The participation of collagenolytic activities in the ovulatory process had been recently studied in experimental animals, though their existence in the human ovary remains obscure. In a previous report, we demonstrated the collagenolytic activity by using synthetic substrates N-carbobenzoxy-Gly-Pro-Gly-Gly-Pro-Ala and the cathepsin B1 activity in human ovarian follicles. To investigate the activity for degradation of native collagen in the human ovary, we used 14C-labeled collagen prepared from young rat skin in the present study. Collagenolytic activity for synthetic substrate DNP-Pro-Gln-Gly-Ile-Ala-Gly-Gln-D-Arg OH, supposed to be specific for vertebrate collagenase, was also measured. Our results clearly demonstrated that vertebrate collagenase activity exists; this collagenolytic activity was measured by using DNP-peptide in the human ovarian follicles. The correlation coefficient between both enzymatic activities was 0.56. The DNP-peptide-degrading activity seemed to partly represent the collagenolytic activity from vertebrate collagenase. It was concluded that vertebrate collagenase, besides collagenolytic activities, did exist in the human ovary and that ovaries seemed to be involved in the degradation of collagen fibers in the follicular apex at the time of ovulation.
|Number of pages||7|
|Journal||Acta Obstetrica et Gynaecologica Japonica|
|Publication status||Published - 1980 Dec 1|
ASJC Scopus subject areas
- Obstetrics and Gynaecology