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- Ghosh, F, et al.
(författare)
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Graft-host connections in long-term full-thickness embryonic rabbit retinal transplants
- 1999
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Ingår i: Investigative Ophthalmology and Visual Science. - 0146-0404. ; 40:1, s. 32-126
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Tidskriftsartikel (refereegranskat)abstract
- PURPOSE: To establish neuronal connections in the rod and cone pathway between laminated rabbit retinal transplants and the host retina.METHODS: Fourteen adult rabbits received a complete full-thickness embryonic transplant. After survival times of 3 to 10 months, the retinas were studied under light microscope and with immunohistochemistry. Antibodies against protein kinase C (PKC), parvalbumin, and calbindin were used to label rod bipolar cells, AII amacrine cells, and cone bipolar cells, respectively. The AB5 antibody was used to label ganglion cells.RESULTS: The transplants displayed laminated morphology with layers parallel to the host retinal pigment epithelium. In the oldest specimens (10 months after surgery), laminated layers of graft and host approached each other and almost reconstructed the normal retinal appearance. The ganglion and cone bipolar cells of the host survived well, as was seen with AB5 and calbindin double-labeling. Connections between cone bipolar cells in the graft and ganglion cells in the host were not common. PKC-labeled rod bipolar cells and parvalbumin-labeled AII amacrine cells of host and graft showed sprouting activity directed toward an intermediate plexiform layer located between the graft and host. In specimens double-labeled with PKC and parvalbumin, this intermediate plexiform layer was seen to contain numerous PKC- and parvalbumin-labeled processes. Direct connections between rod bipolar and AII amacrine cells in host and graft were seen in the 10-month specimens.CONCLUSIONS: Full-thickness embryonic transplants survive for at least 10 months, and normal laminated morphology develops. Host and graft fuse and together contribute nerve cell processes to an intermediate plexiform layer. Direct graft-host contacts are also present between neuronal types that in the normal retina participate in the rod pathway.
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- Ghosh, F, et al.
(författare)
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Immunohistochemical markers in full-thickness embryonic rabbit retinal transplants
- 1999
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Ingår i: Ophthalmic Research. - : S. Karger AG. - 0030-3747 .- 1423-0259. ; 31:1, s. 5-15
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Tidskriftsartikel (refereegranskat)abstract
- PURPOSE: To examine immunohistochemical markers in straight, well-laminated retinal transplants with special attention paid to the interphotoreceptor matrix, the Müller cells and the ganglion cells as these three retinal components have been abnormal in transplants produced by previous methods.METHODS: Nine rabbits underwent subretinal transplantation of a complete full-thickness embryonic neuroretina. After 31 or 49 days, the transplants were stained for light microscopy and processed for immunohistochemistry.RESULTS: Six of 9 eyes contained transplants with straight, well-laminated regions with all light-microscopic characteristics of a normal retina. In the outer segment region, the expression of peanut agglutinin showed segmental labeling of cone domains in the interphotoreceptor matrix, and interphotoreceptor retinoid binding protein immunoreactivity was found. Glial fibrillary acidic protein and vimentin immunoreactivity revealed normal Müller cell morphology. In 3 transplants the AB5-antibody-labeled ganglion cells in the ganglion cell layer and all transplants contained nerve fibers in the nerve fiber layer labeled by an antibody against neurofilament of 160 kD. The latter also labeled fibers connecting the transplant with the host.CONCLUSIONS: Full-thickness embryonic retinal transplants develop the normal retinal appearance and display several of the retinal components necessary for normal function which are not found in transplants produced by previous methods.
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- Pal, S., Chandra (Sanyal), S., Chowdhury, S., Sarkar, D., Ghosh, A.N., DasGupta, C.
(författare)
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Complementary role of two fragments of domain V of 23 S ribosomal RNA in protein folding
- 1999
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Ingår i: J Biol Chem. ; 274:46, s. 32771-7
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Tidskriftsartikel (refereegranskat)abstract
- We have shown that the domain V of bacterial 23 S rRNA could fold denatured proteins to their active state. This segment of 23 S rRNA could further be split into two parts. One part containing mainly the central loop of domain V could bind denatured human
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