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Bautz, Ekkehard K. F. [Hrsg.]; Heidelberger Akademie der Wissenschaften / Mathematisch-Naturwissenschaftliche Klasse [VerfasserIn] [Hrsg.]
Sitzungsberichte der Heidelberger Akademie der Wissenschaften, Mathematisch-Naturwissenschaftliche Klasse (1989, 4. Abhandlung): Molecular and cell biology of autoantibodies and autoimmunity: abstracts, 1. international workshop, July 27 - 29, 1989, Heidelberg — Berlin, Heidelberg [u.a.]: Springer, 1989

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https://doi.org/10.11588/diglit.48120#0055
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Abstracts

37

In the following study “hsp 70 class” proteins were isolated from Ht-1080 cells
by a modification of the method reported by Welch et al. [2]. The heat “induci-
ble” hsp 72 kDa protein as well as the “constitutive” hsp 73 kDa protein were used
as antigen source in immunoblotting experiments. In some experiments a protein
of 75 kDa, copurifying with the hsp 70 group proteins and known as non induci-
ble protein with great sequence homology to the hsp 70 s [2] was included as an-
tigen source. Sera obtained from SLE patients were analyzed for antibodies
against the isolated heat shock proteins. The antibodies of some sera showed reac-
tivity towards the proteins with molecular weight of 72000 and 73000. The 75000
copurifying heat shock protein was also recognized by some sera. However, sera
from normal subjects, tested for their reaction to a hsp 70 protein extract showed
surprisingly similar reactivity to the respective proteins as sera from SLE patients.
No significant difference was noted between the two groups of individuals tested.
In the study herein, we demonstrate that autoantibodies, found in sera from
SLE patients as well as in healthy subjects, recognize the “hsp 70 class” proteins.
These findings indicate the possibility that hsp 70 s can serve as in vivo im-
munogens, capable of inducing a spontaneous expression of autoantibodies.
References
1. Deguchi, I.Y. (1987): Biochem. Biophys. Res. Commun. 148, 3, 1063
2. Welch, W.J. (1985): Mol. Cell. Biol. 5, 6, 1229

Cross-Reactive Rheumatoid Factor in Rheumatoid Arthritis with
Extra-Articular Disease
M. Kinoshita, S. Aotsuka, and R. Yokohari
Division of Immunology, Clinical Research Institute, National Medical Center, Tokyo,
Japan
Rheumatoid factors (RF) have been shown to have considerable heterogeneity
and bind not only with IgG but also with a variety of substances, such as nuclear
histone, nitrophenyl groups or single-stranded DNA (ssDNA).
In the present study, we investigated the appearance of IgM, RF cross-reactive
with ssDNA in sera from patients with rheumatoid arthritis (RA), Sjogren’s
syndrome, systemic lupus erythematosus and progressive systemic sclerosis.
 
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