scholarly journals Autoantibodies to the constitutive 73-kD member of the hsp70 family of heat shock proteins in systemic lupus erythematosus.

1988 ◽  
Vol 168 (4) ◽  
pp. 1475-1480 ◽  
Author(s):  
S Minota ◽  
B Cameron ◽  
W J Welch ◽  
J B Winfield
Keyword(s):  
Systemic Lupus Erythematosus ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Lupus Erythematosus ◽  
Solid Phase ◽  
Systemic Lupus ◽  
Hsp70 Family ◽  
Hsp70 Protein ◽  
Sds Page ◽  
Shock Proteins

Serum from patients with systemic lupus erythematosus (SLE) frequently contain IgM and IgG autoantibodies to the constitutively expressed 73-kD/pI 5.5 member of the hsp70 family of heat shock proteins, as determined by one-dimensional (SDS-PAGE) and two-dimensional (IEF/SDS-PAGE) immunoblotting, and by solid-phase SLE Ig immunoprecipitation experiments using hsp70 protein-specific mAbs as probes. Autoantibodies to hsp70 also were detected in a minority of sera from patients with other rheumatic or viral diseases, but not in normal sera. These data may provide additional insight into etiologic and pathophysiologic mechanisms in this and related autoimmune disorders.

Review: Heat Shock Proteins and Systemic Lupus Erythematosus

Lupus ◽  
1991 ◽  
Vol 1 (1) ◽  
pp. 3-8 ◽  
Author(s):  
V. Dhillon ◽  
D. Latchman ◽  
D. Isenberg
Keyword(s):  
Systemic Lupus Erythematosus ◽  
Heat Shock ◽  
Heat Shock Proteins ◽  
Lupus Erythematosus ◽  
Systemic Lupus ◽  
Shock Proteins

scholarly journals Role of Hsp90 in Systemic Lupus Erythematosus and Its Clinical Relevance

2012 ◽  
Vol 2012 ◽  
pp. 1-6 ◽  
Author(s):  
Hem D. Shukla ◽  
Paula M. Pitha
Keyword(s):  
Systemic Lupus Erythematosus ◽  
Heat Shock ◽  
Lupus Erythematosus ◽  
Clinical Manifestations ◽  
Heat Shock Protein 90 ◽  
Type I ◽  
Systemic Lupus ◽  
Conformational Regulation ◽  
Shock Proteins ◽  
Hsp 90

Heat shock proteins (HSP) are a family of ubiquitous and phylogenically highly conserved proteins which play an essential role as molecular chaperones in protein folding and transport. Heat Shock Protein 90 (Hsp90) is not mandatory for the biogenesis of most proteins, rather it participate in structural maturation and conformational regulation of a number of signaling molecules and transcription factors. Hsp90 has been shown to play an important role in antigen presentation, activation of lymphocytes, macrophages, maturation of dendritic cells, and in the enhanceosome mediated induction of inflammation. Systemic lupus erythematosus (SLE) is a chronic autoimmune inflammatory disease with complex immunological and clinical manifestations. Dysregulated expression of Type I interferonα, activation of B cells and production of autoantibodies are hallmarks of SLE. The enhanced levels of Hsp90 were detected in the serum of SLE patients. The elevated level of Hsp90 in SLE has also been correlated with increased levels of IL-6 and presence of autoantibodies to Hsp90. This suggests that Hsp90 may contribute to the inflammation and disease progression and that targeting of Hsp 90 expression may be a potential treatment of SLE. The pharmacologic inhibition of Hsp90 was successfully applied in mouse models of autoimmune encephalomyelitis and SLE—like autoimmune diseases. Thus targeting Hsp90 may be an effective treatment for SLE, especially if combined with other targeted therapeutic approaches.

Enzyme-linked immunosorbent assay for detection of antibodies to extractable nuclear antigens in systemic lupus erythematosus, with nylon as solid phase.

1983 ◽  
Vol 29 (5) ◽  
pp. 823-827 ◽  
Author(s):  
M Ishaq ◽  
R Ali
Keyword(s):  
Systemic Lupus Erythematosus ◽  
Immunosorbent Assay ◽  
Lupus Erythematosus ◽  
Solid Phase ◽  
Enzyme Linked Immunosorbent Assay ◽  
Prolonged Storage ◽  
Antibody Activity ◽  
Systemic Lupus ◽  
Nuclear Antigens ◽  
As Solid Phase

Abstract In this enzyme-linked immunosorbent assay (ELISA) for detection of antibodies against extractable nuclear antigens (ENA) in sera of patients with systemic lupus erythematosus (SLE), nylon is used as solid phase for antigen binding instead of the commonly used polystyrene surface. Optimal conditions for activation of the nylon beads, antigen coating, and other relevant factors have been investigated. We compared the incidence of anti-ENA antibodies in SLE, using chromogenic and fluorogenic enzyme substrates. Of SLE patients, 54% were positive for anti-ENA antibodies when chromogenic substrate was used as compared with 68% for fluorogenic substrate. Antibody activity against Sm and RNP antigens was distinguished on the basis of ribonuclease sensitivity of the RNP antigen. The method described offers advantages such as decreased background activity, increased surface area, facility for prolonged storage of antigen-coated solid phase, and miniaturization of the assay.

scholarly journals Heat shock protein 90 inhibition by 17-DMAG lessens disease in the MRL/lpr mouse model of systemic lupus erythematosus

2012 ◽  
Vol 9 (3) ◽  
pp. 255-266 ◽  
Author(s):  
Samuel K Shimp ◽  
Cristen B Chafin ◽  
Nicole L Regna ◽  
Sarah E Hammond ◽  
Molly A Read ◽  
...  
Keyword(s):  
Systemic Lupus Erythematosus ◽  
Heat Shock ◽  
Mouse Model ◽  
Heat Shock Protein ◽  
Lupus Erythematosus ◽  
Heat Shock Protein 90 ◽  
Systemic Lupus
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