scholarly journals Suppression of human cartilage proteoglycan synthesis by rheumatoid synovial fluid mononuclear cells activated with mycobacterial 60-kd heat-shock protein

1993 ◽  
Vol 36 (4) ◽  
pp. 514-518 ◽  
Author(s):  
B. Wilbrink ◽  
M. Holewijn ◽  
J. W. J. Bijlsma ◽  
J. L. A. M. Van Roy ◽  
W. Den Otter ◽  
...  
Keyword(s):  
Heat Shock ◽  
Synovial Fluid ◽  
Heat Shock Protein ◽  
Mononuclear Cells ◽  
Proteoglycan Synthesis ◽  
Human Cartilage ◽  
Rheumatoid Synovial Fluid ◽  
Cartilage Proteoglycan

scholarly journals Recognition of a mycobacteria-specific epitope in the 65-kD heat-shock protein by synovial fluid-derived T cell clones.

1990 ◽  
Vol 171 (3) ◽  
pp. 831-841 ◽  
Author(s):  
J S Gaston ◽  
P F Life ◽  
P J Jenner ◽  
M J Colston ◽  
P A Bacon
Keyword(s):  
Amino Acids ◽  
T Cell ◽  
Heat Shock ◽  
Synovial Fluid ◽  
Heat Shock Protein ◽  
Mononuclear Cells ◽  
Cell Clone ◽  
T Cell Clones ◽  
Cell Clones ◽  
T Cell Clone

Adjuvant arthritis in rats is induced by a T cell clone specific for amino acids 180-188 of the mycobacterial 65-kD heat-shock protein, and synovial T cell responses to this same Ag have been noted in human arthritis. We have isolated 65-kD Ag-specific T cell clones from synovial fluid mononuclear cells of a patient with acute arthritis, which, unlike the corresponding PBMC, showed a marked proliferative response to the 65-kD Ag. Using synthetic peptides corresponding to the whole sequence of the 65-kD Ag, all the clones were shown to recognize an epitope present in the first NH2-terminal peptide (amino acids 1-15), with no response to the adjacent peptide (amino acids 6-22) or to any other peptide. The complete dominance of this epitope in the response to the 65-kD Ag was shown by documenting responses to the peptide in PBMC obtained after recovery from the arthritis. This epitope, like that recognized by the rat arthritogenic T cell clone, is in a portion of the 65-kD sequence that is not conserved between bacteria and eukaryotes, so that in this case, joint inflammation could not be attributed to bacteria-induced T cell clones cross-reacting with the self 65-kD Ag.

Synovial fluid-derivedYersinia-reactive T cells responding to human 65-kDa heat-shock protein and heat-stressed antigen-presenting cells

1991 ◽  
Vol 21 (9) ◽  
pp. 2139-2143 ◽  
Author(s):  
Elisabeth Hermann ◽  
Ansgar W. Lohse ◽  
Ruurd Van Der Zee ◽  
Willem Van Eden ◽  
Werner J. Mayet ◽  
...  
Keyword(s):  
T Cells ◽  
Heat Shock ◽  
Synovial Fluid ◽  
Heat Shock Protein ◽  
Antigen Presenting Cells ◽  
Antigen Presenting

scholarly journals A 70-Kilodalton Recombinant Heat Shock Protein ofCandida albicans Is Highly Immunogenic and Enhances Systemic Murine Candidiasis

1998 ◽  
Vol 66 (5) ◽  
pp. 2154-2162 ◽  
Author(s):  
Carla Bromuro ◽  
Roberto La Valle ◽  
Silvia Sandini ◽  
Francesca Urbani ◽  
Clara M. Ausiello ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Protein ◽  
Mononuclear Cells ◽  
Cell Mediated Immunity ◽  
Healthy Human ◽  
Peripheral Blood Mononuclear ◽  
Necrosis Factor Alpha ◽  
Ifn Γ

ABSTRACT The 70-kDa recombinant Candida albicans heat shock protein (CaHsp70) and its 21-kDa C-terminal and 28-kDa N-terminal fragments (CaHsp70-Cter and CaHsp70-Nter, respectively) were studied for their immunogenicity, including proinflammatory cytokine induction in vitro and in vivo, and protection in a murine model of hematogenous candidiasis. The whole protein and its two fragments were strong inducers of both antibody (Ab; immunoglobulin G1 [IgG1] and IgG2b were the prevalent isotypes) and cell-mediated immunity (CMI) responses in mice. CaHsp70 preparations were also recognized as CMI targets by peripheral blood mononuclear cells of healthy human subjects. Inoculation of CaHsp70 preparations into immunized mice induced rapid production of interleukin-6 (IL-6) and tumor necrosis factor alpha, peaking at 2 to 5 h and declining within 24 h. CaHsp70 and CaHsp70-Cter also induced gamma interferon (IFN-γ), IL-12, and IL-10 but not IL-4 production by CD4+ lymphocytes cocultured with splenic accessory cells from nonimmunized mice. In particular, the production of IFN-γ was equal if not superior to that induced in the same cells by whole, heat-inactivated fungal cells or the mitogenic lectin concanavalin A. In immunized mice, however, IL-4 but not IL-12 was produced in addition to IFN-γ upon in vitro stimulation of CD4+ cells with CaHsp70 and CaHsp70-Cter. These animals showed a decreased median survival time compared to nonimmunized mice, and their mortality was strictly associated with organ invasion by fungal hyphae. Their enhanced susceptibility was attributable to the immunization state, as it did not occur in congenitally athymic nude mice, which were unable to raise either Ab or CMI responses to CaHsp70 preparations. Together, our data demonstrate the elevated immunogenicity of CaHsp70, with which, however, no protection against but rather some enhancement of Candida infection seemed to occur in the mouse model used.

Influence of rheumatoid synovial fluid and cells on proteoglycans in human cartilage explants. Modulation by piroxicam

1992 ◽  
Vol 11 (1) ◽  
pp. 86-91
Author(s):  
B. Wilbrink ◽  
J. Vernooy ◽  
W. Den Otter ◽  
J. L. A. M. Van Roy ◽  
J. Huber ◽  
...  
Keyword(s):  
Synovial Fluid ◽  
Cartilage Explants ◽  
Human Cartilage ◽  
Rheumatoid Synovial Fluid

SYNOVIAL FLUID T CELLS AND 65 kD HEAT-SHOCK PROTEIN

The Lancet ◽  
1988 ◽  
Vol 332 (8615) ◽  
pp. 856-857 ◽  
Author(s):  
J.S.H. Gaston ◽  
P.F. Life ◽  
L. Bailey ◽  
P.A. Bacon ◽  
I.L. McLean ◽  
...  
Keyword(s):  
T Cells ◽  
Heat Shock ◽  
Synovial Fluid ◽  
Heat Shock Protein

Heat shock protein 60 from Klebsiella pneumoniae protects mononuclear cells from apoptotic cell death induced by dexamethasone

2011 ◽  
Vol 51 (5) ◽  
pp. 352-359 ◽  
Author(s):  
Yolanda Ortega-Ortega ◽  
Ethel Awilda García-Latorre ◽  
Ruth Angélica Lezama ◽  
Julieta Luna-Herrera ◽  
Armando Vega-López ◽  
...  
Keyword(s):  
Cell Death ◽  
Heat Shock ◽  
Klebsiella Pneumoniae ◽  
Heat Shock Protein ◽  
Mononuclear Cells ◽  
Apoptotic Cell ◽  
Apoptotic Cell Death ◽  
Heat Shock Protein 60
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