Development of the interphotoreceptor matrix inXenopus laevis
| العنوان: | Development of the interphotoreceptor matrix inXenopus laevis |
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| المؤلفون: | Robert A. Landers, Joe G. Hollyfield, Devjani Lahiri |
| المصدر: | Journal of Morphology. 223:325-339 |
| بيانات النشر: | Wiley, 1995. |
| سنة النشر: | 1995 |
| مصطلحات موضوعية: | Male, Wheat Germ Agglutinins, Xenopus, Biology, Interphotoreceptor matrix, Eye, Retina, Xenopus laevis, chemistry.chemical_compound, medicine, Extracellular, Animals, Photoreceptor Cells, Eye Proteins, Pigment Epithelium of Eye, Glycoproteins, Retinal pigment epithelium, Retinal, Anatomy, biology.organism_classification, Wheat germ agglutinin, Cell biology, Molecular Weight, medicine.anatomical_structure, chemistry, Cytochemistry, Female, Animal Science and Zoology, sense organs, Developmental Biology |
| الوصف: | Xenopus laevis interphotoreceptor matrix (IPM) contains a relatively aqueous insoluble wheat germ agglutinin (WGA)-binding component containing unidentifiied sialoglycoconjugates (Wood et al [1984] J. Comp. Neurol. 228:299–307). The appearance of WGA-binding macromolecules in the IPM was assessed during late embryonic stages (32–45) and in retinal rudiment cultures, using lectin cyutochemistry and Western blotting techniques. Metabolic labeling of the neural retina versus retinal pigment epithelium (RPE)-choroid of juvenile Xenopus with 35S-MET was also evaluated in vivo and in vitro. Lectin cytochemistry of eyes from developmental stages 32–42 demonstrated distinct WGA-ferritin-binding sites on the developing outer segment membranes and in the IPM compartment. At stages 44–46 extensive WGA-binding domains were present as an extracellular network with other randomly scattered domains near the retinal pigment epithelium. Retinal rudiments from stage 32–33 were isolated and allowed to differentiate in hanging drop culture (Hollyfield and Witkowsky [1974] J. Exp. Zool. 189:357–377) with or without an iinvesting pigment epithelium. Cultures developing with RPE exhibited an elaborate IPM with an anastomosing meshwork of WGA-ferritin binding sites. In the absence of RPE only limited amoutns of binding restricted to the immediate vicinity of the developing photoreceptor outer segement membranes was observed. When Western blots were probed with WGA-HRP, stage 32–45 retinas demonstrated a major WGA-binding band of 126 kD. Similar amounts of WGA-binding macromolecules were synthesized in preparations cultured in the presence or absence of the investing RPE. During development the major WGA-binding component is a 126-kD protein. Equivalent synthesis of this protein in the presence and absence of RPE suggests that the PE is not required for synthesis of this 126-kD component. These results suggest that the retina is the primary site of synthesis of the WGA-binding components of the Xenopus IPM, whereas the PE plays a principal role in their assembly and organization. © 1995 Wiley-Liss, Inc. |
| تدمد: | 1097-4687 0362-2525 |
| الوصول الحر: | https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7957c819738d011cb274e899095e1f10Test https://doi.org/10.1002/jmor.1052230308Test |
| حقوق: | CLOSED |
| رقم الانضمام: | edsair.doi.dedup.....7957c819738d011cb274e899095e1f10 |
| قاعدة البيانات: | OpenAIRE |
| تدمد: | 10974687 03622525 |
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