Effect of various proteinase inhibitors on ovulation of explanted hamster ovaries

Ichikawa, S.; Morioka, Hiroshi; Ohta, Mitsuaki; Oda, Keiji; Murao, Sawao

doi:10.1530/jrf.0.0680407

Cited by 29 publications

(12 citation statements)

References 18 publications

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“…Many studies have demonstrated that MMPs play important roles in folliculogenesis, including development, luteinization, and luteolysis. Injection of synthetic metalloproteinase inhibitors has blocked ovulation in hamsters and rats [18,19]. Others have shown that MMP-1 protein and its enzymatic activity of ovine and rabbit ovaries were concentrated at the site of future rupture in the capillary lumina at the apex of the follicle [20,21].…”

Section: Introductionmentioning

confidence: 99%

Bovine Follicular Fluid and Serum Share a Unique Isoform of Matrix Metalloproteinase-2 That Is Degraded by the Oviductal Fluid1

Kim

Hong

Kim

et al. 2001

Biology of Reproduction

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Whereas the mammalian fertilization environment consists of possible products of the mutual interaction between oviductal and follicular fluids in addition to both fluid components, little is known regarding the interaction. In the present study, we have demonstrated that a mutual interaction occurs, resulting in the biochemical changes of follicular fluid components. Gelatin zymographic analyses of bovine follicular fluid (bFF) showed consistently a distinct, gelatinolytic activity having a molecular weight of 110 kDa (GA110) in addition to other gelatinases, whereas bovine oviductal fluid (bOF) showed a lack of GA110. Surprisingly, when bFF was mixed with bOF before zymography, the GA110 of bFF mostly disappeared at a 1:1 (v/v) mixture, completely disappeared at a 1:10 mixture, as fast as within 30 min after mixing. Other bFF gelatinase activities were not affected by bOF at 1:1 or 10:1 mixtures. Addition of EDTA or phenanthroline, but not of phenylmethylsulfonyl fluoride or trypsin inhibitor, to the mixture greatly increased the gelatinolytic activity of bFF GA110. The increased activity of bFF GA110 by EDTA was again abolished by subsequent bOF treatment. Addition of aminophenylmercuric acetate to the EDTA-treated bFF also abolished GA110; however, this was accompanied by the disappearance of other gelatinases, except the 62-kDa gelatinase, the activity of which increased as the treatment continued up to 24 h. Addition of EDTA or phenanthroline to the gelatin gel incubation buffer after electrophoresis abolished almost all gelatinases of bFF, except those of 88-84 kDa, demonstrating that they were indeed gelatinases or isoforms. Bovine serum and fetal bovine serum also showed the presence of GA110, the activity of which was increased by EDTA. However, ovarian granulosa cell homogenate did not exhibit GA110. Immunoblot experiments using antibodies against matrix metalloproteinase (MMP)-2 and MMP-9 demonstrated that bFF GA110 was an isoform of MMP-2, and that the 62-kDa form was an active form of MMP-2. Disappearance of immunoreactive GA110 of bFF and serum by bOF was also observed. Based on these observations, we conclude that bFF and bovine serum share a unique isoform of MMP-2, and that bOF can specifically degrade the isoform, suggesting that a mutual interaction between bFF and bOF could occur at the time of ovulation.

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Section: Introductionmentioning

confidence: 99%

Bovine Follicular Fluid and Serum Share a Unique Isoform of Matrix Metalloproteinase-2 That Is Degraded by the Oviductal Fluid1

Kim

Hong

Kim

et al. 2001

Biology of Reproduction

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“…7 describes the effect of benzamidine; similar dose response.was obtained with €-amino caproic acid). Similarly, several inhibitors of serine proteases inhibited in vitro ovulation of hamster ovaries (Ichikawa et al, 1983). Even though follicular rupture occurs 9-12 h after hCG stimulation, administration of inhibitors of serine proteases prior to 1.5 h after hCG blocked ovulation in rats (> 65%) but had limited effect « 30%) after 3 h. This result implies that the activity of serine proteases is required only during the first 3 h after hCG stimulation.…”

Section: -------------------------------------- Cmentioning

confidence: 88%

Mechanisms Involved in Follicular Rupture in the Rat

Reich

Tsafriri

1984

Hormonal Control of the Hypothalamo-Pituitary-Gonadal Axis

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“…In mammals, ICHIKAWA et al 21) suggested that serine-proteinase(s) participate in ovulation, since specific inhibitors to these enzymes inhibit ovulation. BEERS22) and BEERS et al 23) reported that plasmin, one of the serine-proteinases, is capable of inducing ovulation since the plasminogen activator activity in the ovarian follicle usually increases with the approach of ovulation or in response to LH or cyclic AMP.…”

Section: Discussionmentioning

confidence: 99%

Role of Proteolytic Enzymes in the Ovulatory Process of the Domestic Fowl, (Gallus domesticus)

Yoshimura¹,

Katoh²

1985

Nihon Chikusan Gakkaiho

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The role played by proteinase(s) in ovulation in the hen was examined using an in vitro ovulation system and an enzyme assay of the follicle wall. Thiol-proteinase inhibitor, antipain, blocked or delayed ovulation, and its activator, cysteine, promoted the rupture of the follicle. The activity of neutral thiol-proteinase in the follicle wall increased significantly 0.5h before ovulation. Serine-proteinase inhibitors such as soybean trypsin inhibitor and leupeptin, and collagenase inhibitors such as EDTA and ZnCl2 did not block ovulation.These results suggest that neutral thiol-proteinase may be involved in the rupture of the follicle at the time of ovulation in the hen.Jpn. J. Zooteck. Sci., 56 (5): [407][408][409][410][411][412][413] 1985 Proteinase (s) may be involved in the process of ovulation in hens, since the rupture of the follicle can be induced by the administration of exogenous proteinases1,2), and the stigma tissue near the time of ovulation appears extremely loose3-5). NAKAMURA and NAKAJO6) demonstrated that the activity of alkaline proteinase in the follicle wall of the Japanese quail decreased at ovulation. TOJO et al.7) observed that the activity of neutral proteinase in the hen's follicle wall increased immediately after ovulation.However, these results did not provide significant information to define accurately the role of proteinase in the rupture of the hen's follicle. The present study was thus undertaken to clarify this role. Materials and MethodsWhite Leghorn hens with regular sequence more than four eggs were used in the present study.Experiment I. Effect of proteinase inhibitors or activators on in vitro ovulation Incubation of follicles. The largest follicle was removed from the hen 0.5 h before the expected time of ovulation (immediately after ovipositione8)), and dipped into the first exposure to the test solution and ovulation was calculated. If the rupture did

show abstract

Effect of various proteinase inhibitors on ovulation of explanted hamster ovaries

Cited by 29 publications

References 18 publications

Bovine Follicular Fluid and Serum Share a Unique Isoform of Matrix Metalloproteinase-2 That Is Degraded by the Oviductal Fluid1

Bovine Follicular Fluid and Serum Share a Unique Isoform of Matrix Metalloproteinase-2 That Is Degraded by the Oviductal Fluid1

Mechanisms Involved in Follicular Rupture in the Rat

Role of Proteolytic Enzymes in the Ovulatory Process of the Domestic Fowl, (Gallus domesticus)

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