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and IL-1 Via Enhancement of the Heat Shock Element Binding Activity of Heat Shock Transcription Factor 1
Departments of
* Internal Medicine (Section 4) and
Clinical Diagnosis Medicine, Sapporo Medical University School of Medicine, Sapporo, Japan; and
Department of Internal Medicine, Kiyota Hospital, Sapporo, Japan
With most immunological reactions, tissue fibrosis, collagen
overproduction caused by immune cytokines, is inevitably associated.
Among the various immune cytokines, heat shock protein 47 (HSP47) is a
procollagen-specific molecular chaperon and is essential for secretion
of procollagen from cells. Induction of HSP47 by TGF-
has been
previously reported in rat skeletal myoblasts and mouse osteoblasts,
but not in human diploid fibroblasts. As for IL-1, its effect on
HSP47 has not been elucidated. In the present study, using human
embryonic lung fibroblast cells, we first disclosed that both TGF-
and IL-1 induced HSP47 synthesis. We then revealed that the binding
of the heat shock element (HSE) by heat shock transcription factor 1
(HSF1) was enhanced by both cytokines. We further demonstrated that
trimer formation of HSF1, which is essential for its binding to HSE,
was induced by these cytokines. The enhancement of HSP47 synthesis and
their trimer formation of HSF1 were augmented by using a combination of
both cytokines. Collectively, TGF- and IL-1 were found to induce
trimer formation of HSF1 which in turn bound to HSE of HSP47, resulting
in the enhancement of HSP47 expression. Thus, HSP47 could well be a
good candidate for molecular targeting in controlling tissue fibrosis,
given that both principal fibrinogenetic cytokines (TGF-, IL-1)
are commonly involved in its induction through HSF1
trimerization.
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