title: Composition, synthesis, and assembly of the embryonic chick retinal basal lamina.
abstract: To study the biology of basal laminae in the developing nervous system the protein composition of the embryonic retinal basal lamina was investigated, the site of synthesis of its proteins in the eye was determined, and basal lamina assembly was studied in vivo in two assay systems. Laminin, nidogen, agrin, collagen IV, and XVIII are major constituents of the retinal basal lamina. However, only agrin is synthesized by the retina, whereas the other matrix constituents originate from cells of the ciliary body, the lens, or the optic disc. The synthesis from extraretinal tissues infers that the retinal basal lamina proteins must be shed from their tissues of origin into the vitreous body and from there bind to receptor proteins provided by the retinal neuroepithelium. The fact that all proteins typical for the retinal basal lamina are abundant in the vitreous body and a new basal lamina is only formed when the vitreous body was directly adjacent to the retina is consistent with the contention of the vitreous body having a function in retinal basal lamina formation. Basal lamina assembly was also studied after disrupting the retinal basal lamina by intraocular injection of collagenase. The basal lamina regenerated after chasing the collagenase with Matrigel, which served as a collagenase inhibitor. The basal lamina was reconstituted within 6 h. However, the regenerated basal lamina was located deeper in the retina than normal by reconstituting along the retracted neuroepithelial endfeet demonstrating that these endfeet are the preferred site of basal lamina assembly.
authors.affiliation: Department of Neurobiology, University of Pittsburgh, 1402 East Biological Science Tower, Pittsburgh, Pennsylvania 15261, USA.
authors.forename: W
authors.initials: W
authors.lastname: Halfter
authors.forename: S
authors.initials: S
authors.lastname: Dong
authors.forename: B
authors.initials: B
authors.lastname: Schurer
authors.forename: A
authors.initials: A
authors.lastname: Osanger
authors.forename: W
authors.initials: W
authors.lastname: Schneider
authors.forename: M
authors.initials: M
authors.lastname: Ruegg
authors.forename: G J
authors.initials: GJ
authors.lastname: Cole
mesh_terms: D018171:Agrin / Q000378:metabolism; D000818:Animals; D001485:Basement Membrane / Q000196:embryology*; D015153:Blotting, Western; D002642:Chick Embryo; D003094:Collagen / Q000378:metabolism; D017364:Collagenases / Q000378:metabolism; D046508:Culture Techniques; D005109:Extracellular Matrix; D019812:Heparan Sulfate Proteoglycans; D006497:Heparan Sulfate / Q000378:metabolism; D017403:In Situ Hybridization; D007797:Laminin / Q000378:metabolism; D008562:Membrane Glycoproteins / Q000378:metabolism; D008856:Microscopy, Fluorescence; D009420:Nervous System / Q000196:embryology*; D011509:Proteoglycans / Q000378:metabolism; D012038:Regeneration; D012160:Retina / Q000196:embryology*; D019063:Tenascin / Q000378:metabolism; D013997:Time Factors; D014822:Vitreous Body / Q000196:embryology
chemical_list: D018171:Agrin; D003094:Collagen; D017364:Collagenases; D019812:Heparan Sulfate Proteoglycans; D006497:Heparan Sulfate; D007797:Laminin; D008562:Membrane Glycoproteins; D011509:Proteoglycans; D019063:Tenascin; C029967:nidogen; C071927:perlecan