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dc.contributor.author | Gato Casado, Ángel Luis | |
dc.contributor.author | Martín, C. | |
dc.contributor.author | Alonso Revuelta, María Isabel | |
dc.contributor.author | Martínez Álvarez, C. | |
dc.contributor.author | Moro Balbás, José Antonio | |
dc.date.accessioned | 2014-06-09T06:56:44Z | |
dc.date.available | 2014-06-09T06:56:44Z | |
dc.date.issued | 2001 | |
dc.identifier.citation | Exp. Eye. Res., 2001, 58 p.1-8 | es |
dc.identifier.issn | 0014-4835 | es |
dc.identifier.uri | http://uvadoc.uva.es/handle/10324/4946 | |
dc.description | Producción Científica | es |
dc.description.abstract | Proteoglycans have been implicated in the invagination and formation of various embryonal cavitied primordia. In this paper the expression of chondroitin sulphate proteoglycan is analysed (CSPG) in the lens primordium during lens vesicle formation, and demonstrate that this proteoglycan has a speci®c distribution pattern with regard to invagination and fusion processes in the transformation of placode into lens vesicle. More speci®cally, CSPG was detached in: (1) the apical surface of lens epithelial cells, where early CSPG expression was observed in the whole of the lens placode whilst in the vesicle phase it was restricted to the posterior epithelium; (2) intense CSPG expression in the basal lamina, which remained constant for the entire period under study; (3) CSPG expression in the intercellular spaces of the lens primordium epithelium, which increased during the invagination of the primordium and which at the vesicle stage was more evident in the posterior epithelium; and (4) CSPG expression on the edges of the lens placode both prior to and during fusion. Treatment with b-D-xyloside causes signi®cant CSPG depletion in the lens primordium together with severe alterations in the invagination and fusion of the lens vesicle; this leads to the formation of lens primordia which in some cases remain practically ¯at or show partial invagination defects or fusion disruption. Similar results were obtained by enzyme digestion with chondroitinase AC but not with type II heparinase, which indicates that alterations induced by b-Dxyloside were due to interference in CSPG synthesis. The ®ndings demonstrate that CSPG is a common component of the lens primordium at the earliest developmental stages during which it undergoes speci®c modi®cations. It also includes experimental evidence to show that `in vivo' CSPG plays an important role in the invagination and fusion processes of the lens primordium. # 2001 Academic Press Key words: lens development; CSPG; b-D-xyloside; extracellular matrix; epithelial invagination | es |
dc.format.mimetype | application/pdf | es |
dc.language.iso | eng | es |
dc.publisher | Ideal | es |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | es |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0/ | |
dc.subject | Embriología | es |
dc.title | Chondroitin sulphate proteoglycan is involved in lens vesicle morphogenesis in chick embryos | es |
dc.type | info:eu-repo/semantics/article | es |
dc.identifier.doi | 10.1006/exer.2001.1060 | es |
dc.relation.publisherversion | http://www.idealibrary.com | es |
dc.identifier.publicationfirstpage | 1 | es |
dc.identifier.publicationlastpage | 8 | es |
dc.identifier.publicationtitle | Exp. Eye. Res. | es |
dc.identifier.publicationvolume | 58 | es |
dc.peerreviewed | SI | es |
dc.rights | Attribution-NonCommercial-NoDerivatives 4.0 International |
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