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11. |
Changes in conjunctival lymphocyte populations induced by oral immunization withChlamydia trachomatis |
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Current Eye Research,
Volume 5,
Issue 12,
1986,
Page 973-979
WhittumJudith A.,
PrendergastRobert A.,
TaylorHugh R.,
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摘要:
The populations of lymphocyte subsets in the conjunctiva were assessed in monkeys enterically immunized with different preparations ofChlamydia trachomatisprior to ocular challenge. Subsets were identified in immunohistochemical studies employing cross-reactive anti-human monoclonal and polyclonal reagents. Ocular challenge of orally immunized animals resulted in more equal numbers of T-helper and T suppressor/cytotoxic cells, compared to the higher proportion of TSseen in naive monkeys. TH:TS/CTLratios of 1.0-2.0 and 0.1-0.5 respectively were observed. Orally immunized monkeys also showed proportionately more IgA- and IgG-bearing cells and less IgM-bearing cells. B cells of each class were commonly seen immediately under the epithelial basement membrane. Although oral immunization induced a number of changes in the proportions and distribution of lymphocyte subsets which subsequently appeared in the conjunctiva, these changes were not correlated with disease outcome, except for the appearance of increased proportions of follicular IgA-bearing cells in partially protected monkeys.
ISSN:0271-3683
DOI:10.3109/02713688608995179
出版商:Taylor&Francis
年代:1986
数据来源: Taylor
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12. |
Immunocytochemical localization of chondroitin sulfates in the interphotoreceptor matrix of the normal and dystrophic rat retina |
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Current Eye Research,
Volume 5,
Issue 12,
1986,
Page 981-993
PorrelloKathryn,
LavailMatthew M.,
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摘要:
The interphotoreceptor matrix (IPM) is a mixture of proteoglycans and glycoproteins through which metabolites must pass in transit between the retinal pigment epithelium (RPE) and the photoreceptor cells. In order to localize various species of chondroitin sulfates in the IPM of the normal and dystrophic rat retina, we have used monoclonal antibodies directed against 6-sulfated chondroitin sulfate (6S), 4-sulfated chondroitin sulfate (4S) and unsulfated chondroitin (OS). Immunofluorescence and immunoperoxidase methods were carried out on frozen and wax-embedded sections of rat eyes. In the normal rat retina, strong labeling with the 6S antibody was observed in the basal IS/OS zone and, to a lesser extent, in the photoreceptor interstices extending to the apical RPE surface. In the RCS retina, the IPM in the basal IS/OS zone and much of the outer segment debris zone were labeled intensely with 6S antibody, but no strong labeling was present at the apical RPE surface. The labeling pattern with OS antibody was similar to that of the 6S antibody for both normal and RCS retinas. We failed to detect any 4S antibody labeling of the IPM in both the normal and RCS retinas using these methods. These results indicate that in the rat retina, the IPM contains 6-sulfated chondroitin sulfate and unsulfated chondroitin proteoglycans that are most concentrated in the basal IS/OS zone and, to a lesser degree, between the photoreceptor outer segments. Furthermore, it appears that the rat IPM contains little or no 4-sulfated chondroitin sulfate or dermatan sulfate proteoglycan.
ISSN:0271-3683
DOI:10.3109/02713688608995180
出版商:Taylor&Francis
年代:1986
数据来源: Taylor
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13. |
S-antigen: identification of the MAbA9-C6 monoclonal antibody binding site and the uveitopathogenic sites |
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Current Eye Research,
Volume 5,
Issue 12,
1986,
Page 995-1004
DonosoLarry A.,
MerrymanCarmen F.,
ShinoharaToshimichi,
DietzscholdBernard,
WistowGrame,
CraftCheryl,
MorleyWynne,
HenryRobert T.,
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摘要:
The location of the monoclonal antibody, MAbA9-C6, binding site and two uveitopathogenic sites in S-antigen have been determined. Using cyanogen bromide, S-antigen was cleaved into nine peptides, designated C1 to C9. MAbA9-C6 bound selectively to one large peptide designated C5, consisting of 122 amino acids. Six peptides (20 to 22 amino acids in length) designated 2, 3, K, L, N and M, corresponding to the entire length of peptide C5, were synthesized chemically. In a radioimmunoassay and a dot-binding immunoassay, MAbA9-C6 bound selectively to one of the six peptides, peptide 3, indicating that this region of peptide C5 contains the MAbA9-C6 binding site. Twelve smaller peptides (ten amino acids in length), corresponding to the amino acid sequence of peptide 3, were synthesized and used in a competitive inhibition binding assay. These studies localized the MAbA9-C6 binding site to a small region within peptide 3. In addition, peptide K and peptide M were highly pathogenic for the induction of experimental autoimmune uveitis (EAU). Clinical and histological evidence of a severe uveo-retinitis, indistinguishable from that seen with native S-antigen, was documented in Lewis rats immunized with the synthetic peptides (50μg), 11-12 days following immunization. Our results show that the MAbA9-C6 binding site and the two uveitopathogenic sites lie in close proximity to each other within the region of S-antigen corresponding to peptide C5. Furthermore, microcomputer analysis of the average hydrophili-city/hydrophobicity values of the amino acid sequence corresponding to peptide C5 shows that the MAbA9-C6 binding site and one uveitopathogenic site (peptide K) lie on the adjacent peaks. The significance of these findings and their relationship to the role of S-antigen in the pathogenesis of EAU and the phototransduction of vision is discussed.
ISSN:0271-3683
DOI:10.3109/02713688608995181
出版商:Taylor&Francis
年代:1986
数据来源: Taylor
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14. |
Editors' note |
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Current Eye Research,
Volume 5,
Issue 12,
1986,
Page 1005-1006
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ISSN:0271-3683
DOI:10.3109/02713688608995182
出版商:Taylor&Francis
年代:1986
数据来源: Taylor
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