Objective: To analyze the role of the local renin-angiotensin system (RAS) in the female reproductive system to modulate ovarian steroidogenesis and its relationship with alpha(1)adrenergic receptors.
Design: Observational study.
Setting: University laboratory.
Animal(s): Adult female Wistar rats treated with doxazosin (10 mg/kg) or vehicle for 15 days.
Intervention(s): Samples from the whole right ovary were dissected after perfusion with saline. The soluble and membrane-bound fractions were obtained from these samples. Also, blood samples were used to obtain the serum.
Main Outcome Measure(s): Fluorometric measurement of soluble and membrane-bound RAS-regulating proteolytic regulatory enzyme activities by using arylamide derivatives as substrates. Time-resolved fluoroimmunoassay of serum E(2) and P.
Result(s): alpha(1)Adrenergic receptor blockade increases ovarian soluble and membrane-bound aminopeptidase A and decreases membrane-bound aminopeptidase N and aminopeptidase B. Furthermore, serum P levels increased, whereas serum E(2) did not change.
Conclusion(s): Ovarian P production, at least in the rat, is regulated by noradrenaline through a mechanism of action in which the RAS is involved, with a main role for angiotensin III.
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http://dx.doi.org/10.1016/j.fertnstert.2006.12.021 | DOI Listing |
Methods Mol Biol
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Estrella Mountain Community College, Phoenix, AZ, USA.
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Department of Ophthalmology, National Taiwan University Hospital, No. 7, Chung Shan S. Rd. (Zhongshan S. Rd.), Zhongzheng Dist., Taipei City 100225, Taiwan.
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Department of Immunology, School of Medicine, Zanjan University of Medical Sciences, Zanjan, Iran. Electronic address:
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Department of Internal Medicine, University of Texas Southwestern Medical Center, Dallas, TX, USA.
Soluble, circulating Klotho (sKlotho) is essential for normal health and renal function. sKlotho is shed from the renal distal convoluted tubule (DCT), its primary source, via enzymatic cleavage. However, the physiologic mechanisms that control sKlotho production, trafficking, and shedding are not fully defined.
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Department of Biochemistry, Groningen Biomolecular Science and Biotechnology Institute, University of Groningen, Nijenborgh 3, Groningen, The Netherlands.
Cyclic di-adenylate monophosphate (cyclic di-AMP) is an important second messenger in microorganisms. Cyclic di-AMP regulates bacterial cell volume and turgor via control of potassium and compatible solute transport but is also involved in many other processes, including the activation of the metazoan innate immune response to bacterial infections. We compare the activity of full-length membrane-embedded CdaA, the enzyme that synthesizes cyclic di-AMP, with the water-soluble catalytic domain CdaA-DAC.
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