Background: The aim of this study was to assess the efficacy and safety of a new herbal preparation (Menopause Relief EP®), the hybrid combination of Actaea racemosa L. (black cohosh, BC) and Rhodiola rosea L. (RR) root extracts, compared with the most effective dose of BC extract in women with menopausal complaints. Methods: A total of 220 women were randomly assigned to receive two capsules either BC (6.5 mg), BC500 (500 mg), Menopause Relief EP® (206,5), or placebo once per day for 12 weeks. The efficacy endpoints were relief of menopausal symptoms, measured using the Kupperman Menopausal Index (KMI), Menopause Relief Score (MRS), and menopause Utian Quality of Life (UQOL) index. Results: The menopause symptom relief effects of RR-BC were significantly superior in all tests to the effects of BC and placebo after their repeated administration for 6 and 12 weeks. There was no statistically significant difference between the effects of BC and BC500 over time. RR-BC significantly improved the QOL index in patients, compared to BC, BC500, and placebo, mainly due to the beneficial effects on the emotional and health domains. Conclusions: BC is more effective in combination with RR in relief of menopausal symptoms, particularly psychological symptoms.
Beta-microseminoprotein (MSP) is a predominant protein of human seminal plasma and originates from prostate secretions. MSP from boar seminal plasma has been sequenced and shows only 50%-52% homology with that of human. Porcine MSP is synthesized by the post-natal prostate gland and is identical with the sperm motility inhibitor. Although MSP is a protein characteristic of the prostate gland, we have established the presence of its mRNA transcript not only in boar prostate but also in other reproductive organ tissues. In extracts of all these organs, specific polyclonal antiMSP antibody recognizes a 12-kDa protein band identified by mass spectrometry as MSP. Immunofluorescence (IMF) has revealed the occurrence of MSP in the epithelial tissue of the prostate, epididymis, seminal vesicles and Cowper's glands. MSP has been localized on epididymal spermatozoa in the acrosomal region and on the flagellum of ejaculated spermatozoa. The absence of MSP on the surface of capacitated spermatozoa together with the antibody detection of MSP in the sperm acidic extract after in vitro capacitation indicates its acrosomal origin. Additionally, MSP has been localized by IMF in the sperm acrosome in capacitated spermatozoa with a permeabilized plasma membrane and by electron microscopy in ejaculated spermatozoa. The function of MSP in seminal plasma and spermatozoa is not fully understood. Nevertheless, the secretion of porcine MSP by various reproductive organs indicates its multiple roles in the reproductive process. For the first time in mammalian species, MSP has been localized in various physiological stages of sperm.
Proteinases and proteinase inhibitors play key roles in almost all physiological processes. Proteinase inhibitors are present in all tissues and body fluids. They interfere with the activity of proteinases and thus maintain homeostasis. The main role of proteinase inhibitors in the reproductive tract is the inactivation of prematurely released hydrolytic enzymes from damaged spermatozoa and the protection of reproductive tracts and spermatozoa against proteolytic degradation. In the boar reproductive system, acrosin inhibitors are found in seminal plasma and on spermatozoa. The amino acid sequence of seminal plasma and sperm-associated acrosin inhibitors is 90% identical, and their biochemical properties have been completely resolved. However, their origin and localization have not been fully elucidated. Using rabbit polyclonal antibody, we have studied the expression and localization of the seminal plasma acrosin inhibitor in the boar reproductive tract. The antibody recognizes a 12-kDa band in extracts from the cauda epididymidis, seminal vesicles, prostate, and Cowper's glands, and immunofluorescence has revealed the acrosin inhibitor in the epithelium and lumen of these organs. Gene expression of the acrosin inhibitor has been studied by reverse transcription together with the polymerase chain reaction. Acrosin inhibitor mRNA transcript is detectable in the epididymis, seminal vesicles, prostate, and Cowper's glands. The antibody has localized the acrosin inhibitor on the surface of epididymal and ejaculated spermatozoa in the acrosomal region. In extracts from epididymal and ejaculated spermatozoa, the specific antibody recognizes acrosin inhibitor at 8 kDa and 12 kDa. The presence of acrosin inhibitor on the sperm surface as a protective molecule for receptors mediating the sperm-zona pellucida binding suggests that it is crucial for the reproductive process.
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