title: Inhibition of human retinal pigment epithelial cell attachment, spreading, and migration by the human lectin galectin-1.
abstract: OBJECTIVE
  Adhesion and migration of dislocated retinal pigment epithelial (RPE) cells are initial steps in the pathogenesis of proliferative vitreoretinopathy (PVR). The role of the endogenous lectin, galectin-1, in attachment, spreading, and migration of human RPE cells was investigated from a therapeutic perspective.
  
  
  METHODS
  Human RPE cells were treated with galectin-1 concentrations that ranged 0-250 microg/ml. Cell viability was tested by 3-[4,5-dimethylthiazol-2-yl]-2,5-diphenyltetrazoliumbromide (MTT) assay. Galectin-1 binding to the RPE cells was investigated by immunocytochemistry. Attachment of RPE cells was assessed on 96-well plates coated with laminin, or fibronectin, or galectin-1, or the glycoprotein-lectin combinations and subsequent MTT-testing. RPE migration in the absence or presence of galectin-1 on the respective substrates was tested using a modified Boyden chamber assay with platelet derived growth factor (PDGF)-BB as the chemoattractant. Cellular spreading was characterized by cytoplasmic halo formation of RPE cells after three hours in contact with the surface coating.
  
  
  RESULTS
  Galectin-1 bound to the cell surface. Binding could be inhibited by a beta-galactoside. MTT assays revealed no toxicity within control limits for the concentration range tested. When added to the medium, galectin-1 dose-dependently inhibited RPE cell attachment, spreading, and migration by more than 70%, irrespective of the substratum tested. When coated onto the plastic surface, galectin-1 alone impaired spreading and migration of RPE cells, and reduced attachment to and migration on fibronectin by up to 80%.
  
  
  CONCLUSIONS
  Galectin-1 inhibits RPE cell attachment, migration, and spreading in vitro with no apparent cytotoxicity. This activity of the endogenous effector deserves consideration as a potential therapeutic agent for the prevention of PVR.
authors.affiliation: Department of Ophthalmology, Ludwig-Maximilians-University, Munich, Germany.
authors.forename: Claudia S
authors.initials: CS
authors.lastname: Alge-Priglinger
authors.forename: Sabine
authors.initials: S
authors.lastname: André
authors.forename: Thomas C
authors.initials: TC
authors.lastname: Kreutzer
authors.forename: Cornelia A
authors.initials: CA
authors.lastname: Deeg
authors.forename: Anselm
authors.initials: A
authors.lastname: Kampik
authors.forename: Marcus
authors.initials: M
authors.lastname: Kernt
authors.forename: Harald
authors.initials: H
authors.lastname: Schöffl
authors.forename: Siegfried G
authors.initials: SG
authors.lastname: Priglinger
authors.forename: Hans-Joachim
authors.initials: HJ
authors.lastname: Gabius
mesh_terms: D000328:Adult; D002448:Cell Adhesion / Q000187:drug effects; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism; D002465:Cell Movement / Q000187:drug effects; D048430:Cell Shape / Q000187:drug effects; D002470:Cell Survival / Q000187:drug effects; D002478:Cells, Cultured; D004847:Epithelial Cells / Q000166:cytology / Q000187:drug effects / Q000378:metabolism; D005260:Female; D005353:Fibronectins / Q000494:pharmacology; D037483:Galectin 1 / Q000494:pharmacology* / Q000633:toxicity; D006801:Humans; D007797:Laminin / Q000494:pharmacology; D008297:Male; D008875:Middle Aged; D010857:Pigment Epithelium of Eye / Q000166:cytology* / Q000187:drug effects; D011485:Protein Binding / Q000187:drug effects; D012995:Solubility / Q000187:drug effects
chemical_list: D005353:Fibronectins; D037483:Galectin 1; C445499:LGALS1 protein, human; D007797:Laminin