Pathogenesis of Metabolic Syndrome from "Qi of five Internal Organs" / 中国实验方剂学杂志

Metabolic syndrome (MS) is a group of syndromes caused by the disorder of metabolism of various substances in the body. The main clinical manifestations are dyslipidemia, central obesity, hypertension, abnormal glucose tolerance and insulin resistance. With the changes of diet structure and habits, the incidence rate of MS is increasing, and the patients are younger. It is an important factor in many diseases, such as diabetes, atherosclerosis, coronary heart disease, hyperlipidemia, cirrhosis and some cancers. MS has seriously affected people's lives and health. Central obesity and insulin resistance are recognized as important pathogenic factors. At present, the pathogenesis of MS and its components has not been fully understood. The clinical manifestations of metabolic syndrome are complex and diverse. Traditional Chinese medicine (TCM) believes that the occurrence of metabolic syndrome is related to such factors as proper diet, emotional disorders, excessive escape and little movement, old age and physical deficiency. TCM scholars have studied the pathogenesis of MS in such pathological factors as phlegm and blood stasis, such visceral functions as liver, spleen and kidney, roles of Qi and blood, and emotional factors. As the basic substance of organism, Qi is closely related to the process of metabolism. The occurrence of MS is closely related to the rise and fall of Qi moving to and from the body as well as the abnormal gasification function of the transformation of Qi. Qi is derived from the five internal organs, which are respectively called Heart Qi, liver Qi, spleen Qi, lung Qi and kidney Qi. The "Qi of the five internal organs" is involved in the whole process of the generation, transportation and excretion of the essence of the body. Based on the "Qi of five internal organs", this paper discusses the pathogenesis of MS with phlegm, blood stasis and water drink as pathological factors.

Combined immunoprophylaxis induces changes in anti-hepatitis B surface protein titer in infants born to mothers with positivity for hepatitis B surface antigen / 中华肝脏病杂志

<p><b>OBJECTIVE</b>To conduct a prospective randomized controlled trial of infants born to hepatitis B virus (HBV) surface antigen (HBsAg)-positive mothers in order to investigate the dynamic changes in the titer of anti-HBV surface protein (HBS) induced by treatment with combined immunoprophylaxis (200 IU hepatitis B immunoglobulin (HBIG) and 5 or 10 mug yeast recombinant hepatitis B vaccine), to compare the protective effect of 5 and 10 mug hepatitis B vaccine, and to provide an immunization strategy, monitoring mode and booster immunization schedule for the high-risk group.</p><p><b>METHODS</b>Two-hundred-and-sixty-nine infants born to HBsAg positive mothers were given combined immunoprophylaxis at birth, and the venous blood samples (at birth, and 1, 7 and 12 months) were tested for HBV DNA load, and HBsAg and anti-HBS titers.</p><p><b>RESULTS</b>The overall 1-year protective rate of combined immunoprophylaxis was 95.9%. There was no significant difference between the infectious rates of infants given the 5 mug or the 10 mug hepatitis B vaccine (x2 = 0.876, P = 0.377). The geometric mean titers (GMTs) of anti-HBS were 144.1 mIU/ml at 1-month old and 564.9 mIU/ml at the age of 7 months old (the highest point), but declined to 397.6 mIU/ml at the age of 12 months old. The rate of infants with anti-HBS titer less than 100 mIU/ml was 20.9%, and that of less than 10 mIU/ml was 7.4% at 7-month-old; the rate of infants with anti-HBS titer less than 100 mIU/ml increased to 30.2% and that of less than 10 mIU/ml increased to 15.9% at 12-month-old. At 7-month-old, the GMT of the 10 mug vaccine group was higher than that of the 5 mug vaccine group (675.3 mIU/ml vs. 25.0 mIU/ml, P = 0.001) and the rate of infants with anti-HBS titer less than 10 mIU/ml was significantly lower in the 10 mug vaccine group (2.3% vs. 12.6%, P = 0.002); at 12-month-old, the rate of infants with anti-HBS titer less than 100 mIU/ml was also significantly lower in the 10 mug group (20.6% vs. 40.2%, P = 0.001).</p><p><b>CONCLUSION</b>Combined immunoprophylaxis is therapeutically efficacious for treating infants born to HBsAg positive mothers. Monitoring these infants' anti-HBs titer will help to identify non- or low-responders in a timely manner. The high-dose hepatitis B vaccine is preferable to the low-dose, and should be considered for use in immunization strategies for these infants.</p>

