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Biology of Reproduction 61, 1309-1316 (1999)
© 1999 Society for the Study of Reproduction, Inc.


Articles

Collagenase and Gelatinase Messenger Ribonucleic Acid Expression and Activity During Follicular Development in the Rat Ovary1

Robert G. III Cooke3,a, Warren B. Nothnicka, Carolyn Komara, Patrick Burnsb, and Thomas E. Curry Jr2,a

a Department of Obstetrics and Gynecology and b the Department of Animal Science, University of Kentucky, Lexington, Kentucky 40536-0293

Metalloproteinases are members of a family of proteinases that remodel the extracellular matrix throughout the body. To test the hypothesis that metalloproteinases are regulated by gonadotropin-induced changes during follicular growth, rats were injected with eCG (20 IU, s.c.), and ovaries and serum were collected at the time of eCG administration (0 h) and at 6, 12, 24, 36, or 48 h later for analysis of metalloproteinase mRNA expression, metalloproteinase activity, and steroidogenesis. Serum estradiol levels increased from 18.9 pg/ml at 0 h to 503.8 pg/ml at 48 h. Analysis of mRNA expression was performed for collagenase-3, 72-kDa gelatinase, and 92-kDa gelatinase (n = 3–4). For collagenase-3, eCG stimulated a 32-fold increase in collagenase-3 mRNA at 48 h after eCG injection as compared to that in ovaries collected at the time of eCG administration (i.e., 0-h control). The mRNA levels for 72-kDa gelatinase were 2.8-fold compared to 0 h at 36 h after eCG treatment and returned to control levels by 48 h after gonadotropin treatment. Levels of the 92-kDa mRNA expression peaked at 24 h (4.2-fold compared to 0 h) and returned to control levels by 36 h. Gel zymography revealed 3 gelatinolytic bands corresponding to the gelatinases of approximately 72 kDa, 92 kDa, and 105 kDa. Analysis of metalloproteinase activity as the degradation of collagen or gelatin per ovary showed an increase in gelatinolytic and collagenolytic activity between 12 and 48 h after eCG treatment. In summary, these findings demonstrate that the gonadotropin induction of folliculogenesis results in changes in the metalloproteinases that may be responsible for extracellular matrix remodeling associated with follicular growth.

1 This work was supported by NIH HD23195.

2 Correspondence: Thomas E. Curry, Jr., Department of Obstetrics and Gynecology, University of Kentucky Medical Center, 800 Rose Street, Lexington, KY 40536-0293. FAX: 606 323 1931; tecurry{at}pop.uky.edu

3 Current address: Robert Cooke, Eastover OB-GYN Associates, 1822 Brunswick Ave., Charlotte, NC 27208.




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