Perceptions and attitudes toward partners support for cervical cancer screening among married men in Ghana.

OBJECTIVES: The majority of literature on cervical cancer (CC) and cervical cancer screening (CCS) focused on women all over the world. However, research has indicated that men's involvement in CCS can lead to improved health outcomes for women. Despite this, there is limited information available in the literature regarding men's attitudes toward CCS. This highlights the need for further study on the subject to increase understanding and improve outcomes. The purpose of this study was therefore to explore the perceptions and attitudes toward partners' support for CCS among married men from the Adentan Municipality. STUDY DESIGN: An exploratory descriptive qualitative approach was used in the study to explore the perceptions of married men about male involvement in CCS. METHODS: Thirty-four married men were purposively selected to be part of the interviews. A semistructured interview guide was used to collect data, which were recorded. The tape-recorded data were reproduced verbatim, and content analysis was carried out to generate the themes and subthemes. RESULTS: Three themes and nine subthemes were constructed from the data analysis. The study revealed that the perceptions of males about cervical cancer had a positive or a negative influence on women's behaviors toward CCS. It was interesting that some men constantly reminded their wives to participate in CCS. However, some barriers to men's support included fear of trauma to the wife's vagina during screening and concerns about exposure to the wife's nakedness. CONCLUSION: It was therefore recommended that healthcare facilities should roll out sustainable programs and policies to involve men in CC prevention. In addition, health workers should devise innovative ways to make male involvement in CCS more attractive to men.

Unique Genetic and Histological Signatures of Mouse Pericardial Adipose Tissue.

Obesity is a major risk factor for a plethora of metabolic disturbances including diabetes and cardiovascular disease. Accumulating evidence is showing that there is an adipose tissue depot-dependent relationship with obesity-induced metabolic dysfunction. While some adipose depots, such as subcutaneous fat, are generally metabolically innocuous, others such as visceral fat, are directly deleterious. A lesser known visceral adipose depot is the pericardial adipose tissue depot. We therefore set out to examine its transcriptional and morphological signature under chow and high-fat fed conditions, in comparison with other adipose depots, using a mouse model. Our results revealed that under chow conditions pericardial adipose tissue has uncoupling-protein 1 gene expression levels which are significantly higher than classical subcutaneous and visceral adipose depots. We also observed that under high-fat diet conditions, the pericardial adipose depot exhibits greatly upregulated transcript levels of inflammatory cytokines. Our results collectively indicate, for the first time, that the pericardial adipose tissue possesses a unique transcriptional and histological signature which has features of both a beige (brown fat-like) but also pro-inflammatory depot, such as visceral fat. This unique profile may be involved in metabolic dysfunction associated with obesity.

Increasing doxorubicin activity against breast cancer cells using PPARγ-ligands and by exploiting circadian rhythms.

BACKGROUND AND PURPOSE: Doxorubicin is effective against breast cancer, but its major side effect is cardiotoxicity. The aim of this study was to determine whether the efficacy of doxorubicin on cancer cells could be increased in combination with PPARγ agonists or chrono-optimization by exploiting the diurnal cycle. EXPERIMENTAL APPROACH: We determined cell toxicity using MCF-7 cancer cells, neonatal rat cardiac myocytes and fibroblasts in this study. KEY RESULTS: Doxorubicin damages the contractile filaments of cardiac myocytes and affects cardiac fibroblasts by significantly inhibiting collagen production and proliferation at the level of the cell cycle. Cyclin D1 protein levels decreased significantly following doxorubicin treatment indicative of a G1/S arrest. PPARγ agonists with doxorubicin increased the toxicity to MCF-7 cancer cells without affecting cardiac cells. Rosiglitazone and ciglitazone both enhanced anti-cancer activity when combined with doxorubicin (e.g. 50% cell death for doxorubicin at 0.1 µM compared to 80% cell death when combined with rosiglitazone). Thus, the therapeutic dose of doxorubicin could be reduced by 20-fold through combination with the PPARγ agonists, thereby reducing adverse effects on the heart. The presence of melatonin also significantly increased doxorubicin toxicity, in cardiac fibroblasts (1 µM melatonin) but not in MCF-7 cells. CONCLUSIONS AND IMPLICATIONS: Our data show, for the first time, that circadian rhythms play an important role in doxorubicin toxicity in the myocardium; doxorubicin should be administered mid-morning, when circulating levels of melatonin are low, and in combination with rosiglitazone to increase therapeutic efficacy in cancer cells while reducing the toxic effects on the heart.

