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<mods:namePart>Gato Casado, Ángel Luis</mods:namePart>
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<mods:namePart>Martín, C.</mods:namePart>
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<mods:namePart>Alonso Revuelta, María Isabel</mods:namePart>
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<mods:namePart>Martínez Álvarez, C.</mods:namePart>
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<mods:namePart>Moro Balbás, José Antonio</mods:namePart>
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<mods:dateIssued encoding="iso8601">2001</mods:dateIssued>
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<mods:identifier type="citation">Exp. Eye. Res., 2001, 58 p.1-8</mods:identifier>
<mods:identifier type="issn">0014-4835</mods:identifier>
<mods:identifier type="uri">http://uvadoc.uva.es/handle/10324/4946</mods:identifier>
<mods:identifier type="doi">10.1006/exer.2001.1060</mods:identifier>
<mods:identifier type="publicationfirstpage">1</mods:identifier>
<mods:identifier type="publicationlastpage">8</mods:identifier>
<mods:identifier type="publicationtitle">Exp. Eye. Res.</mods:identifier>
<mods:identifier type="publicationvolume">58</mods:identifier>
<mods:abstract>Proteoglycans have been implicated in the invagination and formation of various embryonal cavitied&#xd;
primordia. In this paper the expression of chondroitin sulphate proteoglycan is analysed (CSPG) in the lens&#xd;
primordium during lens vesicle formation, and demonstrate that this proteoglycan has a speci®c&#xd;
distribution pattern with regard to invagination and fusion processes in the transformation of placode into&#xd;
lens vesicle. More speci®cally, CSPG was detached in: (1) the apical surface of lens epithelial cells, where&#xd;
early CSPG expression was observed in the whole of the lens placode whilst in the vesicle phase it was&#xd;
restricted to the posterior epithelium; (2) intense CSPG expression in the basal lamina, which remained&#xd;
constant for the entire period under study; (3) CSPG expression in the intercellular spaces of the lens&#xd;
primordium epithelium, which increased during the invagination of the primordium and which at the&#xd;
vesicle stage was more evident in the posterior epithelium; and (4) CSPG expression on the edges of the&#xd;
lens placode both prior to and during fusion. Treatment with b-D-xyloside causes signi®cant CSPG&#xd;
depletion in the lens primordium together with severe alterations in the invagination and fusion of the&#xd;
lens vesicle; this leads to the formation of lens primordia which in some cases remain practically ¯at or&#xd;
show partial invagination defects or fusion disruption. Similar results were obtained by enzyme digestion&#xd;
with chondroitinase AC but not with type II heparinase, which indicates that alterations induced by b-Dxyloside&#xd;
were due to interference in CSPG synthesis. The ®ndings demonstrate that CSPG is a common&#xd;
component of the lens primordium at the earliest developmental stages during which it undergoes speci®c&#xd;
modi®cations. It also includes experimental evidence to show that `in vivo' CSPG plays an important role&#xd;
in the invagination and fusion processes of the lens primordium. # 2001 Academic Press&#xd;
Key words: lens development; CSPG; b-D-xyloside; extracellular matrix; epithelial invagination</mods:abstract>
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<mods:languageTerm authority="rfc3066">eng</mods:languageTerm>
</mods:language>
<mods:accessCondition type="useAndReproduction">Attribution-NonCommercial-NoDerivatives 4.0 International</mods:accessCondition>
<mods:subject>
<mods:topic>Embriología</mods:topic>
</mods:subject>
<mods:titleInfo>
<mods:title>Chondroitin sulphate proteoglycan is involved in lens vesicle morphogenesis in chick embryos</mods:title>
</mods:titleInfo>
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