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Characterization of galactose-containing glycoconjugates in the human retina: A lectin histochemical study

 

作者: KivelaTero,  

 

期刊: Current Eye Research  (Taylor Available online 1990)
卷期: Volume 9, issue 12  

页码: 1195-1209

 

ISSN:0271-3683

 

年代: 1990

 

DOI:10.3109/02713689009003476

 

出版商: Taylor&Francis

 

数据来源: Taylor

 

摘要:

Seven specimens of morphologically normal formalin-fixed and paraffin-embedded human retina were studied using a panel of fourteen biotinylated lectins, all of which react with glycoconjugates containing galactose andN-acetylgalactosamine residues.Agaricus bi-sporus(ABA),Bauhiniapurpurea (B?A),Phaseolus vulgaris(PHA-E), peanut (PNA) andRicinus communis(RCA-1) agglutinins labeled photoreceptor cells prior to enzymatic predigestion. BPA and PNA bound specifically to cones. The plexiform layers reacted with ABA, BPA and PHA-E, while only ABA and PHA-E labeled the nuclear layers. After pretreatment with neuraminidase to remove terminal sialii acid, all five lectins, as well asErythrina cristagalli(ECA),Helixpomatia(HP A) andMadura pomifera(MPA) agglutinins labeled both rods and cones. Furthermore, the plexiform layers additionally reacted withECAPNA and RCA-1, and the nuclear layers with BPA and RCA-1 after neuraminidase pretreatment. Retinal vascular endothelial cells consistently bound ABA, ECA, PHA-E and RCA-1, but they could also bine BPA, HP A,Bandeiraea simplicifolia(BSA-I),Dolichos biflorus(DBA) andEuonymus europaeus(EEA) agglutinins in unpretreated sections, a well as MP A, PNA, soybean (SBA) andSophora japonica(SJA) agglutinins subsequent to predigestion with neuraminidase. The nonpig-mented ciliary epithelium reacted with the same lectins as photorecepfc cells, but it was also labeled by DBA.Sambucus nigraagglutinin (SNA) did not specifically bind to any intraocular structure. These findings favor the theory that, in unpretreated specimens, Gal(Bl-→3)GalNAc (BPA and PNA) is mainly responsible for labeling of cones, while Gal(Bl-→3/4)GlcNAc units, partly substituted with terminal sialic acid (PHA-E and RCA-1), explain labeling of rods. Following pretreatment with neuraminidase, further Gal(Bl-→3)GalNAc (BPA and PNA) and, especially, Gal(Bl-→3/4)GlcNAc (BPA, ECA, PHA-E, PNA and RCA-1) and aGalNAc units (BPA, HP A and MP A), the latter partly linked to the protein backbone, contribute to labeling of photoreceptoi cells. Gal(Bl-→3/4)GlcNAc units may be mainly responsible for labeling of nuclear and plexiform layers. Finally, other related receptor sites (SBA and SJA), some of which are blood-group specific (BSA-I, DBA, EEA and HP A) are restricted to retinal vascular endothelia.

 

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