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- 저자 : Lagi, Marco (검색결과 4 건)
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Hypertensive emergencies: a new clinical approach
Alfonso Lagi,Simone Cencetti 대한고혈압학회 2015 Clinical Hypertension Vol.21 No.16
The expression ‘hypertensive urgencies’ includes many diseases. The unifying features of these diseases are a high level of arterial pressure and acute distress of one or more organs. The aim of the review was to define the idea of the ‘acute hypertension’ as a new concept, different from ‘chronic hypertension’. Acute hypertension might be related to ‘organ damage’ because it is the cause, the consequence or an effect of the acute stress. We compounded a narrative review which has included analyses of 373 articles. The structure of the search strategy included a literature search of PubMed, MEDLINE, Cochrane Library and Google Scholar databases. We applied the following inclusion criteria: prospective double-blind randomised controlled trials, experimental animal work studies, case–control studies and recruiting patients representative of the general sick population. In this review, the diseases included in the term ‘hypertensive emergencies’ share ‘acute’ hypertension. This is a new idea that emphasises the suddenly increased arterial pressure, irrespective of the initial arterial pressure and independent of the goals of hypertension control. The ‘hypertensive emergencies’ have been grouped together in three subsets: (1) diseases that result from acute hypertension that is caused by faulty regulation of the peripheral circulation (acute primary hypertension), (2) diseases that produce hypertension (acute secondary hypertension) and 3) diseases that have hypertension as an effect of the acute stress caused by the principle disease (acute associated hypertension). This review highlights a novel idea: acute hypertension is a common sign of different diseases characterised by the sudden surge of arterial pressure, so overwhelming the difference between hypertensive emergencies and urgencies. The judgment of acute hypertension is independent of the initial arterial pressure, normotension or hypertension and is linked with the transient failure of the baroreflex. Hypertensive emergencies are grouped together because all of these diseases require prompt therapy to prevent the negative outcomes of acute hypertension
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Chen, Sow-Hsin,Lagi, Marco,Chu, Xiang-qiang,Zhang, Yang,Kim, Chansoo,Faraone, Antonio,Fratini, Emiliano,Baglioni, Piero IOS Press 2010 Spectroscopy Vol.24 No.1
<P>This review article describes our neutron scattering experiments made in the past four years for the understanding of the single-particle (hydrogen atom) dynamics of a protein and its hydration water and the strong coupling between them. We found that the key to this strong coupling is the existence of a fragile-to-strong dynamic crossover (FSC) phenomenon occurring at around TL=225±5 K in the hydration water. On lowering of the temperature toward FSC, the structure of hydration water makes a transition from predominantly the high density form (HDL), a more fluid state, to predominantly the low density form (LDL), a less fluid state, derived from the existence of a liquid–liquid critical point at an elevated pressure. We show experimentally that this sudden switch in the mobility of hydration water on Lysozyme, B-DNA and RNA triggers the dynamic transition, at a temperature TD=220 K, for these biopolymers. In the glassy state, below TD, the biopolymers lose their vital conformational flexibility resulting in a substantial diminishing of their biological functions. We also performed molecular dynamics (MD) simulations on a realistic model of hydrated lysozyme powder, which confirms the existence of the FSC and the hydration level dependence of the FSC temperature. Furthermore, we show a striking feature in the short time relaxation (β-relaxation) of protein dynamics, which is the logarithmic decay spanning 3 decades (from ps to ns). The long time α-relaxation shows instead a diffusive behavior, which supports the liquid-like motions of protein constituents. We then discuss our recent high-resolution X-ray inelastic scattering studies of globular proteins, Lysozyme and Bovine Serum Albumin. We were able to measure the dispersion relations of collective, intra-protein phonon-like excitations in these proteins for the first time. We found that the phonon energies show a marked softening and at the same time their population increases substantially in a certain wave vector range when temperature crosses over the TD. Thus the increase of biological activities above TD has positive correlation with activation of slower and large amplitude collective motions of a protein.</P>
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