Different modulation of steroidogenesis and prostaglandin production in frog ovary in vitro by ACE and ANG II

The purpose of the present study was to identify angiotensin converting enzyme (ACE) in bovine ovarian follicular fluid and to relate the ACE activity to the phase of the oestrous cycle, pregnancy, and the follicular fluid concentrations of oestradiol and progesterone. The ACE activity was similar to that found in bovine serum and was completely inhibited by the specific ACE inhibitor captopril. The 50% inhibitory concentration (IC50) was 1.4 x 10(-8) mol/l (range 0.8 x 10(-8) to 5.0 x 10(-8) mol/l; n=6), which is similar to that found in bovine and human serum. The ACE activity did not differ in the pre-ovulatory and luteal phase, pregnancy or cystic follicles. It correlated with the follicular fluid concentration of progesterone in cycling cows (rho=0.476; p < 0.005; n=36), but did not correlate with the diameter of the follicles, the follicular fluid concentration of oestradiol or the ratio between the oestradiol and progesterone concentrations. The demonstration of ACE in bovine ovarian follicular fluid provides further evidence for the presence of a local renin-angiotensin system in the bovine ovary.

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“…1990; Howard and Husain 1992), rabbit (Brentjens et al. 1986) and frog (Bramucci et al. 1997) ovary.…”

Section: Introductionmentioning

confidence: 99%

Angiotensin Converting Enzyme in Bovine Ovarian Follicular Fluid and its Relationship with Oestradiol and Progesterone

Nielsen¹,

Schauser²,

Svenstrup

et al. 2002

Reprod Domestic Animals

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“…ANG III, ANG-(1-7), and ANG- (3)(4)(5)(6)(7)(8) have some overlapping actions with ANG II because of partial occupancy of ANG II receptors, but importantly, ANG-(1-7) and ANG- (3)(4)(5)(6)(7)(8) have their own receptors that mediate opposing actions to ANG II (27,47). In the present study, HPLC analysis of luteal cell incubations showed peaks that eluted with the same retention times as ANG II, ANG III, and ANG-(1-7), and their relative quantities were ANG II Ն ANG-(1-7) Ͼ ANG III.…”

Section: Discussionmentioning

confidence: 99%

“…The substrate angiotensinogen is hydrolyzed by renin, releasing the decapeptide ANG I, which in turn is substrate for angiotensin-converting enzyme (ACE). ACE hydrolysis of ANG I results in the formation of the octapeptide ANG II, considered the major biologically active peptide of the cascade, and its proteolysis produces ANG III [ANG- (2)(3)(4)(5)(6)(7)(8)]. Historically, ANG II was considered an adrenal hormone restricted to renal function, but evidence that ANG II is produced by other tissues, including the ovaries, began to emerge in the 1980s.…”

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confidence: 99%

“…13,20). ACE hydrolysis of ANG I results in the formation of ANG II that is further proteolytically degraded by aminopeptidase A to ANG III [ANG- (2)(3)(4)(5)(6)(7)(8)] or by aminopeptidase D to ANG IV [ANG- (3)(4)(5)(6)(7)(8)] and other fragments (57). An additional pathway for lysis of ANG I is via prolyl endopeptidase (PEP; EC 3.4.21.26) or neutral endopeptidase (NEP; EC 3.4.24.11), resulting in the formation of ANG-(1-7).…”

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confidence: 99%

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Localized accumulation of angiotensin II and production of angiotensin-(1–7) in rat luteal cells and effects on steroidogenesis

