Objective: To describe the prevalence of depressive and/or anxiety symptom and disorder in patients with coronary heart disease(CHD) in the general hospitals.Methods: A hospital-based cross-sectional study was conducted in four main cities in China in 2004.359 eligible subjects with CHD were recruited from the outpatient or inpatient departments within six months.Face-to-face interviews were used in data collection together with the self-completed HAD scale for depressive and/or anxiety symptom screening.Subjects getting a HAD score of 9 and above were further assessed for depressive and/or anxiety disorders with HAMA scales and HAMD scales by the licensed psychologists or psychiatrists.Results: The prevalence of depressive symptoms,anxiety symptoms,depressive and anxiety symptoms,and total depressive and/or anxiety symptoms were 19.8%,16.7%,13.6% and 22.8% respectively in patients with CHD.Less than 4% of the subjects had been diagnosed or treated for the depressive or anxiety disorders prior to the investigation.In inpatients,the diagnosis and treatment rate was low to less than 1% during the current admission.Conclusion: It was noticeable to health care providers and health policy makers that there was high prevalence of depressive and/or anxiety symptoms and depressive and/or anxiety disorders,and low percentages of previous diagnosis and treatment in patients with CHD in general hospitals.

HIV-1 integrase enzyme is a 32kDa protein encoded by HIV pol gene. It is responsible for integration of viral cDNA into host chromosomal DNA, which is indispensable for HIV replication.Since there was no functional equivalent for this enzyme in human cells, inhibition of integrase will bring little side effect to human body. Thus HIV integrase has become an attractive and rational target for therapy of AIDS after reverse transcriptase and protease.The Recent research on HIV-1integrase structure,inhibitors and new therapeutic method target at HIV integrase was reviewed.

Molecularly imprinted polymers (MIPs) with high selectivity to tilmicosin (TIM) were prepared using tylosin(TYL) as dummy template, methacrylic acid(MAA) as monomer, ethylene glycol dimethacrylate (EGDMA) as cross-linker.The effects of 4 porogens including dimethyl formamide, methanol, acetone, and chloroform on the recognition capability of MIPs were investigated.Orthogonal test was used to optimize the preparation of MIPs, and the optimal composition was as follows; 1.0 mmol TYL, 8.0 mmol MAA, 20.0 mmol EGDMA, 6.0 mL chloroform, 20.0 mg azobisisobutyronitrile.The solid phase extraction condi tions and characteristics of MIPs as adsorptive material for the selective extraction and enrichment of TIM were also studied.The recovery of TIM was above 90% when the following procedure was applied to MIPs cartridge: conditioning with methanol and water(pH 9.0), loading with acetonitrile, cleaning with methanol and chloroform respectively, and eluting with 3 mL methanol-ammonia(95:5, V/V).The recovery of TIM on non-imprinted polymers cartridge was only 32%.

Acupuncture Points ; Acupuncture Therapy ; Adult ; Female ; Hiccup ; therapy ; Humans ; Male ; Middle Aged

Amino Acid Sequence ; Animals ; Calcium Channel Blockers ; pharmacology ; Calcium Channels ; drug effects ; Humans ; Molecular Sequence Data ; Structure-Activity Relationship ; omega-Conotoxins ; chemistry ; pharmacology

Animals ; Cytoplasm ; metabolism ; Endoplasmic Reticulum, Rough ; metabolism ; Golgi Apparatus ; metabolism ; Humans ; Protein Transport ; Ricin ; chemistry ; pharmacokinetics ; therapeutic use

Objective To study the feasibility and safety of hand-assisted laparoscopic hepatectomy for huge left hepatoma.Methods Nine patients with huge left hepatoma underwent hand- assisted laparoscopic hepatectomy including hepatocellular carcinoma(4 cases),intrahepatic cholangioearcinoma(1 case),hepatic metastatic squamous carcinoma(1 case),hepatic cavernous hemangioma(2 cases),and hepatic spindle cell tumor(1 case).The mean age was 45.3 years.AFP was positive in 3 cases and CEA was positive in 1 case.The preoperative liver function was Child-Pugh A in all patients.The procedure included dissection of left hepatic ligaments and portal triad clamping with Pringle's maneuver and hepatectomy.Results The laparoscopic procedures were completed safely in all patients including 6 left lateral segmentectomies and 3 left hemihepatectomies.There was no conversion to laparotomy.Mean surgical time was 111.7 minutes.Mean blood loss was 97.8 ml.Portal triad clamping was used in 8 cases and mean clamping time was 13.4 minutes.Neither formidable bleeding nor gas embolism occurred.There were no serious postoperative complications such as postoperative bleeding or bile leak or liver failure.Liver function recovered within 7 to 10 days.Preoperatively positive AFP and CEA turned negative after operation.The mean postoperative hospital stay was 8.4 days.Four patients with HCC underwent postoperative prophylactic hepatic arterial chemoembolization within the first postoperative month. All patients were tumor-free as evaluated by postoperative follow-up of 4～11 months.Conclusions Hand-assisted laparoscopic hepatectomy for huge left hepatoma is feasible and safe in appropriately selected patients.

