Thy-1 is a neuronal and glial surface antigen which interacts with matrix proteins and plasminogen activator |
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Authors: | P. Liësi E. -M. Salonen D. Dahl A. Vaheri S. -J. Richards |
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Affiliation: | (1) Recombinant DNA Laboratory, University of Helsinki, Valimotie 7, SF-00380 Helsinki, Finland;(2) Department of Virology, University of Helsinki, Haartmaninkatu 3, SF-00290 Helsinki, Finland;(3) SCI Research Medical Centre, Veterans Administration, 1400 Veterans of Foreign Wars Parkway, 02132 West Roxbury, MA, USA;(4) MRC Molecular Genetics Unit, Addenbrookes Hospital, Hills Road, CB2 2QH Cambridge, UK |
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Abstract: | Summary Thy-1 antigen is expressed at high levels in the thymus and in adult brain of rodents however its function remains undetermined. We report that immobilised Thy-1 binds laminin, fibronectin and the less active precursor form of the tissue type plasminogen activator (t-PA) yet it does not bind urokinase. The incorporation of serine protease inhibitors within the experimental procedures suggested that Thy-1 bound to the lysine-containing, protein-binding domain of t-PA thus leaving the active site available to interact with other proteins. By using an immunocytochemical approach designed to maximally preserve Thy-1 antigenicity, we were able to demonstrate that in the adult rat peripheral nervous system (PNS) Thy-1 was seen to co-localise with laminin on the Schwann cell membranes and accumulated at the nodes of Ranvier within sciatic nerve. The only neuronal structures to express Thy-1 within the PNS were the unmyelinated nerve fibres. In the adult rat central nervous system (CNS), the most distinct and novel association of Thy-1 was its presence along the myelin forming glial cells and their fibres. |
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Keywords: | Glial cells Fibronectin Laminin Proteases Thy-1 Rat |
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