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1.
J Hum Hypertens ; 25(7): 444-50, 2011 Jul.
Article in English | MEDLINE | ID: mdl-20686500

ABSTRACT

The prognostic value of ambulatory blood pressure (BP) monitoring for long-term prognosis varies in recent studies. The study aimed to investigate the role of ambulatory BP parameters in mortality and cardiovascular (CV) events in hypertensive patients. A series of 412 participants (59.3 ± 4.0 years) who received ambulatory BP monitoring for their fluctuated BP, either untreated or treated since 1995, were enroled. The mortality and CV events were obtained by follow-up and linked to the National Death Registry in Taiwan. There were 233 untreated and 179 treated patients. The latter were older with more comorbidity when compared with the former. After follow-up for 8.5 ± 1.7 years, both ambulatory systolic BP and pulse pressure (PP) could predict all-cause mortality, non-CV mortality, CV disease and stroke after adjusting for baseline covariates. However, only ambulatory PP could predict CV mortality and coronary heart disease. Ambulatory PP is better than ambulatory systolic BP, particularly in prediction of all-cause mortality. There was no predictive value of office BP in any outcome. In conclusion, ambulatory PP is a good predictor for long-term outcomes in hypertensive patients. The parameters of ambulatory rather than office BP could be applied for risk stratification either before or under antihypertensive treatment.


Subject(s)
Blood Pressure/physiology , Cardiovascular Diseases/physiopathology , Hypertension/physiopathology , Adult , Aged , Blood Pressure Monitoring, Ambulatory , Female , Follow-Up Studies , Humans , Male , Middle Aged , Prognosis , Registries , Taiwan
2.
Mol Cell Proteomics ; 9(10): 2089-98, 2010 Oct.
Article in English | MEDLINE | ID: mdl-20562470

ABSTRACT

Surface topography and texture of cell culture substrata can affect the differentiation and growth of adherent cells. The biochemical basis of the transduction of the physical and mechanical signals to cellular responses is not well understood. The lack of a systematic characterization of cell-biomaterial interaction is the major bottleneck. This study demonstrated the use of a novel subcellular fractionation method combined with quantitative MS-based proteomics to enable the robust and high-throughput analysis of proteins at the adherence interface of Madin-Darby canine kidney cells. This method revealed the enrichment of extracellular matrix proteins and membrane and stress fibers proteins at the adherence surface, whereas it shows depletion of extracellular matrix belonging to the cytoplasmic, nucleus, and lateral and apical membranes. The asymmetric distribution of proteins between apical and adherence sides was also profiled. Apart from classical proteins with clear involvement in cell-material interactions, proteins previously not known to be involved in cell attachment were also discovered.


Subject(s)
Proteomics , Animals , Cells, Cultured , Dogs , Extracellular Matrix Proteins/metabolism , Mass Spectrometry
3.
Curr Microbiol ; 33(4): 224-7, 1996 Oct.
Article in English | MEDLINE | ID: mdl-8824167

ABSTRACT

The cytotoxic effects of anthrax lethal toxin purified from an avirulent strain were examined on mouse macrophage-like J774A.1 cells. Cell death induced by high concentration of purified lethal toxin had the characteristics of necrosis. At lower concentrations, the toxin caused no morphological change and most of the cells were viable. Interestingly, apoptotic cells were observed when the cells were preincubated with a serine/threonine phosphatase inhibitor, calyculin A, and then exposed to a toxin concentration of 0.1 microg/ml. This is the first report that lethal toxin of the anthrax bacillus can induce both necrosis and apoptosis and that protein phosphatases are implicated in the regulation of bacterial toxin-induced apoptosis.


Subject(s)
Bacillus anthracis/chemistry , Bacterial Toxins/pharmacology , Macrophages/drug effects , Animals , Apoptosis , Marine Toxins , Mice , Necrosis , Oxazoles/pharmacology , Phosphoprotein Phosphatases/metabolism
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