Ethno-Botanical Survey Of Medicinal Plants In The Plant Genetic Resources Centre Arboretum - Bunso

The ethnobotanical uses and mode of administration of twenty-nine medicinal plants; found in the arboretum of the Plant Genetic Resource Centre located at Bunso in the eastern region of Ghana; against some disease conditions are hereby documented

Low-dose ramipril treatment improves relaxation and calcium cycling after established cardiac hypertrophy.

Rapid cooling contractures were used in this study to test whether low-dose ramipril improves sarcoplasmic reticulum (SR) Ca(2+) uptake and Na(+)/Ca(2+) exchanger function in isolated hypertrophied rat myocytes. Compensated cardiac hypertrophy was induced by abdominal aortic constriction for 5 wk followed by administration of ramipril (50 microg x kg(-1) x day(-1)) or vehicle for 4 wk. Myocyte cell length and cell width were significantly (P < 0.05) increased in both hypertrophied groups (+/-ramipril). Myocytes were loaded with indo 1, and relaxation was investigated after rapid cooling. Hypertrophied myocyte relaxation in Na(+)-free/Ca(2+)-free solution was 63% slower (P < 0.01) and the fall in intracellular Ca(2+) was 60% slower (P < 0.05) than the relaxation of control cells. After ramipril treatment both relaxation and the decline in intracellular Ca(2+) returned to control rates through improved SR Ca(2+)-ATPase function. Relaxation in caffeine showed no change after hypertrophy; however, after ramipril treatment the time to 50% relaxation in caffeine decreased by 30% (P < 0.05). The improvement in Ca(2+) extrusion across the sarcolemmal membrane occurred independently of changes in Na(+)/Ca(2+) exchanger mRNA and protein abundance. These data demonstrate that ramipril improves both SR-dependent and non-SR-dependent calcium cycling after established cardiac hypertrophy. However, the improvements in function are independent of transcriptional activation and likely to involve altered intracellular ion concentrations.

Translation is regulated via the 3' untranslated region of alpha-myosin heavy chain mRNA by calcium but not by its localization.

Posttranscriptional regulation plays an important role in alpha-myosin heavy chain (alpha-MyHC) protein synthesis in cardiac muscle cells. In the present study, we test the effects of calcium and mRNA mislocalization on alpha-MyHC translation in order to determine the mechanism(s) contributing to translational block via the 3' untranslated region (3'UTR). Neonatal rat cardiac myocytes were treated for 6 h with L-isoproterenol (10 microM) to enhance beating, with 10 microM verapamil to block beating and mislocalize mRNA, or with 3 microM colchicine to enhance beating but mislocalize mRNA by depolymerization of the microtubules. In order to determine whether translation is regulated by the 3'UTR, either a control (SV40 3'UTR) or the experimental (alpha-MyHC 3'UTR) was placed after a luciferase reporter gene and transfected into the myocytes. The amount of luciferase protein only decreased significantly in verapamil arrested cells transfected with the alpha-MyHC 3'UTR construct (P < 0.01). To control for the possibility that pharmacological treatments might affect transcription or message stability, we analyzed neomycin and luciferase mRNA levels transcribed from the same transfected plasmid. No significant changes were found with an RNase protection assay. These results suggest that calcium but not mRNA localization regulates protein synthesis and further, this is mediated by the 3' untranslated region of alpha-MyHC.

Sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA2) gene products are regulated post-transcriptionally during rat cardiac development.

