ABSTRACT
Variceal bleeding occurs primarily in the esophagus or stomach in patients with liver cirrhosis, but can also occur rarely in the duodenum. Duodenal variceal bleeding has a high mortality and poor prognosis due to heavy blood flow originating from the portal vein (PV) and the technical difficulty of hemostatic procedures. Treatments including endoscopic sclerotherapy, endoscopic ligations, endoscopic clipping and transjugular intrahepatic portosystemic shunt have been tried, with only moderate and variable success. A percutaneous transsplenic approach offers another way of accessing the PV. Here we report a case of successfully treated duodenal variceal bleeding by percutaneous transsplenic embolization.
Subject(s)
Esophageal and Gastric Varices/diagnosis , Gastrointestinal Hemorrhage/therapy , Liver Cirrhosis/diagnosis , Portasystemic Shunt, Transjugular Intrahepatic , Aged , Duodenum , Embolization, Therapeutic , Endoscopy, Gastrointestinal , Esophageal and Gastric Varices/complications , Humans , Liver Cirrhosis/complications , Male , Portal Vein/diagnostic imaging , Recurrence , Tomography, X-Ray ComputedABSTRACT
A 51-year-old highly fit man presented for dyspnea with strenuous aerobic exercise. The patient was asymptomatic and all tests were normal at rest. With increasing exercise intensity, he suddenly complained of dyspnea and showed a severe exercise-induced hypoxemia with an excessive alveolar-arterial oxygen tension difference. In agitated saline contrast echocardiography at peak exercise, a large amount of left to right shunt was identified after > 5 cardiac cycles, which suggests the presence of exercise-induced intrapulmonary arteriovenous shunt in this patient.
ABSTRACT
The neurofibrillary tangles (NFTs) formed by the accumulation of abnormal tau filaments have been shown to be involved in Alzheimer's disease (AD) brain degeneration. In this study, a tau transgenic mouse (pNSE/htau23) model was used to monitor changes in protein levels and to search for novel biomarker candidates suitable for the early diagnosis of AD before onset of clinical symptoms. Plasma samples from 2-month (n=13, asymptomatic) and 4-month (n=7, symptomatic) tau transgenic mice were compared to the control group (n=8) by 2-dimensional gel electrophoresis (2-DE) coupled with liquid chromatography-tandem mass spectrometry (LC-MS/MS). Three proteins, ATP synthase, Adenosine kinase and Regucalcin showed significantly decreased levels in the plasma of tau transgenic mouse, which was further confirmed by Western blotting. This study suggests that these proteins could be used as candidate biomarkers for early diagnosis of AD in combination with previously discovered protein biomarkers.
Subject(s)
Gene Expression Regulation/genetics , Plasma/metabolism , Proteomics , tau Proteins/genetics , ATP Synthetase Complexes/genetics , ATP Synthetase Complexes/metabolism , Adenosine Kinase/genetics , Adenosine Kinase/metabolism , Age Factors , Analysis of Variance , Animals , Calcium-Binding Proteins/genetics , Calcium-Binding Proteins/metabolism , Chromatography, Liquid , Electrophoresis, Gel, Two-Dimensional , Humans , Intracellular Signaling Peptides and Proteins/genetics , Intracellular Signaling Peptides and Proteins/metabolism , Mice , Mice, Transgenic/blood , Mutation/genetics , Silver Staining , Tandem Mass SpectrometryABSTRACT
Recent reports have suggested that vibration has beneficial effects on knee healing response; however, the biomechanism of these beneficial effects still need to be determined on the anterior cruciate ligament (ACL) cell level. In this study, we applied a 20 Hz vibration to ACL cells, which produced a 20% increase (P < 0.001) in cell activity and 17% increase (P < 0.001) in intracellular sulfated glycosaminoglycan levels. In the 20 Hz vibration-stimulated ACL cell group, eight up-regulated (100 â¼ 300%) protein spots were identified compared with the control group by proteomics analysis. Among these proteins, Annexin A2 and Prolyl 4 hydroxylase (PH4B) were shown to have a 71% and 16% higher expression, respectively, in the 20 Hz vibration-stimulated ACL cell group by Western blotting (P < 0.001). These results indicate that vibration produces a positive cellular environment, and Annexin A2 and prolyl 4 hydroxylase are expected to help ligament repair and ACL cell proliferation by controlling cell membrane and extracellular matrix formation.
