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A Monoclonal Antibody to the Mycobacterial 65kDa Heat Shock Protein (ML 30) Binds to Cells in Normal and Arthritic Joints of Rats
Author(s) -
KLEINAU S.,
SÖDERSTRÖM K.,
KIESSLING R.,
KLARESKOG L.
Publication year - 1991
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1991.tb03749.x
Subject(s) - staining , pathology , arthritis , bone marrow , monoclonal antibody , immunohistochemistry , western blot , cartilage , antibody , heat shock protein , microbiology and biotechnology , chemistry , inflammation , synovial fluid , immunology , medicine , biology , osteoarthritis , anatomy , biochemistry , alternative medicine , gene
A monoclonal antibody reactive with the mycobacterial 65 kDa heal 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 arthrilis (CIA). Immunohistochemical stainings with the ant‐hsp 65 antibody on paralVm 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 oceasioniil staining. In biopsies from inflamed joints obtained from rats suffering from AA or CIA. an intense staining with ML 30 was seen with in the Ciirtilage‐pannus junction as well as sites of bone erosion. An increased staining, compared with the normal, was also seen in chondroeytes 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 hyperscnsitivity 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.