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Kleinau S, Söderström K, Kiessling R, et al. A monoclonal antibody to the mycobacterial 65 kDa heat shock protein (ML 30) binds to cells in normal and arthritic joints of rats. Scand J Immunol. 1991;33(2):195-202doi: 10.1111/j.1365-3083.1991.tb03749.x.
Kleinau, S., Söderström, K., Kiessling, R., & Klareskog, L. (1991). A monoclonal antibody to the mycobacterial 65 kDa heat shock protein (ML 30) binds to cells in normal and arthritic joints of rats. Scandinavian journal of immunology, 33(2), 195-202. https://doi.org/10.1111/j.1365-3083.1991.tb03749.x
Kleinau, S, et al. "A monoclonal antibody to the mycobacterial 65 kDa heat shock protein (ML 30) binds to cells in normal and arthritic joints of rats." Scandinavian journal of immunology vol. 33,2 (1991): 195-202. doi: https://doi.org/10.1111/j.1365-3083.1991.tb03749.x
Kleinau S, Söderström K, Kiessling R, Klareskog L. A monoclonal antibody to the mycobacterial 65 kDa heat shock protein (ML 30) binds to cells in normal and arthritic joints of rats. Scand J Immunol. 1991 Feb;33(2):195-202. doi: 10.1111/j.1365-3083.1991.tb03749.x. PMID: 2017657.
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Scand J Immunol. 1991 Feb;33(2):195-202. doi: 10.1111/j.1365-3083.1991.tb03749.x.

A monoclonal antibody to the mycobacterial 65 kDa heat shock protein (ML 30) binds to cells in normal and arthritic joints of rats.

Scandinavian journal of immunology

S Kleinau, K Söderström, R Kiessling, L Klareskog

Affiliations

  1. Department of Medical and Physiological Chemistry, Uppsala University, Sweden.

PMID: 2017657 DOI: 10.1111/j.1365-3083.1991.tb03749.x

Abstract

A monoclonal antibody reactive with the mycobacterial 65 kDa heat shock protein (ML 30) was investigated for reactivity with biopsies from normal rat joints and with inflamed joints due to adjuvant arthritis (AA) or collagen induced arthritis (CIA). Immunohistochemical stainings with the anti-hsp 65 antibody on paraffin sections from normal rat joints revealed a weak but exclusive staining of cells within the synovial lining. Also normal chondrocytes and bone marrow cells showed occasional staining. In biopsies from inflamed joints obtained from rats suffering from AA or CIA, an intense staining with ML 30 was seen within the cartilage-pannus junction as well as sites of bone erosion. An increased staining, compared with the normal, was also seen in chondrocytes of the eroded cartilage and in some bone marrow cells. No staining with ML 30 was seen in biopsies from inflammatory lesions due to delayed type hypersensitivity reactions in the skin of rats. Reactivity of ML 30 was also seen in a Western blot assay performed on lysates from inflamed synovia from rats with CIA, preferentially with a component slightly below 60 kDa in molecular weight. The demonstration of epitopes cross-reactive with hsp 65 of mycobacteria in normal and, in higher quantity, in arthritic rat joints, suggests, together with our preliminary biochemical findings, that a recently identified mammalian counterpart to bacterial hsp 65 is both preferentially expressed in normal joints and subject to increased expression in arthritis of different aetiologies.

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