Interleukin-1β triggers matrix metalloprotease-3 expression through p65/RelA activation in melanoma cells

Melanoma shows highly aggressive behavior (i.e., local invasion and metastasis). Matrix metalloprotease-3 (MMP-3), a zinc-dependent endopeptidase, degrades several extracellular substrates and contributes to local invasion by creating a microenvironment suitable for tumor development. Here, we repor...

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Veröffentlicht in:PloS one 2022-11, Vol.17 (11)
Hauptverfasser: Junichi Nunomura, Rei Nakano, Atsuto Naruke, Yoko Suwabe, Masumi Nakano, Naoya Yachiku, Manami Kuji, Mana Sugimura, Shinichi Namba, Taku Kitanaka, Nanako Kitanaka, Hiroshi Sugiya, Tomohiro Nakayama
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Sprache:eng
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Zusammenfassung:Melanoma shows highly aggressive behavior (i.e., local invasion and metastasis). Matrix metalloprotease-3 (MMP-3), a zinc-dependent endopeptidase, degrades several extracellular substrates and contributes to local invasion by creating a microenvironment suitable for tumor development. Here, we report that interleukin-1β (IL-1β) triggers the MMP-3 expression in canine melanoma cells. The activity of MMP-3 in the culture supernatant was increased in IL-1β-treated melanoma cells. IL-1β time- and dose-dependently provoked the mRNA expression of MMP-3. IL-1β induced the migration of melanoma cells; however, this migration was attenuated by UK356618, an MMP-3 inhibitor. When the cells were treated with the nuclear factor-κB (NF-κB) inhibitor TPCA-1, the inhibition of MMP-3 expression was observed. In IL-1β-treated cells, the phosphorylation both of p65/RelA and p105 was detected, indicating NF-κB pathway activation. In p65/RelA-depleted melanoma cells, IL-1β-mediated mRNA expression of MMP-3 was inhibited, whereas this reduction was not observed in p105-depleted cells. These findings suggest that MMP-3 expression in melanoma cells is regulated through IL-1β-mediated p65/RelA activation, which is involved in melanoma cell migration.
ISSN:1932-6203
DOI:10.1371/journal.pone.0278220