofibroma
AU - Fleischmajer, R.
AU - Timpl, R.
AU - Dziadek, M.
AU - Lebwohl, M.
N1 - Funding Information:
Normal Schwann cells are able to synthesize collagens I, III, and V [8], collagen IV [9], and Iaminin (4]. In the absence of nerve axons, synthesis is decreased or deposition of an intact basement membrane is impaired [4,9]. Fibroblasts are thought to produce fibronectin and collagen fibrils of large diameter which are deposited in the perineurium [4,5,8]. Schwannoma cell lines produce collagen I and an unknown procollagen [10,11) and also fibronectin and laminin [5,11). The synthesis Manuscript received August 1, 1984; accepted for publication Janu· ary 8, 1985. Supported in part by NIH Grants AM 07376, NATO Grant 1960, and the Deutsche Forschungsgemeinschaft (project Ti 95/6-1). Reprint requests to: Raul Fleischmajer, M.D., Department of Dermatology, Mount Sinai School of Medicine, Ooe Gustave L. Levy Place, New York , New York 10029. Abbreviations: EHS: Engelbreth-Holm-Swarm (sarcomfl) PBS: phosphate-buffered saline, pH 7.2.
PY - 1985
Y1 - 1985
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0021874312&partnerID=8YFLogxK
U2 - 10.1111/1523-1747.ep12275341
DO - 10.1111/1523-1747.ep12275341
M3 - Article
C2 - 3925026
AN - SCOPUS:0021874312
SN - 0022-202X
VL - 85
SP - 54
EP - 59
JO - Journal of Investigative Dermatology
JF - Journal of Investigative Dermatology
IS - 1
ER -