Detection of genetic defect within ABCA3 from newborns with respiratory distress syndrome / 中华儿科杂志

<p><b>OBJECTIVE</b>To detect possible relationship between genetic defect within the gene encoding member A3 of the ATP Binding Cassette family (ABCA3) and neonatal respiratory distress syndrome (NRDS), thus to understand the genetic mechanisms of NRDS in Han ethnic group.</p><p><b>METHOD</b>The clinical data of 11 cases with NRDS hospitalized in neonatal intensive care unit was investigated. Blood samples were collected from 11 cases with NRDS and 97 unassociated normal individuals. Polymerase chain reaction (PCR) and DNA direct sequencing were performed to screen all exons and their flanking introns of ABCA3 gene for mutation analysis in 11 cases with NRDS. If a new missense variation was identified, single strand conformation polymorphism analysis was performed in 97 healthy controls. Lung tissue sample from a case who died 12 hours after birth was examined with light microscopy and electron microscopy.</p><p><b>RESULT</b>Three missense genetic variants in exons, which include c. 2169 G > A (p.M723I), c. 1010 T > G (p.V337G), c. 4972 A > G (p.S1658G), one splice junction site variation (Exon 30 + 2 T/G), several unreported polymorphism sites [213 C > T(p.F71F), exon 21 + 34C/T] and reported polymorphism site (p.F353F) were identified on ABCA3 gene coding region in 11 case. The homozygous variation (c.2169G > A), which was in exon 17 and causes an M723I amino acid change, was found in the case who died 13 hours after birth, but not detected in 97 controls, indicating that this variation is indeed a mutation and not a polymorphism. In the case carrying c.2169G > A, ultrastructural examination of the alveolar type II cells with electron microscopy demonstrated abnormally small and dense lamellar body with eccentrically distributed electron dense substance.</p><p><b>CONCLUSION</b>Genetic variants within ABCA3 may be the genetic cause of or a contributor to some unexplained refractory NRDS. Identification of ABCA3 genetic variant in NRDS infants is important to establish appropriate management and evaluation of treatment options, as well as to offer genetic counseling and prenatal diagnosis.</p>

Site-directed mutagenesis and protein expression of KCNQ2 gene associated with neonatal convulsions / 中国当代儿科杂志

<p><b>OBJECTIVE</b>To study the protocol of construction of a KCNQ2-c.812G>T mutant and it's eukaryotic expression vector, the c.812G>T (p.G271V) mutation which was detected in a Chinese pedigree of benign familial infantile convulsions, and to examine the expression of mutant protein in human embyonic kidney (HEK) 293 cells.</p><p><b>METHODS</b>A KCNQ2 mutation c.812G>T was engineered on KCNQ2 cDNAs cloned into pcDNA3.0 by sequence overlap extension PCR and restriction enzymes. HEK293 cells were co-transfected with pRK5-GFP and KCNQ2 plasmid (the wild type or mutant) using lipofectamine and then subjected to confocal microscopy. The transfected cells were immunostained to visualize the intracellular expression of the mutant molecules.</p><p><b>RESULTS</b>Direct sequence analysis revealed a G to T transition at position 812. The c.812G>T mutation was correctly combined to eukaryotic expressive vector pcDNA3.0 and expressed in HEK293 cells. Immunostaining of transfected cells showed the expression of both the wild type and mutant molecules on the plasma membrane, which suggested that the c.812G>T mutation at the pore forming region of KCNQ2 channel did not impair normal protein expression in HEK293 cells.</p><p><b>CONCLUSIONS</b>Successful construction of mutant KCNQ2 eukaryotic expression vector and expression of KCNQ2 protein in HEK293 cells provide a basis for further study on the functional effects of convulsion-causing KCNQ2 mutations and for understanding the molecular pathogenesis of epilepsy.</p>