Mycoplasmas and arthritis.

Hakkarainen, Kati; Turunen, Hannu; Miettinen, A; Karppelin, Matti; Kaitila, K; Jansson, E

doi:10.1136/ard.51.10.1170

Cited by 23 publications

(9 citation statements)

References 38 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…Mycoplasmas have been implicated in rheumatic arthritis (2,8), fever (4), and AIDS (10, 14). It is not unlikely that MDHM-like substances play a role in some of these syndromes.…”

Section: Discussionmentioning

confidence: 99%

Purification and partial biochemical characterization of a Mycoplasma fermentans-derived substance that activates macrophages to release nitric oxide, tumor necrosis factor, and interleukin-6

Mühlradt

Frisch

1994

Infect Immun

View full text Add to dashboard Cite

Mycoplasmal products may exert a number of diverse in vitro effects on cells of the immune system. A macrophage-activating substance from Mycoplasma fermentans was described in this laboratory and named mycoplasma-derived high-molecular-weight material (MDHM). Using synthesis of nitric oxide by peritoneal cells from endotoxin low-responder mice as an assay system, MDHM was purified as follows. After freeze-thawing of M. fernentans, MDHM activity was sedimented with the membrane fraction. Membranes were delipidated with chloroform-methanol, and MDHM activity was extracted with octyl glucoside. Coextracted proteins were degraded by proteinase K. MDHM was further purified by reversed-phase high-pressure liquid chromatography and eluted in one major and one minor peak of activity. Neither carbohydrates nor amino acids were found as constituents. MDHM had the following properties: it partitioned into the phenol phase upon phenol-water extraction and into the Triton phase after extraction with Triton X-114. MDHM was not inactivated by either phospholipase A2 or triglyceride lipases. However, mild periodate treatment led to a >95% loss of activity. Also, alkaline hydrolysis at 25°C completely abolished MDHM activity with a half-life of 2 min. MDHM activity was spread out over a wide molecular weight range upon sodium dodecyl sulfatepolyacrylamide gel electrophoresis of membranes, whereas after proteinase treatment MDHM activity migrated close to the front. These features of MDHM, taken together, speak in favor of an amphiphilic molecule with a lipid moiety carrying fatty acids in ester linkage and a polyol moiety of unknown character. MDHM was active in the nanogram-per-milliliter range, activating macrophages to release nitric oxide, interleukin-6, and tumor necrosis factor.

show abstract

“…Mycoplasmas have been implicated in rheumatic arthritis (2,8), fever (4), and AIDS (10, 14). It is not unlikely that MDHM-like substances play a role in some of these syndromes.…”

Section: Discussionmentioning

confidence: 99%

Purification and partial biochemical characterization of a Mycoplasma fermentans-derived substance that activates macrophages to release nitric oxide, tumor necrosis factor, and interleukin-6

Mühlradt

Frisch

1994

Infect Immun

View full text Add to dashboard Cite

show abstract

“…(5,12,[35][36][37].Immunoblotting patterns of patient synovial fluids on Triton X-114 extracts of Mycoplasma fernenfans (A) and Mycoplasma horninis (B). Arrows mark the size (in kd) of known membrane proteins (indicated by single asterisks), which were stained with a combination of corresponding monoclonal antibodies.…”

mentioning

confidence: 99%

Mycoplasma infection and rheumatoid arthritis: Analysis of their relationship using immunoblotting and an ultrasensitive polymerase chain reaction detection method

Hoffman¹,

O’Sullivan²,

Schäfermeyer³

et al. 1997

Arthritis & Rheumatism

View full text Add to dashboard Cite

Objective.To examine the relationship between infection with Mycoplasma and the development of rheumatoid arthritis (RA) and juvenile rheumatoid arthritis ( J U ) . Methods.Immunoblotting of patient synovial fluid and sera on detergent-phase membrane protein extracts of various Mycoplasma species was carried out to learn whether patients exhibited serologic evidence of previous exposure to mycoplasmas. Moreover, an ultrasensitive polymerase chain reaction (PCR) method was developed for assessing whether Mycoplasma DNA could be detected in synovial fluid from patients and controls.Results. Immunoblotting provided serologic evidence of previous Mycoplasma exposure in patients and controls. The genus-specific PCR detected known human Mycoplasma species and could reliably detect <5 copies of Mycoplasma hominis, Mycoplasma fermentans, or a molecular mimic control in synovial fluid. Repeat testing revealed no evidence of Mycoplasma DNA in patient synovial samples.Conclusion. This study provided serologic evidence suggesting that, while previous exposure to Mycoplasma was common, there was no detectable persistence of Mycoplasma DNA in the synovial fluid or tissue of patients with RA or JRA.

show abstract

“…'21' Like every superantigen MAS has a specificity for distinct VjSsubfamilies of the T cell receptor (TCR). To date, we know that the \ß 3.1, 11.1, 12.1, 13.1, and 19.1 in humans and V/3 5 IL-1, IL-2, IL-4, IL-6, tumor necrosis factorcu (TNF-a) and interferon-y (IFN-y) in human PBMC '30-31' and TNF-a, and IL-6 in murine cells. '10,31,32' The induction of these cytokines was also shown for other superantigens.…”

Section: Introductionmentioning

confidence: 99%

Induction of a Proinflammatory Cytokine Network byMycoplasma arthritidis-Derived Superantigen (MAS)

Rink

Nicklas²,

Luhm³

et al. 1996

Journal of Interferon & Cytokine Research

View full text Add to dashboard Cite

Mycoplasma arthritidis is an arthritogenic organism for rodents, producing a superantigen (MAS). It has been postulated that mycoplasmas or superantigens thereof might play a role in human rheumatoid arthritis. Since M. arthritidis fulfills both, the present study was performed to investigate MAS-specific cytokine induction. Human or murine leukocytes were stimulated with MAS, staphylococcal enterotoxin E (SEE), or lipopolysaccharide (LPS). Cytokines were measured by ELISA, Bioassay, and RT-PCR. The response to MAS in humans was individually restricted, in contrast to the response to SEE or LPS. Furthermore, MAS showed the same capacity for inducing proinflammatory cytokines as interleukin (IL)-1 IL-6, and IL-8 as SEE and LPS. However, MAS showed a significantly decreased capacity to induce the anti-inflammatory cytokine IL-10 and IL-1RA. In mice, the reactivity to MAS was strictly MHC-II restricted, in contrast to that of SEE or LPS. The individual response to MAS in humans might be explained by the difference of the HLA-DR haplotype because H-2-differing mouse strains showed the same discrepancies. MAS induced an overproduction of proinflammatory cytokines, when its ability to induce proinflammatory and anti-inflammatory cytokines was compared with those of SEE and LPS. The individual response may explain an MHC linkage, and the failure to induce anti-inflammatory cytokines may be the reason for a chronic disease in contrast to acute inflammation.

show abstract

Mycoplasmas and arthritis.

Cited by 23 publications

References 38 publications

Purification and partial biochemical characterization of a Mycoplasma fermentans-derived substance that activates macrophages to release nitric oxide, tumor necrosis factor, and interleukin-6

Purification and partial biochemical characterization of a Mycoplasma fermentans-derived substance that activates macrophages to release nitric oxide, tumor necrosis factor, and interleukin-6

Mycoplasma infection and rheumatoid arthritis: Analysis of their relationship using immunoblotting and an ultrasensitive polymerase chain reaction detection method

Induction of a Proinflammatory Cytokine Network byMycoplasma arthritidis-Derived Superantigen (MAS)

Contact Info

Product

Resources

About