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Z Cui

Publications and source records attributed to Z Cui.

104 records · Page 6Linked to original sources

Expression of a G protein subunit, alpha i-1, in Balb/c 3T3 cells leads to agonist-specific changes in growth regulation.

Cellular receptors for many hormones, neurotransmitters, and growth factors are coupled to intracellular effector enzymes or ion channels through a set of heterotrimeric G proteins. In order to determine whether isoforms of G protein alpha subunits contribute differentially to mitogenic responses, we introduced an alpha subunit isoform, alpha i-1, into Balb/c 3T3 cells that normally lack this subtype. Balb/c 3T3 cells transfected with a plasmid containing cDNA encoding alpha i-1 expressed the alpha i-1 protein as judged both by the appearance of immunoreactive alpha i-1 protein on Western blots and by two-dimensional analysis of the proteins [32P]ADP-ribosylated by pertussis toxin. The amount of alpha i-1 expressed is less than the amount of alpha subunits endogenously present in these cells. Expression of alpha i-1 in the transfected cells slightly blunts stimulation of adenylylcyclase by GTP, guanosine 5'-3-O-(thio)triphosphate, or forskolin, but has no major effect on the ability of thrombin to inhibit the enzyme. In contrast, the expression of alpha i-1 has significant effects on cell growth and on the mitogenic response to thrombin. The alpha i-1-transfected cells have a doubling time that is twice as long as control cells transfected with the same plasmid without a cDNA insert. Despite their slower growth, thymidine incorporation in response to thrombin is greater in transfected than in control cells. Thrombin-stimulated DNA synthesis is sensitive to inhibition by pertussis toxin and is 5-fold more sensitive to inhibition by pertussis toxin in transfected cells than in control cells. The changes are receptor-specific since the mitogenic response to platelet-derived growth factor is indistinguishable between control and transfected cells. These studies suggest that the alpha i subunit composition of the cell may have profound effects on its growth and its response to stimulation through a specific cell surface receptor.

3T3 Cells↗

[Androgen-like and anabolic action of Antheraea pernyi Guerin-Meneville Pas].

It has been found that the ethyl acetate extract isolated from Antheraea pernyi Pas is able to increase the weight of prostate-semina and levator ani muscle-bulbocavarnosus muscle of castrated mice. In addition, the extract also accelerates the growth of younger male mice and enhances the contents of RNA, DNA and protein in the liver tissue of mice. It has been determined that beta-ecdysone is one of the effective constituents for the androgen-like and anabolic action.

Animals↗

A single nucleotide substitution at the rib2 locus of the yeast mitochondrial gene for 21S rRNA confers resistance to erythromycin and cold-sensitive ribosome assembly.

We have studied a mutation (cs23) in the mitochondrial gene for 21S rRNA that affects the peptidyl transferase center of the ribosome and conditionally blocks the assembly of the 54S ribosomal subunit. Strains carrying this mutation are resistant to erythromycin and cold-sensitive for growth on nonfermentable carbon sources (Singh et al. 1978) Mitochondria isolated from mutant cells grown on glucose at 20 degrees C, the nonpermissive temperature, were depleted of the 54S subunit and instead contained a novel 45S ribosomal particle. After mutant cells were shifted from 20 degrees C to 32 degrees C, 54S subunits were assembled, apparently from the 45S particles and pre-existing ribosomal proteins. DNA sequencing revealed that the mutant phenotype is a consequence of a C to A transversion at position 3993 of the 21S rRNA gene. Previously, C to U and C to G mutations have been identified at the same position in the 21S rRNA sequence. This position corresponds to C-2611 in the E. coli 23S RNA, a nucleotide that appears to be conserved in the large rRNA of all erythromycin-sensitive ribosomes.

Base Sequence↗

Serologic differences among nondefective reticuloendotheliosis viruses.

