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KMID : 0391319940040020209
Korean Journal of Biological Response Modifiers
1994 Volume.4 No. 2 p.209 ~ p.212
Processing and Release of Interleukin-1(IL-2) and their Pathophysiological Significance
Yoshiro Kobayashi
Abstract
While interleukin-1(IL-1) is lacking in a so-called signal peptide in its precursor, it is secreted from producing cells. The mechanisms for the processing and secretion of IL-1 have been enigmas. We have investigated those of IL-1 ¥áand found
the
following points; (1) Pre-IL-1 ¥á binds to acidic phospholipids in the inner side of the membrane in a calcium-dependent manner. (2) Calpain, a calcium-activated cysteine protease, cleaves pre-IL-1¥á into mature IL-1¥á. (3) The secretion of
IL-1¥á
appears to be coupled with processing. (4) Mature IL-1¥á makes acidic phospholipids permeable to macromolecules, thereby enabling itself to translocate through the cell membrane. We recently reported that synovial cells freshly isolated from
patients
with rheumatoid arthritis (RA) produced much pre-IL-1¥â and little mature IL-1¥â, but that the levels of IL-1¥â and IL-1¥â converting enzyme (ICE) were closely correlated. The latter finding suggests the involvement of ICE in RA.
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