Lamellar Bodies in Synoviocytes, Mesothelium and Specific Epithelia as Possible Site of Auto-Antigen in Rheumatoid Disease

Dobbie, James W.; Tasiaux, Nicole; Meijers, P; Anderson, J. D.; Bodart, C; Hind, C. R. K.; Bourguet, C.; Perret, Jason

doi:10.1093/rheumatology/33.6.508

Cited by 26 publications

(13 citation statements)

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“…8 as a cause for primary atrophic rhinitis. Dobbie et al 20 detected antibodies raised against surfactant protein-A, exhibit a ranking of tissue reactivity in area, intensity and density of cells that also paralleled the frequency and degree of pathological involvement characteristic of rheumatoid disease.…”

Section: Discussionmentioning

confidence: 96%

Study of surfactant level in cases of primary atrophic rhinitis

Sayed

Abou-Elhamd²,

Abdel‐Kader³

et al. 2000

J. Laryngol. Otol.

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The surfactant system of the nose was examined biochemically in control cases and compared to cases of primary atrophic rhinitis. The study group included 25 cases with primary atrophic rhinitis compared to 10 normal volunteers. Biochemical analysis of the nasal aspirate in these cases revealed the presence of phospholipids constituting surfactant with phosphatidylcholine constituting 75.35 per cent of the total phospholipids. Biochemical analysis of the nasal aspirate in cases with primary atrophic rhinitis revealed a significant decrease in the total phospholipids compared to normal cases and also a significant change in the phospholipid profile. Thus significant biochemical changes in the surfactant system of the nose is an evident and early finding in cases of primary atrophic rhinitis. This suggests a possible role for surfactant deficiency in the aetiopathogenesis of cases of primary atrophic rhinitis.

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Section: Discussionmentioning

confidence: 96%

Study of surfactant level in cases of primary atrophic rhinitis

Sayed

Abou-Elhamd²,

Abdel‐Kader³

et al. 2000

J. Laryngol. Otol.

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“…9,10 However, although these results strongly suggest that mammalian hsp60 is an important target autoantigen in PIA, there is no direct evidence as to whether hsp60 from joints or other joint antigens also play a role in the development of the disease. The view that responses to multiple antigens in the target tissue may be necessary for disease to develop is supported both by the wide range of candidate autoantigens implicated in the pathogenesis of RA, [11][12][13][14] and by the identification of multiple autoantigens in other autoimmune diseases, such as autoimmune haemolytic anaemia (AIHA) 15,16 and diabetes. [17][18][19][20] The aim of the current work was therefore to determine whether the autoimmune response in PIA is focused solely on hsp, or whether other joint antigens are also targeted.…”

Section: Introductionmentioning

confidence: 99%

B‐ and T‐cell autoantigens in pristane‐induced arthritis

et al. 1996

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SUMMARYPristane-induced arthritis (PIA) is a murine disease resembling rheumatoid arthritis (RA) which is characterized by autoimmune responses to joint tissues. To identify the range of potential antigens targeted in PIA, proteins from arthritic or normal joint extracts were fractionated by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) and systematically screened for the ability to react with either serum IgG, or cultured splenic T cells, obtained from healthy or arthritic mice. Extracts from both normal and arthritic animals contained multiple proteins that were capable of reacting with murine serum IgG in immunoblotting experiments. In healthy controls, more bands were identified in extracts prepared from 30-week-old mice than from 8-week-old animals, but the widest range of proteins bound were derived from arthritic joints. Furthermore, the sera from PIA-positive mice reacted with more bands from each of the extracts than did normal sera. Fractionated extracts prepared from healthy joints failed to stimulate the in vitro proliferation of splenic T cells from either normal or arthritic animals. When arthritic joint components were screened, T cells from healthy mice responded weakly to some fractions, but multiple fractions elicited strong proliferation by T cells from mice with PIA. A band of apparent molecular mass 60 000 was the protein most commonly bound by serum IgG from arthritic mice, and the corresponding fraction stimulated the highest responses by T cells from PIA-positive animals. These results are consistent with the notion that the 60 000 MW mammalian heatshock protein is an important antigen in PIA, but that the autoimmune response diversifies with the development of arthritis to target multiple joint components.

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“…Recent reports indicate that the SP-A gene also is expressed in other tissues. Surfactant-like particles have been detected in rat and human colon [ 16 ] ; SP-A has been detected in the peritoneal cavity in rat and human [ 34,35 ] , in the middle ear in pig and rabbit [ 17,36 ] , and identi® ed in rat small and large intestine. In all these sites, SP-A is likely to be involved in innate immune processes.…”

Section: Discussionmentioning

confidence: 99%

Both Human Sp-A1 and Sp-A2 Genes Are Expressed in Small and Large Intestine

Lin

deMello

Phelps

et al. 2001

Pediatric Pathology & Molecular Medicine

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& The human SP-A locus consists of two functional genes and one pseudogene, and SP-A is shown to play a role in local host defense and the regulation of in¯ammation in lung. Because the intestine, like the lung, is constantly exposed to foreign and potentially harmful substances, we investigated the hypothesis that both human SP-A genes are expressed in intestine. We demonstrate that both SP-A genes are expressed in human small and large intestine. The presence of SP-A mRNA in human intestine was detected by reverse transcriptionpolymerase chain reaction ( RT -PCR ) , Northern blot analysis, and immunohistochemistry. The size of intestinal SP-A mRNA is the same as that in human lung, but the level of expression, compared with that in the lung, is very low in both the small and large intestine. Immunohistochemical analysis revealed positive reactivity for SP-A in a subgroup of epithelial cells in the intestine. Expression of both SP-A1 and SP-A2 genes was established by gene-speci® c PCR ampli® cation, PCR-based converted RFLP discrimination, and direct sequencing of RT -PCR products. We speculate that SP-A in the intestine plays a role in local host defense and in¯ammation.

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Lamellar Bodies in Synoviocytes, Mesothelium and Specific Epithelia as Possible Site of Auto-Antigen in Rheumatoid Disease

Cited by 26 publications

References 0 publications

Study of surfactant level in cases of primary atrophic rhinitis

Study of surfactant level in cases of primary atrophic rhinitis

B‐ and T‐cell autoantigens in pristane‐induced arthritis

Both Human Sp-A1 and Sp-A2 Genes Are Expressed in Small and Large Intestine

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