Antigenic relationships among 26 isolates of reticuloendotheliosis virus (REV) obtained from several avian species were compared by cross neutralization tests with polyclonal chicken sera and by immunofluorescent assays with monoclonal antibodies to REV strain T. The isolates were all strongly related by neutralization assays and thus probably constitute a single serotype. However, 3 antigenic subtypes were suggested by minor but distinct differences in neutralization titers. The validity of these 3 subtype designations was confirmed by differential reactivity of viral isolates to selected monoclonal antibodies. Subtype-associated differences in serum antibody titers were noted following the inoculation of chickens with the REV isolates.

Animals↗

Diagnosis of an accessory portal vein and its clinical implications for portosystemic shunts.

PURPOSE: To present a peculiar anatomic portal veins variant and evaluate its clinical implications. METHODS: Among 118 consecutive patients undergoing transjugular intrahepatic portosystemic shunting (TIPS), six male patients were found to have an accessory portal vein, which was seen during direct portography.R ESULTS: In all six patients, portograms showed an accessory small-caliber vein parallel to the trunk of the main portal vein ending in the right lobe of the liver. Two of the six accessory portal veins drained blood from coronary veins, precluding access to coronary vein embolization during TIPS. CONCLUSION: An accessory portal vein is a rare anatomical variation with clinical significance for both surgical shunt placement and TIPS, as well as for transportal embolization of coronary veins.

Humans↗

5'-sulfhydryl-modified RNA: initiator synthesis, in vitro transcription, and enzymatic incorporation.

The detailed syntheses of the sulfhydryl-modified guanosine monophosphates 5'-deoxy-5'-thioguanosine-5'-monophosphorothioate (GSMP), O-[omega-sulfhydryl-tetra(ethylene glycol)]-O-(5'-guanosine) monophosphate (5'-HS-PEG4-GMP), and O-[omega-sulfhydryl-di(ethylene glycol)]-O-(5'-guanosine) monophosphate (5'-HS-PEG2-GMP) are reported. Transcription reactions employing GSMP, 5'-HS-PEG4-GMP, or 5'-HS-PEG2-GMP as the initiator nucleotide for T7 RNA polymerase introduce a thiol group at the 5'-end of RNA. The efficiency of thiol incorporation at the 5'-terminus of modified RNA compounds was assayed with three different thiol-reactive biotinylated reagents followed by streptavidin gel-shift methods. The transcription efficiency with various ratios of GTP to 5'-HS-PEG2-GMP was explored by reaction with a sulfhydryl-reactive maleimide-conjugated protein. This is an efficient method to incorporate enzymatically a thiol group into the 5'-end of RNA.

Biotinylation↗

Construction and characterization of a H19 epitope point mutant of MDV CVI988/Rispens strain.

A recombinant virus, CVI/rpp38, was developed from the Marek's disease virus (MDV) CVI988/Rispens vaccine strain. This recombinant was obtained by transfection of CVI988/Rispens-infected chick embryo fibroblasts (CEFs) with plasmid pHA25 DNA containing pp38 gene from GA strain of MDV. Monoclonal antibody (MAb) H19 which reacts with pp38 from GA but not with that from CVI988 was used to screen for recombinant viruses in transfected cell culture plates by immunofluorescent assay (IFA). A positive plaque was isolated, propagated, and purified from cell-free virus particles after sonication of infected CEFs. The mutant CVI/rpp38 was not only reactive with MAb H19 in IFA but also in immunoprecipitation. A 38 kDa protein was immunoprecipitated from the CVI/rpp38 mutant virus but not from parental CVI988 virus. DNA sequence of the mutant virus showed a substitution of G at position 320 by a resulting in a change of an amino acid residue from arginine to glutamine. Comparison of nucleotide sequence of pp38 from strains GA, Md5 and Md11/75c/R2 and CVI988 revealed change to glutamine in this position. The result of this study provides a direct evidence for the location of the identified H19 epitope in pp38. This mutant is potentially useful to further explore the biological function of pp38 and its H19 epitope.

