Human recombinant interleukin‐1α‐mediated stimulation of procollagenase production and suppression of biosynthesis of tissue inhibitor of metalloproteinases in rabbit uterine cervical fibroblasts

FEBS Letters

Goshowaki, Hideko²  Mori, Yo²  Hayakawa, Taro³  Yamashita, Kyoko³  Sato, Takashi²  Nagase, Hideaki¹  Ito, Akira² 

[1] Department of Biochemistry, School of Medicine, University of Kansas Medical Center, Kansas City, KS 66103, USA;Department of Biochemistry, Tokyo College of Pharmacy, Horinouchi, Hachioji, Tokyo 192-03, Japan;Department of Biochemistry, School of Dentistry, Aichi-Gakuin University, Chikusa-ku, Nagoya 464, Japan

关键词: Recombinant interleukin-1α;    Procollagenase;    Tissue inhibitor of metalloproteinase;    Estradiol-17β;    (Rabbit uterine cervix);    hrIL-1;    human recombinant interleukin-1α;    FCS;    fetal calf serum;    MEM;    Eagle's minimum essential medium;    DMEM;    Dulbecco's modified Eagle's medium;    TIMP;    tissue inhibitor of metalloproteinases;    LAH;    lactalbumin hydrolysate;    ELISA;    enzyme-linked immunosorbent assay;   

DOI  :  10.1016/0014-5793(88)80109-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown