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Lifestyle management is the cornerstone of both primary and secondary prevention of atherosclerotic cardiovascular disease (ASCVD) and the importance of lifestyle management is emphasised by all major guidelines. Despite this, actual implementation of lifestyle management is poor. Lifestyle modification includes smoking cessation, weight loss, dietary change, increasing physical inactivity, and stress management. This review summarises evidence-based opportunities and challenges for healthcare professionals to promote healthy lifestyles at an individual level for the prevention of ASCVD. [ABSTRACT FROM AUTHOR]

The high prevalence and burden of cardiovascular diseases (CVD) is largely attributable to unhealthy lifestyle factors such as smoking, alcohol consumption, physical inactivity and unhealthy food habits. Prevention of CVD, through the promotion of healthy lifestyles, appears to be a Sisyphean task for healthcare professionals, as the root causes of an unhealthy lifestyle lie largely outside their scope. Since most lifestyle choices are habitual and a response to environmental cues, rather than rational and deliberate choices, nationwide policies targeting the context in which lifestyle behaviours occur may be highly effective in the prevention of CVD. In this point-of-view article, we emphasise the need for government policies beyond those mentioned in the National Prevention Agreement in the Netherlands to effectively reduce the CVD risk, and we address the commonly raised concerns regarding 'paternalism'. [ABSTRACT FROM AUTHOR]

Elevated cardiac troponin-I (cTnI) levels have been demonstrated in serum of patients without acute coronary syndromes, potentially via a stretch-related process. We hypothesize that this cTnI release from viable cardiomyocytes is mediated by stimulation of stretch-responsive integrins. Cultured cardiomyocytes were treated with (1) Gly–Arg–Gly–Asp–Ser ( GRGDS, n = 22) to stimulate integrins, (2) Ser–Asp–Gly–Arg–Gly ( SDGRG, n = 8) that does not stimulate integrins, or (3) phosphate-buffered saline (control, n = 38). Cells and media were analyzed for intact cTnI, cTnI degradation products, and matrix metalloproteinase (MMP)-2. Cell viability was examined by assay of lactate dehydrogenase (LDH) activity and by nuclear staining with propidium iodide. GRGDS-induced integrin stimulation caused increased release of intact cTnI (9.6 ± 3.0%) as compared to SDGRG-treated cardiomyocytes (4.5 ± 0.8%, p < 0.001) and control (3.0 ± 3.4%, p < 0.001). LDH release from GRGDS-treated cardiomyocytes (15.9 ± 3.8%) equalled that from controls (15.2 ± 2.3%, p = n.s.), indicating that the GRGDS-induced release of cTnI is not due to cell necrosis. This result was confirmed by nuclear staining with propidium iodide. Integrin stimulation increased the intracellular and extracellular MMP2 activity as compared to controls (both p < 0.05). However, despite the ability of active MMP2 to degrade cTnI in vitro, integrin stimulation in cardiomyocytes was not associated with cTnI degradation. The present study demonstrates that intact cTnI can be released from viable cardiomyocytes by stimulation of stretch-responsive integrins. [ABSTRACT FROM AUTHOR]

The myocardial stretch-induced increase in intracellular [Ca2+] ([Ca2+]i) is considered to be caused by integrin stimulation. Myocardial stretch is also associated with increased nitric oxide (NO) formation. We hypothesised that NO is implicated in calcium signalling following integrin stimulation. Integrins of neonatal rat cardiomyocytes were stimulated with a pentapeptide containing the Arg-Gly-Asp (RGD) sequence. [Ca2+]i was measured with Fura2, [NO]i was measured with DAF2 and phosphorylation of focal adhesion kinase (FAK) was monitored with immunofluorescence techniques. Integrin stimulation increased both [NO]i and [Ca2+]i, the latter response being inhibited by ryanodine receptor-2 (RyR2) blockers and by N G -monomethyl- L-arginine (L-NMMA), an inhibitor of NOS, but resistant to GdCl3, diltiazem and wortmannin. Integrin-induced intracellular Ca2+ release thus appears to be independent of the influx of extracellular Ca2+ and phosphatidylinositol-3 kinase activity. In addition, integrin stimulation induced phosphorylation of FAK. Our results provide evidence for an integrin-induced Ca2+ release from RyR2 which is mediated by NO formation, probably via FAK-induced NOS activation. [ABSTRACT FROM AUTHOR]