• Journal of Yeungnam Medical Science
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• v.16 no.2
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• pp.309-317
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• 1999

Background: Left ventricular diastolic filling is an important determinant for maintenance of cardiac output during hemodialysis. Few investigators have studied the influence of hemodialysis on diastolic function. To evaluate the change of left ventricular systolic and diastolic function. we performed M-mode and Doppler echocardiographic studies before and after hemodialysis. Methods: The study population consisted of 30 patients(15 patients were male, mean age $45{\pm}10$ years) with CRF on maintenance hemodialysis. They have normal left ventricular systolic function(Fractional shortening>30%) and no evidence of valvular heart disease or regional wall motion abnormalities. The ejection fraction (EF) was measured using M-mode echocardiography and Doppler indices such as peak E velocity, peak A velocity, isovolumetric relaxation time(IVRT), deceleration time(DT). and left ventricular ejection time(LVET) obtained from Doppler echocardiography. The index of myocardial performance (IMP) was calculated from each of the Doppler velocity indices. Results: The weight reduction after hemodialysis was $2.1{\pm}1.0kg$(p<0.0001), After hemodialysis, there was some decrease in blood pressure(p<0.05), but no significant change in heart rate, EF and fractional shortening, mean VCF, peak A velocity, and DT. And significant reduction in peak E velocity, E/A ratio(p<0.0001. p<0.001), and significant increase in IVRT and IMP(p<0.05, p<0.0001) were noted. Conclusion: In conclusion, preload reduction is the main mechanism that accounts for changes in Doppler diastolic indices after hemodialysis. And an increased IMP suggests that diastolic function may be aggravated after hemodialysis, and that implies impaired left ventricular filling and disturbed left ventricular compliance.

• Journal of Life Science
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• v.24 no.4
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• pp.343-351
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• 2014

Phosphoinositide 3-kinase (PI3K) plays a central role in cell signaling and leads to cell proliferation, survival, motility, exocytosis, and cytoskeletal rearrangements, as well as specialized cell responses, superoxide production, and cardiac myocyte growth. PI3K is divided into three classes; type I PI3K is preferentially expressed in leukocytes and activated by ${\beta}{\gamma}$ subunits of heterotrimeric G-proteins. In this study, the cDNAs encoding the $PI3K{\gamma}$ gene were isolated from a brain cDNA library constructed using the flounder (Paralichthys olivaceus). The sequence of the isolated $PI3K{\gamma}$ was 1341 bp, encoding 447 amino acids. The nucleotide sequence of the $PI3K{\gamma}$ gene was analyzed with that of other species, including Oreochromis niloticus and Danio rerio, and it turned out to be well conserved during evolution. The $PI3K{\gamma}$ gene was subcloned into the expression vector pET-44a(+), and expressed in the E. coli BL21 (DE3) codon plus cell. The resulting protein was expressed as a fusion protein of approximately 49 kDa containing a C-terminal six-histidine extension that was derived from the expression vector. The expressed protein was purified to homogeneity by His-tag affinity chromatography and showed enzymatic activity corresponding to $PI3K{\gamma}$. The binding of wortmannin to $PI3K{\gamma}$, as detected by anti-wortmannin antisera, closely followed the inhibition of the kinase activities. The results obtained from this study will provide a wider base of knowledge on the primary structure and characterization of the $PI3K{\gamma}$ at the molecular level.