Spatial and temporal analysis of filling flow propagation by color M-mode Doppler echocardiography was free of pseudonormalization and correlated well with the invasive variables of left ventricular relaxation.
The purpose of this study is to assess the association between type 2 diabetes and bone mineral density. This study included 145 Japanese patients (64 men and 81 women) with type 2 diabetes and 95 non-diabetic control subjects (41 men and 54 women) of similar age. We measured bone mineral density (BMD) at the sites with different cortical/cancellous bone ratio (lumbar spine, femoral neck, and distal radius) using dual-energy X-ray absorptiometry. BMD and Z score at the distal radius were significantly lower in type 2 diabetic patients than those in control subjects, and in type 2 diabetic patients, the Z score at the distal radius was lower than that at their own lumbar spine and femoral neck. In type 2 diabetic patients, negative correlation between BMD and the mean HbA1c during the previous 2 years was found significantly at the distal radius in both genders and at the femoral neck in women. These results indicate the selective cortical bone loss in type 2 diabetes and suggest the importance of also determining BMD at the radius and keeping good metabolic control to prevent bone loss in type 2 diabetic patients.
The ability of apolipoprotein E (apoE) to bind to cell-surface glycosaminoglycans (GAG) is important for lipoprotein remnant catabolism. Using surface plasmon resonance, we previously showed that the binding of apoE to heparin is a two-step process; the initial binding involves fast electrostatic interaction, followed by a slower hydrophobic interaction. Here we examined the contributions of the N-and C-terminal domains to each step of the binding of apoE isoforms to heparan sulfate (HS) and dermatan sulfate (DS). ApoE3 bound to less sulfated HS and DS with a decreased favorable free energy of binding in the first step compared to heparin, indicating that the degree of sulfation has a major effect on the electrostatic interaction of GAG with apoE. Mutation of a key Lys residue in the N-terminal heparin binding site of apoE significantly affected this electrostatic interaction. Progressive truncation of the C-terminal α-helical regions which favors the monomeric form of apoE3 greatly reduced the binding ability of apoE3 to HS, with much reduced favorable free energy of binding of the first step, suggesting that the C-terminal domain contributes to the GAG binding of apoE by the oligomerization effect. Supporting this, dimerization of the apoE3 N-terminal fragment via disulfide linkage restored the electrostatic interaction of apoE with HS. Significantly, apoE4 showed much greater binding to HS and DS than apoE2 or apoE3 in both lipidfree and lipidated states, perhaps resulting from enhanced electrostatic interaction through the Nterminal domain. This isoform difference in GAG binding of apoE may be physiologically significant such as in the retention of apoE-containing lipoproteins in the arterial wall.Heparan sulfate proteoglycan (HSPG) is a common constituent of cell surfaces and the extracellular matrix, and is involved in a wide range of biological functions (1). Normal uptake and catabolism of atherogenic lipoproteins is mediated by the interaction of lipoproteins with
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