The use of pulmonary artery catheter can be helpful in managing patients after cardiac surgery. Nevertheless, there is a risk of serious complications, such as knotting. A 61 year old man underwent tricuspid valve replacement under cardiopulmonary bypass (CPB). After implantation of a stented tissue valve in the tricuspid valve, repositioning of the catheter was performed. After weaning from CPB, an abnormal pattern of pulmonary artery pressure was suddenly observed on the monitor. Resistance was met when removing the catheter with the balloon deflated, at a 20 cm distance from the tip of the catheter. Chest radiography showed a knot in the catheter within the right brachiocephalic vein. Superior vena cava opened and the distal part of the catheter with the knot was successfully removed.
Brachiocephalic Veins ; Cardiopulmonary Bypass ; Catheters ; Humans ; Organothiophosphorus Compounds ; Pulmonary Artery ; Stents ; Thoracic Surgery ; Thorax ; Tricuspid Valve ; Vena Cava, Superior ; Weaning

No abstract available.
Ilizarov Technique*

F-box proteins, consisting of 69 members which are organized into the three subclasses FBXW, FBXL, and FBXO, are the substrate specific recognition subunits of the SKP1-Cullin 1-F-box protein E3 ligase complex. Although βTrCP 1 and 2, members of the FBXW subfamily, are known to regulate some protein stability, molecular mechanisms by which these proteins can recognize proper substrates are unknown. In this study, it was found that βTrCP1 showed strong interaction with members of mitogen-activated protein kinases. Although extracellular signal-regulated kinase (ERK) 3, p38β, and p38δ showed weak interactions, ERK2 specifically interacted with βTrCP1 as assessed by immunoprecipitation. In interaction domain determination experiments, we found that ERK2 interacted with two independent ERK docking sites located in the F-box domain and linker domain, but not the WD40 domain, of βTrCP1. Notably, mutations of βTrCP1 at the ERK docking sites abolished the interaction with ERK2. βTrCP1 underwent phosphorylation by EGF stimulation, while the presence of the mitogen-activated protein kinase kinases inhibitor U0126, genetic silencing by sh-ERK2, and mutation of the ERK docking site of βTrCP1 inhibited phosphorylation. This inhibition of βTrCP1 phosphorylation resulted in a shortened half-life and low protein levels. These results suggest that ERK2-mediated βTrCP1 phosphorylation may induce the destabilization of βTrCP1.

F-box proteins, consisting of 69 members which are organized into the three subclasses FBXW, FBXL, and FBXO, are the substrate specific recognition subunits of the SKP1-Cullin 1-F-box protein E3 ligase complex. Although βTrCP 1 and 2, members of the FBXW subfamily, are known to regulate some protein stability, molecular mechanisms by which these proteins can recognize proper substrates are unknown. In this study, it was found that βTrCP1 showed strong interaction with members of mitogen-activated protein kinases. Although extracellular signal-regulated kinase (ERK) 3, p38β, and p38δ showed weak interactions, ERK2 specifically interacted with βTrCP1 as assessed by immunoprecipitation. In interaction domain determination experiments, we found that ERK2 interacted with two independent ERK docking sites located in the F-box domain and linker domain, but not the WD40 domain, of βTrCP1. Notably, mutations of βTrCP1 at the ERK docking sites abolished the interaction with ERK2. βTrCP1 underwent phosphorylation by EGF stimulation, while the presence of the mitogen-activated protein kinase kinases inhibitor U0126, genetic silencing by sh-ERK2, and mutation of the ERK docking site of βTrCP1 inhibited phosphorylation. This inhibition of βTrCP1 phosphorylation resulted in a shortened half-life and low protein levels. These results suggest that ERK2-mediated βTrCP1 phosphorylation may induce the destabilization of βTrCP1.

BACKGROUND: Elevated plasma homocysteine is a recently-recognized independent risk factor for cardiovascular disease. In patients with non-insulin dependent diabetes mellitus (NIDDM), plasma homocysteine concentration was reported to be elevated in association with nephropathy. However, inconsistent results were reported about the association with other microvascular complications. METHODS: To determine the relationship between plasma homocysteine and the development of chronic diabetic microvascular complications, fasting plasma homocysteine, glycemic control, lipid and lipoprotein levels, vitamin status, renal function test, and chronic diabetic microvascular complications were assessed in 101 patients with NIDDM in the present study. RESULTS: There was no difference in the plasma levels of homocysteine by sex, age, status of sugar control, duration of diabetes, other cardiovascular risk factors. Patients with diabetic microangiopathy had higher plasma homocysteine concentrations than those without diabetic microangiopathy. Moreover, there was a significant correlation between amount of urinary albumin excretion and plasma homocysteine level (p=0.004, r=0.357). However, multivariate analysis showed that only serum creatinine (beta=0.635) was independently associated with plasma homocysteine level in NIDDM patients. The increase in plasma homocysteine was not shown to increase the risk of diabetic microvascular complications independently on multiple logistic regression analysis. CONCLUSION: In conclusion, decrease of renal function is an independent determinant of plasma homocysteine level and higher plasma homocysteine is associated to diabetic microangiopathy. But an increase in plasma homocysteine in patients with NIDDM is not independently associated with diabetic microvascular complications considering renal function. Therefore, the renal function should be considered in study about relationship between plasma homocysteine level and the development and/or progression of chronic diabetic microvascular complications in diabetic patients.
Cardiovascular Diseases ; Creatinine ; Diabetes Complications* ; Diabetes Mellitus ; Diabetes Mellitus, Type 2* ; Diabetic Angiopathies ; Fasting ; Homocysteine* ; Humans ; Hypercalcemia ; Lipoproteins ; Logistic Models ; Multivariate Analysis ; Plasma* ; Risk Factors ; Sclerosis ; Vitamins

In the present study, we investigated the effect of Tetaus toxin (TeT) on cell proliferation and neuroblast differentiation using specific markers: 5-bromo-2-deoxyuridine (BrdU) as an exogenous marker for cell proliferation, Ki-67 as an endogenous marker for cell proliferation and doublecortin (DCX) as a marker for neuroblasts in the mouse hippocampal dentate gyrus (DG) after TeT treatment. Mice were intraperitoneally administered 2.5 and 10 ng/kg TeT and sacrificed 15 days after the treatment. In both the TeT-treated groups, no neuronal death occurred in any layers of the DG using neuronal nuclei (NeuN, a neuron nuclei maker) and Fluoro-Jade B (F-J B, a high-affinity fluorescent marker for the localization of neuronal degeneration). In addition, no significant change in glial activation in both the 2.5 and 10 ng/kg TeT-treated-groups was found by GFAP (a marker for astrocytes) and Iba-1 (a marker for microglia) immunohistochemistry. However, in the 2.5 ng/kg TeT-treated-group, the mean number of BrdU, Ki-67 and DCX immunoreactive cells, respectively, were apparently decreased compared to the control group, and the mean number of each in the 10 ng/kg TeT-treated-group was much more decreased. In addition, processes of DCX-immunoreactive cells, which projected into the molecular layer, were short compared to those in the control group. In brief, our present results show that low dosage (10 ng/kg) TeT treatment apparently decreased cell proliferation and neuroblast differentiation in the mouse hippocampal DG without distinct gliosis as well as any loss of adult neurons.
Adult ; Animals ; Bromodeoxyuridine ; Cell Proliferation ; Dentate Gyrus ; Exotoxins ; Fluoresceins ; Gliosis ; Humans ; Immunohistochemistry ; Mice ; Neurogenesis ; Neurons ; Tetanus ; Tetanus Toxin