Objective One part of the project determined the proteins present in the matrix of exfoliation substance and the sites where exfoliation substance is synthesised. In all specimens, amyloid P component and an elastin microfibrillar associated glycoprotein, gp115 was identified in exfoliation substance. Elastin was present in the stroma of the normal iris and of the exfoliative iris but not within exfoliation substance. The most likely source of exfoliation substance within the stroma of the iris seemed to be the perivascular cells which surround the vascular endothelium, and the vascular endothelial cells were not primarily involved. The most likely source of exfoliation substance within the stroma of the iris seemed to be the perivascular cells which surround the vascular endothelium, and the vascular endothelial cells were not primarily involved. A prospective consecutive study has been set up to establish the prevalence of exfoliation syndrome and its influence on the surgical outcome in cataract surgery. Another study was set up to determine the terminal glycosylation of structural glycoproteins supposed to form a constituent part of exfoliation substance, using lectin histochemistry and sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) with blotting and lectin binding. Formalin fixation of exfoliation material induced conformational changes in the glycoproteins in such a way that various sugar moieties were presented in random fashion to the lectins. Unfixed exfoliation material consistently presented the same sugar moieties and harboured a region with a cluster of fucose molecules, which was not expressed in normal basement membranes. However, both exfoliation material and basement membranes expressed fucose in single molecular arrangements. Boiling with SDS uncoiled the glycoproteins exposing fucose in both normal and exfoliative substances. Some of these apparently contradictory findings could be explained by the following hypothesis. In the disease state there is an exfoliation glycoprotein, which partially resembles a structural glycoprotein normally present in the basement membrane complex, but which is not, however, in a fully glycosylated form. If one supposes that the normal fully glycosylated molecule is paired or mirror imaged and curled up in such a fashion that more centrally located fucose molecules are masked, these regions will not be accessible to the tissue plasminogen activator (TPA) lectins. In the abnormal state, a lack of terminal sugar moieties on one of the glycoprotein pairs may expose the fucose molecules, thus making them accessible to the TPA lectin. Fields of science medical and health sciencesclinical medicineophthalmologyglaucomamedical and health sciencesclinical medicinesurgerynatural scienceschemical sciencesinorganic chemistryalkali metalsnatural sciencesbiological sciencesbiochemistrybiomoleculesproteinsnatural scienceschemical scienceselectrochemistryelectrophoresis Programme(s) FP2-SCIENCE - Programme plan (EEC) to stimulate the international cooperation and interchange needed by European research scientists (SCIENCE), 1988-1992 Topic(s) Data not available Call for proposal Data not available Funding Scheme CSC - Cost-sharing contracts Coordinator University of Glasgow EU contribution No data Address 38 Church Street G11 6NT Glasgow United Kingdom See on map Total cost No data Participants (3) Sort alphabetically Sort by EU Contribution Expand all Collapse all Aristotle University of Thessaloniki Greece EU contribution No data Address University Campus 54006 Thessaloniki See on map Total cost No data Aristotle University of Thessaloniki Greece EU contribution No data Address University Campus 54006 Thessaloniki See on map Total cost No data Københavns Universitet Denmark EU contribution No data Address 10,Nørregade 1017 København K See on map Total cost No data