Pepperell¹,

Németh²,

Yamada³

et al. 2006

American Journal of Physiology-Endocrinology and Metabolism

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These studies aim to investigate subcellular distribution of angiotensin II (ANG II) in rat luteal cells, identify other bioactive angiotensin peptides, and investigate a role for angiotensin peptides in luteal steroidogenesis. Confocal microscopy showed ANG II distributed within the cytoplasm and nuclei of luteal cells. HPLC analysis showed peaks that eluted with the same retention times as ANG-(1-7), ANG II, and ANG III. Their relative concentrations were ANG II >or= ANG-(1-7) > ANG III, and accumulation was modulated by quinapril, an inhibitor of angiotensin-converting enzyme (ACE), Z-proprolinal (ZPP), an inhibitor of prolyl endopeptidase (PEP), and parachloromercurylsulfonic acid (PCMS), an inhibitor of sulfhydryl protease. Phenylmethylsulfonyl fluoride (PMSF), a serine protease inhibitor, did not affect peptide accumulation. Quinapril, ZPP, PCMS, and PMSF, as well as losartan and PD-123319, the angiotensin receptor type 1 (AT1) and type 2 (AT2) receptor antagonists, were used in progesterone production studies. ZPP significantly reduced luteinizing hormone (LH)-dependent progesterone production (P < 0.05). Quinapril plus ZPP had a greater inhibitory effect on LH-stimulated progesterone than either inhibitor alone, but this was not reversed by exogenous ANG II or ANG-(1-7). Both PCMS and PMSF acutely blocked LH-stimulated progesterone, and PCMS blocked LH-sensitive cAMP accumulation. Losartan inhibited progesterone production in permeabilized but not intact luteal cells and was reversed by ANG II. PD-123319 had no significant effect on luteal progesterone production in either intact or permeabilized cells. These data suggest that steroidogenesis may be modulated by angiotensin peptides that act in part through intracellular AT1 receptors.

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“…We used an amphibian model to study the influence of ACE and Ang II on ovarian steroidogenesis and prostaglandin production. In the water frog Rana esculenta , 17 β ‐estradiol, progesterone, and prostaglandin E 2 (PGE 2 ) production was modulated by ovary ACE; on the other hand, Ang II modulated the production of progesterone and prostaglandin F 2 α (PGF 2 α ), whereas androgen production was not influenced (Bramucci et al . 1997).…”

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confidence: 99%

Bradykinin is not involved in angiotensin converting enzyme modulation of ovarian steroidogenesis and prostaglandin production in frog Rana esculenta

Bramucci

Miano

Gobbetti

et al. 2002

Acta Physiologica Scandinavica

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Angiotensin converting enzyme (ACE) was demonstrated to modulate the production of 17beta-estradiol, progesterone and prostaglandin E2 (PGE2) in frog ovary of Rana esculenta. However, the activity was not mediated by angiotensin II (Ang II). In an attempt to identify the peptide involved in the pathway modulated by ACE, bradykinin, another physiological substrate of ACE, was chosen and incubated in the presence of the membrane suspension purified from the frog ovary homogenate. The hydrolytic products were analysed by reverse-phase high-pressure liquid chromatography (HPLC) analysis and the results showed that bradykinin was metabolized by membrane suspension. The presence of the protease inhibitors in the incubation mixture indicated ACE and neutral endopeptidase as being responsible for the bradykinin hydrolysis. Frog ovary was incubated in vitro in the presence of bradykinin (10 microM), bradykinin receptor antagonist NPC 567 (1 mg mL-1), bradykinin fragment (1-7) (10 microM), ACE (2.5 mU mL-1), captopril (0.1 mM) and lisinopril (0.1 mM). The results showed no modulating activity by bradykinin on ovarian 17beta-estradiol and PGE2 production, thus demonstrating that it was not involved in the ACE-modulated pathway.

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Different modulation of steroidogenesis and prostaglandin production in frog ovary in vitro by ACE and ANG II

Cited by 9 publications

References 32 publications

Angiotensin Converting Enzyme in Bovine Ovarian Follicular Fluid and its Relationship with Oestradiol and Progesterone

Angiotensin Converting Enzyme in Bovine Ovarian Follicular Fluid and its Relationship with Oestradiol and Progesterone

Localized accumulation of angiotensin II and production of angiotensin-(1–7) in rat luteal cells and effects on steroidogenesis

Bradykinin is not involved in angiotensin converting enzyme modulation of ovarian steroidogenesis and prostaglandin production in frog Rana esculenta

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