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Arthritis and rheumatism 1993-Jun

Stimulation of the secretion of latent cysteine proteinase activity by tumor necrosis factor alpha and interleukin-1.

Зөвхөн бүртгэлтэй хэрэглэгчид л нийтлэл орчуулах боломжтой
Нэвтрэх / Бүртгүүлэх
Холбоосыг санах ойд хадгалдаг
G Huet
R M Flipo
C Colin
A Janin
B Hemon
M Collyn-d'Hooghe
R Lafyatis
B Duquesnoy
P Degand

Түлхүүр үгс

Хураангуй

OBJECTIVE

Cultured synovial fibroblast-like cells from 3 patients with rheumatoid arthritis (RA) and 3 patients with osteoarthritis (OA) were evaluated for their potential to secrete cysteine proteinases spontaneously and after stimulation by tumor necrosis factor alpha (TNF alpha) or interleukin-1 (IL-1).

METHODS

Culture media and cell lysates were analyzed before and after high performance liquid chromatography (HPLC) using the enzymatic substrate, Z-Phe-Arg-AMC, and by immunoblotting with anti-cathepsin B antiserum. Immunolocalization of cathepsin B was studied on cell monolayers.

RESULTS

Latent cysteine proteinase activity was found to be secreted spontaneously by cultured synovial fibroblast-like cells. This activity was increased after treatment with either TNF alpha or IL-1. Stimulated protease activity was eluted by HPLC at a peak coincident with that of purified cathepsin B. By immunoblot, cell supernatants contained a 43-kd form of cathepsin B, while cell lysates contained a 30-kd form, consistent, respectively, with cathepsin B before and after cleavage of its propeptide. An intracellular increase in cathepsin B after treatment with TNF alpha was also seen with immunohistochemical studies.

CONCLUSIONS

TNF alpha (in the 6 cases studied) and IL-1 (in 4 cases) stimulated the secretion of a latent cysteine proteinase activity from synovial fibroblast-like cells, which appears to represent primarily cathepsin B.

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