OBJECTIVE: The Sarco(endo)plasmic reticulum Ca(2+)-ATPase (SERCA2) plays a major role in the contraction-relaxation cycle and is responsible for transporting calcium into the lumen of the sarcoplasmic reticulum. This study was performed to determine if the increase in SERCA2 messenger RNA (mRNA) abundance during the perinatal period is regulated transcriptionally. METHODS: Transcriptional activity was determined by nuclear run-on assays and mRNA and protein abundances were determined during late fetal and early neonatal cardiac development in rat. RESULTS: From nuclear run-on assays, SERCA2 gene transcription at 17/18 embryonic days (139 +/- 41 parts per million (ppm), n = 7) did not differ from that at 20 neonatal days (139 +/- 37 ppm, n = 6) after birth. No increase in transcriptional activity could be demonstrated during the time frame examined. In contrast, both alpha and beta myosin heavy chains showed significant changes in measured transcriptional activity. SERCA2 mRNA normalized to 18S RNA levels are very low in the fetus (9.8 +/- 1.9 to 13.4 +/- 4.9 arbitrary units (A.U.) from 17/18 to 19/20 embryonic days) and significantly increase from birth (15 +/- 3.8 A.U.) to reach a maximum at 20 days of age (29.1 +/- 9.5 to 48.3 +/- 7.0 in 15 to 20 neonatal days rats respectively). Similarly, SR Ca(2+)-ATPase protein levels are less abundant in the fetus (0.82 +/- 0.08 to 1.13 +/- 0.13 A.U./microgram total protein) and reach a maximum at 15-20 neonatal days (3.08 +/- 0.58 to 2.98 +/- 0.17). Ca2+ uptake in the fetal heart is about one sixth the level seen in the adult, reaches the highest observed value at 5 days after birth (6.05 +/- 0.77 pmole Ca2+ per microgram/min) and remains relatively constant over the next 15 days. The activity increases even though phospholamban protein increases in abundance. CONCLUSIONS: Since the transcriptional activity of this gene is unchanged whereas the mRNA, protein abundance and activity increase, we conclude that the abundance of SERCA2 gene products is regulated primarily through post-transcriptional mechanisms during the perinatal period.

The role of natriuretic peptides in cardiovascular disorders and human cardiac allografts (Review).

The human myocardium is composed of a variety of cardiac cell types that synthesise cardioactive factors with autocrine, paracrine and endocrine functions. These cardioactive factors include a family of structurally and functionally related peptides, natriuretic peptides (NPs), that act as cardiovascular cell growth modulatory factors and have significant influence on the regulation of cardiovascular function. The three members of the NP family are atrial natriuretic peptide, brain natriuretic peptide and C-type natriuretic peptide. NPs are ubiquitously expressed in cardiovascular tissues and have specific receptors in cardiac cells, brain cells, vascular endothelial cells and extracardiac tissues through which they elicit a variety of biological responses including natriuresis, diuresis and vasodilation. Cardiac transplantation is the most effective and definitive treatment for end-stage cardiac failure in humans. Orthotopic cardiac transplantation and cardiovascular disorders including hypertension, cardiac hypertrophy, cardiac failure, result in increased myocardial expression of NPs, suggesting a pathophysiological role for these peptides in the heart. The mechanism by which the expression of NPs is regulated in the transplanted human heart is not well understood. Understanding the mechanism of local expression of NPs and their interactions with other putative growth regulatory factors in the human heart may have important implications for potential management of cardiovascular disorders and cardiac transplantation. This article will discuss the current knowledge of NPs in cardiovascular disorders. Most of the emphasis will focus on their possible role in human cardiac allografts as there have been no reviews on this important topic.

Sub-antihypertensive doses of ramipril normalize sarcoplasmic reticulum calcium ATPase expression and function following cardiac hypertrophy in rats.

We examined the hypothesis that the angiotensin converting enzyme inhibitor ramipril at sub-antihypertensive concentrations could improve sarcoplasmic reticulum (SR) CaATPase expression and function in compensated hypertrophied rat hearts. Five weeks after abdominal aortic constriction, rats received a daily dose (50 micrograms/kg/day) of ramipril or vehicle for 4 weeks. Cardiac angiotensin-converting enzyme (ACE) activity increased with cardiac hypertrophy (CH) but returned to normal following ramipril treatment. SR CaATPase protein levels and activity decreased with CH (P < 0.05) and were normalized following ramipril treatment (P < 0.05 for protein and activity). No change in phospholamban (PLB) protein levels could be demonstrated between any of the groups. In contrast, ramipril treatment specifically increased control SR CaATPase and PLB mRNA levels by > 60% (P < 0.01) and > 30%, respectively. In the hypertrophied group, SR CaATPase increased by 35% (P < 0.05 n = 6) after ramipril treatment. Calsequestrin mRNA levels were unaffected by ramipril administration. In conclusion, ramipril normalizes SR CaATPase protein expression and function in pressure-overloaded and compensated CH. The effects of ramipril are however multifaceted, affecting RNA and protein expression differentially.