OBJECTIVETo clone and produce ribosome inactivating protein MAP30 from the seeds of Momordica charantia L(bitter melon), and to evaluate the biological activity of the recombinant protein.

METHODSThe DNA sequence encoding MAP30 was cloned from the fresh seeds of Momordica charantia by PCR, the target DNA fragments were sequenced after T-A cloning. The expression plasmid was constructed by inserting the MAP30 fragment into vector pET30a. MAP30 was expressed in E.coli by addition of IPTG into final concentration of 1.0 mmol/L. The recombinant MAP30 was identified by SDS-PAGE, and the biological activity of MAP30 protein was evaluated by using MTT assay in cancer cells and normal cells following fluid-phase endocytosis.

RESULTThe nucleotide and amino acid sequences of the cloned MAP30 were identical with those of reported MAP30. The solubility of recombinant protein was analyzed by SDS-PAGE, and the MAP30 was mainly produced in soluble form. The recombinant MAP30 showed a greater cytotoxicity to cancer cells than that to normal cells.

CONCLUSIONThe gene of MAP30 has been successfully cloned.The recombinant MAP30 protein expressed by E.coli is bioactive.

Cloning, Molecular ; Escherichia coli ; genetics ; metabolism ; Gene Expression ; Genetic Vectors ; Momordica charantia ; chemistry ; Recombinant Proteins ; biosynthesis ; genetics ; metabolism ; Ribosome Inactivating Proteins, Type 2 ; biosynthesis ; genetics ; metabolism ; Seeds ; chemistry ; Transformation, Bacterial

OBJECTIVETo clone luffin-a cDNA from the seeds of Luffa cylindrical, and to obtain bioactive recombinant luffin-a protein using the expression vector pET-44a (+) in E. coli.

METHODSThe cDNA sequence encoding luffin-a was cloned from the fresh seeds of Luffa cylindrical by RT-PCR. The target DNA fragments were sequenced after T-A cloning. The luffin-a expression plasmid was constructed by inserting the luffin-a cDNA fragment into vector pET-44a (+). Luffin-a was expressed in E. coli by addition of IPTG into final concentration 1.0 mmol/L. The recombinant luffin-a was identified by SDS-PAGE. The biological activity of luffin-a protein was evaluated by using the MTT assay in HepG2 cells following fluid-phase endocytosis.

RESULTSIn comparison with the reported luffin-a, the homology of nucleotide sequence of the cloned luffin-a gene was 99.73%, while their amino acid sequences were identical. The solubility of recombinant protein was analyzed by SDS-PAGE, and the luffin-a was mainly produced in inclusion bodies. The recombinant luffin-a, renatured by dialysis of the denatured products, showed a similar cytotoxicity to ricin A chain.

CONCLUSIONThe cDNA of luffin-a has been successfully cloned. The recombinant luffin-a protein expressed by E. coli is bioactive.

Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Luffa ; chemistry ; Molecular Sequence Data ; Plant Proteins ; biosynthesis ; genetics ; Polymerase Chain Reaction ; Ribosome Inactivating Proteins, Type 1 ; Seeds ; chemistry

OBJECTIVETo study the expression and purification of a fusion protein of ricin A chain (RTA) and green fluorescent protein (GFP).

METHODSThe DNA sequence encoding ricin A chain was inserted into pEGFPC1 first to make the template sequence of the fusion protein. The fusion gene was amplified from the plasmid pEGFP-RTA by PCR, and directly subcloned into T vector. The fusion gene then was cloned into expression vector pET-28a(+), and the sequence was confirmed by sequencing. Expression was induced by IPTG in E. coli BL21(DE3). The fusion protein was purified by metal chelated affinity chromatography. The cytotoxicity of fusion protein was analyzed by the MTT assay in HepG2 and Hela cells.

RESULTSThe fusion protein of ricin A chain and GFP could be produced in E. coli transformed with the expression plasmid of pET-28a(+)-GFP-RTA. The molecular weight of the recombinant protein was measured by SDS-PAGE. The fusion protein showed a green fluorescence and had a similar cytotoxicity of RTA.

CONCLUSIONA recombinant fusion protein of RTA and GFP expressed in E. coli is possessed of similar biological activity of individual GFP and RTA, which could be used in study of the intracellular trafficking and translocation of RTA.

Escherichia coli ; genetics ; metabolism ; Green Fluorescent Proteins ; genetics ; HeLa Cells ; Humans ; Luminescent Proteins ; genetics ; Recombinant Fusion Proteins ; biosynthesis ; genetics ; Ricin ; genetics