Amino Acid Sequence↗

Development and characterization of monoclonal antibodies to subgroup J avian leukosis virus.

In an attempt to develop a specific diagnostic test for avian leukosis virus (ALV) subgroup J (ALV-J) strain Hc1, four monoclonal antibodies (MAbs), JE9, G2, 145, and J47, were generated that are specific for ALV-J envelope glycoprotein, gp85. Polymerase chain reaction (PCR) was used to amplify genomic pro-viral DNA of Avian Disease and Oncology Laboratory (ADOL)-Hc1 and ADOL-4817 envelope genes. Both open reading frames encoding glycoproteins gp85 and gp37 were cloned into baculoviruses. Abundant expression of gp85 and gp37 was detected in the recombinant viruses with specific antibody to Hc1 strain of the ALV-J. The expressed proteins were used for immunization of mice to produce hybridoma cell lines secreting MAbs specific to ALV-J envelope protein. A panel of MAbs was generated by fusing NS1 myeloma cells and spleen cells from mice immunized with the recombinant baculoviruses. With the use of an immunofluorescence assay, three MAbs (JE9, G2, 145) reacted with ALV-J but not with subgroups A, B, C, D, or E of ALV. MAb J47 reacted with all exogenous subgroups of ALV including A, B, C, D, and J but not with endogenous subgroup E viruses. Western blot analysis was performed with all four MAbs against recombinant baculovirus and Hc1-infected chicken embryo fibroblast (CEF) lysates. A major band with a molecular weight about 90 kD corresponding to the size of ALV-J envelope was consistently obtained. With these MAbs, we detected the Hc1 antigen in CEFs infected with several ALV-J viruses isolated in the United States and also in tissue sections from chickens infected with Hc1 strain of ALV-J. These MAbs will be useful reagents for the diagnosis of ALV-J infection because they recognize a common antigenic epitope in six isolates tested thus far.

Animals↗

Phosphatidylethanolamine methylation and hepatoma cell growth.

Phosphatidylethanolamine is converted to phosphatidylcholine in hepatocytes via the enzyme phosphatidylethanolamine N-methyltransferase (PEMT). An isoform, PEMT2 has been cloned, expressed and localized to a mitochondria-associated membrane in rat liver. Expression of PEMT2 caused a decreased rate of cell division of cultured rat hepatoma cells. Mechanistic studies suggest that the slower growth of transfected hepatoma cells may be due to down regulation of CTP: phosphocholine cytidylyltransferase and the CDP-choline pathway for phosphatidylcholine biosynthesis. A role for PEMT2 in the regulation of hepatocyte cell division is also indicated by PEMT2 down-regulation in regenerating rat liver.

Animals↗

Transjugular intrahepatic portosystemic shunts: midterm results in 28 patients.

This paper reports the clinical and procedural results of 28 consecutive TIPS procedures in 25 males and three females with a mean age of 48 years. All patients had cirrhosis with portal hypertension and varices. Twenty-two patients had recurrent bleeding. Shunts were completed in 26 of 28 patients, and no death was associated with the procedure. Portal vein pressure was reduced from 3.98 +/- 0.24 KPa before shunting to 2.40 +/- 0.16 KPa after shunting. Doppler US revealed that the maximum blood flow velocity in the main portal vein increased from 14.0 +/- 4.5 cm/sec to 48.0 +/- 16.5 cm/sec. Shunt patency was determined by color Doppler US in 20 patients. Shunt stenosis was found in five patients and occlusion in one, and these findings were confirmed by angiography. Ascites disappeared in six of eight cases, and varices disappeared completely in 11 patients and abated greatly in 12 patients two months after TIPS. Rebleeding occurred in three cases (occlusion, 1; stenosis, 2) during a mean follow-up time of 6.5 months. One of these cases was successfully redilated. The initial results suggest that TIPS is a safe and effective method of portal decompression and that the key to portal vein puncture is to understand the three-dimensional relationship between the hepatic and portal veins.

Adult↗