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Human recombinant interleukin‐1α‐mediated stimulation of procollagenase production and suppression of biosynthesis of tissue inhibitor of metalloproteinases in rabbit uterine cervical fibroblasts
Author(s) -
Ito Akira,
Goshowaki Hideko,
Sato Takashi,
Mori Yo,
Yamashita Kyoko,
Hayakawa Taro,
Nagase Hideaki
Publication year - 1988
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(88)80109-1
Subject(s) - collagenase , matrix metalloproteinase , stimulation , endocrinology , recombinant dna , medicine , interstitial collagenase , tissue inhibitor of metalloproteinase , cervix , ovariectomized rat , interleukin , chemistry , uterine cervix , cytokine , biology , enzyme , hormone , biochemistry , cancer , carcinoma , gene
Influence of human recombinant interleukin‐1 (hrIL‐1) on collagen metabolism was investigated with rabbit uterine cervical fibroblasts. Enzyme‐linked immunosorbent assays for collagenase and tissue inhibitor of metalloproteinases (TIMP) indicated that hrIL‐1 participates in both stimulation of procollagenase production and suppression of TIMP synthesis by uterine cervical cells. IL‐1 did not modulate collagen synthesis. In addition, the sensitivity to IL‐1 of uterine cervix from ovariectomized rabbits was augmented by estradiol‐17β treatment. Thus it is proposed that IL‐1 accelerates collagenolysis in the cervical tissue and its effect on uterine cervix is hormonally regulated.