Inhibition of endogenous cardiac phosphatase activity and measurement of sarcoplasmic reticulum calcium uptake: a possible role of phospholamban phosphorylation in the hypertrophied myocardium.

The activity of the sarcoplasmic reticulum (SR) CaATPase in cardiac muscle is regulated by phospholamban via its ability to be phosphorylated. It is unclear what role phospholamban phosphorylation plays in cardiac adaptation and disease. The study of the native phospholamban phosphorylation in tissue has been technically difficult because of the presence of endogenous enzymes. Using mobility shifts on SDS PAGE gels we have demonstrated that significant dephosphorylation of phospholamban occurs during tissue homogenisation in the absence of phosphatase inhibitors. Endogenous kinases do not appear to alter phospholamban phosphorylation. When 10 mM NaF (a phosphatase inhibitor) was used in the preparation of crude SR homogenates, CaATPase activity (measured by oxalate stimulated calcium uptake) was stimulated almost 2 fold, p < 0.01. Increased CaATPase activity in NaF was associated with increased phospholamban phosphorylation. Phosphatase inhibitors were used in tissue homogenisation to determine phospholamban phosphorylation in normal hearts and in cardiac hypertrophy induced by abdominal aortic constriction. In 50 mM NaF which completely inhibits endogenous phosphatases, phospholamban from hypertrophied hearts had a slower mobility compared with normal hearts. This suggests that phospholamban was more highly phosphorylated in cardiac hypertrophy. Increased phospholamban phosphorylation following cardiac hypertrophy may enable the myocardium to compensate functionally in the early stages of adaptation.

Kinetics of induction and protective effect of heat-shock proteins after cardioplegic arrest.

BACKGROUND: Heat-shock proteins are known to enhance cardiac resistance to ischemia. METHODS: To evaluate the kinetics of heat-shock protein 70 in relation to its effect on postischemic recovery of cardiac mechanical (cardiac output) and endothelial function (as percentage increase of coronary flow in response to 5-hydroxytryptamine), isolated rat hearts were subjected to prolonged hypothermic cardioplegic arrest at different intervals ranging from 12 to 96 hours after heat stress (n = 6 in each interval). RESULTS: Immunoblotting showed the maximal level of heat-shock protein 70, 0.65 +/- 0.10 (arbitrary units +/- standard error of the mean), at 24 hours after heat shock and similar values at 26 and 30 hours (p = not significant). Postischemic recovery of cardiac output and endothelial function (percentage of preischemic value +/- standard error of the mean) observed at 24 hours was 74.0 +/- 2.4 and 58.3 +/- 7.2, respectively. Similar values were observed at 26 and 30 hours (p = not significant). CONCLUSIONS: In a protocol mimicking conditions for cardiac transplantation, postischemic recovery of cardiac output and endothelial function was improved when the interval between heat stress and ischemia ranged from 24 to 30 hours. This correlated with an apparently critical amount of heat-shock protein 70.

Induction of heat-shock proteins enhances myocardial and endothelial functional recovery after prolonged cardioplegic arrest.

The aim of this study was to investigate the role of heat-shock proteins after heat-shock stress on the post-ischemic recovery of cardiac mechanical and endothelial function following a prolonged cardiac arrest. Isolated working rat hearts were subjected to a cardioplegic arrest for 4 hours at 4 degrees C. Three groups (n = 8 in each) were studied: (1) control, (2) sham-treated, and (3) heat-shocked rats. Postischemic recovery of cardiac output and endothelial function (as percent of preischemic control values) was 57.8% +/- 2.8% and 20.8% +/- 3.9% in group 1, 50.9% +/- 4.0% and 26.3% +/- 5.9% in group 2, and 74.0% +/- 2.4% and 51.2% +/- 8.0% in group 3, respectively. Both postischemic myocardial and endothelial function were improved by heat stress.