Subject(s)
Anterior Cruciate Ligament/chemistry , Anterior Cruciate Ligament/metabolism , Proteome/analysis , Stress, Physiological , Vibration , Blotting, Western , Electrophoresis, Gel, Two-Dimensional , Gene Expression Regulation , Spectrometry, Mass, Electrospray IonizationABSTRACT
Tau is a main component of the aberrant paired helical filaments (PHF) found in Alzheimer's disease (AD). It has also been reported to enhance oxidative stress, which is a major factor in the pathogenesis of neurodegenerative diseases. However, protective functions of Tau have recently been reported, including antagonizing apoptosis, in addition to its role in stabilizing microtubules. In this study, the interaction between Tau and triose phosphate isomerase (TPI) in a normal, nondisease state as well as in a neurodegeneration state was examined and demonstrated for the first time. More importantly, we also showed that Tau protects TPI against oxidative damage. An oxidative stress-induced decrease in the activity of TPI was attenuated in Tau-overexpressing cells, indicating that Tau protects TPI against oxidative damage. By contrast, the activity of TPI was decreased in Tau-transgenic (Tg) mice compared to non-Tg (NTg) mice even though protein levels were not changed in both groups. Some TPIs were found on the PHF in Tg mice, which explains the decrease in the activity of TPI. Taken together, we concluded that while Tau binds and protects TPI in normal cells, and conversely, the formation of PHF induced by Tau phosphorylation trap some TPI and trigger the functional loss of TPI in the development of neurodegenerative diseases. Our results provide new insights into understanding the in-depth involvement of Tau in the development of neurodegenerative disorders.
Subject(s)
Brain/metabolism , Neurons/metabolism , Triose-Phosphate Isomerase/metabolism , tau Proteins/physiology , Alzheimer Disease/enzymology , Alzheimer Disease/metabolism , Alzheimer Disease/pathology , Animals , Brain/enzymology , Brain/pathology , CHO Cells , Cricetinae , Cricetulus , Disease Models, Animal , Down-Regulation/physiology , Mice , Mice, Transgenic , Neurodegenerative Diseases/enzymology , Neurodegenerative Diseases/metabolism , Neurodegenerative Diseases/pathology , Neurons/enzymology , Oxidative Stress/genetics , Phosphorylation , tau Proteins/geneticsABSTRACT
The preparation of plasma membrane (PM) proteome samples is seriously difficult and time-consuming, owing to their profound hydrophobicity and low abundance. We have developed an efficient PM sample preparation method using Ultracentrifugation with Percoll and an aqueous two-phase extraction. The developed method was rapid (3 h) and provided high purities (26-fold of cell lysate) with a high yield (2.6% of whole cell lysate proteins). This method is especially useful for PM proteome studies using 2D gel electrophoresis.
Subject(s)
Blood Proteins/analysis , Proteome , Blotting, Western , Electrophoresis, Gel, Two-Dimensional , UltracentrifugationABSTRACT
Adipose tissues play a crucial endocrine role in the control of whole body glucose homeostasis and insulin sensitivity. Considering the current substantial rise in obesity and obesity-related diseases, including diabetes, it is important to understand the molecular basis of adipocyte differentiation and its control. In this study, we have analyzed the protein expression inherent to adipogenic differentiation, by 2-DE, MALDI-TOF, and RT-PCR. This study focused on proteins that were differentially expressed by the differentiation of human mesenchymal stem cells (hMSCs) to adipocytes. We conducted 2-DE for each set of proteins in the cytosol of adipocytes that had differentiated from hMSC, in a pH range from 3-10. Thirty-two protein spots were shown to have different expression levels. Among these, eight up-regulated proteins were identified by MALDI-TOF/MS, as the following: syntaxin binding protein 3, OSBP-related protein 3, phosphodiesterase, glycophorin, immunoglobulin kappa chain variable region, peroxisome proliferative activated receptor gamma (PPAR-gamma), bA528A10.3.1 (novel protein similar to KIAA01616, isoform 1), and T cell receptor V-beta 4. Four proteins: syntaxin-3, OSBP-related protein 3, PPAR-gamma and glycophorin were associated with adipogenesis.
