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Transgenic Chicken, Mice, Cattle, and Pig Embryos by Somatic Cell Nuclear Transfer into Pig Oocytes
Gupta, Mukesh Kumar,Das, Ziban Chandra,Heo, Young Tae,Joo, Jin Young,Chung, Hak-Jae,Song, Hyuk,Kim, Jae-Hwan,Kim, Nam-Hyung,Lee, Hoon Taek,Ko, Dae Hwan,Uhm, Sang Jun Mary Ann Liebert 2013 Cellular reprogramming Vol.15 No.4
Gupta, Mukesh Kumar,Singh, Raj Pal The Polymer Society of Korea 2009 Macromolecular Research Vol.17 No.4
The present study firstly describes the synthesis of novel, thermo-latent initiators based on xanthenyl phosphonium salts with different counter anions and phosphine moieties and secondly examines their efficiency in the bulk polymerization of glycidyl phenyl ether(GPE). The polymerization was performed with phosphonium salt initiators($I_{SbF6}$, $I_{PF6}$, $I_{AsF6}$ and $I_{BF4}$) at ambient temperature to $200^{\circ}C$ for 1 h. The order of initiator activity was $I_{SbF6}>I_{PF6}>I_{AsF6}>I_{BF4}$. To examine the effect of the phosphine moiety on the initiator activity, polymerization was carried out with $I_{SbF6}(Ph_{3}P)$ and $II_{SbF6}(Bu_{3}P)$ at ambient temperature to $170^{\circ}C$ for 1 h. The order of reactivity was $I_{SbF6}>II_{SbF6}$. In general, the conversion percentage increased with increasing polymerization temperature. The thermal stability of these salts was measured by thermo gravimetric analysis(TGA). The solubility of phosphonium salts in various organic solvents and epoxy monomers was also investigated.
Embryo quality and production efficiency of porcine parthenotes is improved by phytohemagglutinin
Gupta, Mukesh Kumar,Uhm, Sang Jun,Han, Dong Wook,Lee, Hoon Taek Wiley Subscription Services, Inc., A Wiley Company 2007 Molecular reproduction and development Vol.74 No.4
<P>In vitro production of porcine embryos has become routine in most laboratories but the yield and quality of the resultant blastocysts remain suboptimal. Phytohemagglutinin (PHA) is an N-acetylgalactosamine/galactose sugar-specific lectin with a wide variety of biological activities including mitogenesis, mediation of cell recognition, and agglutination of cells. This study was therefore, designed to investigate the effect of PHA on the preimplantation embryo development and quality of in vitro produced porcine parthenotes. Parthenogenetic presumptive diploid zygotes were produced in vitro by electrical activation and cultured in the absence or presence of PHA at different concentrations (0, 5, 10, 15, 20 µg/ml). There were no significant differences in the cleavage rate of porcine parthenotes in control and treatment groups at all tested concentrations of PHA (P < 0.05). However, supplementation of PHA at the concentration of 15 µg/ml significantly improved the blastocyst rate (68.9 ± 1.5% vs. 43.1 ± 4.1%), hatching rate (25.8 ± 3.1% vs. 8.9 ± 2.0%), and total nuclei number (95.5 ± 9.3 vs. 63.4 ± 4.3) when compared to control group (P > 0.05). TUNEL labeling revealed that blastocysts in PHA group were less predisposed to biochemical apoptosis than in control group while total apoptosis and nuclear fragmentation remained unaltered. Real-time reverse transcription-polymerase chain reaction (RT-PCR) analysis further revealed that PHA decreased the expression ratio of BAX/BCL-XL and enhanced the relative abundance of IGF2 transcripts. Therefore, our study suggests that PHA improves the blastocyst yield and quality by enhancing blastocyst expansion, hatching, and total cell number and decreasing the apoptosis by positively modulating the expression of embryo survival related genes. Mol. Reprod. Dev. 74: 435–444, 2007. © 2006 Wiley-Liss, Inc.</P>
Combining selected reaction monitoring with discovery proteomics in limited biological samples
Gupta, Mukesh Kumar,Jung, Jin Woo,Uhm, Sang Jun,Lee, Hookeun,Lee, Hoon Taek,Kim, Kwang Pyo WILEY-VCH Verlag 2009 Proteomics Vol.9 No.21
<P>Simultaneous quantification of multiple proteins by selected reaction monitoring (SRM) has several applications in cell signaling studies including embryo proteomics. However, concerns have recently been raised over the specificity of SRM assays due to possible ion redundancy and/or sequence similarity of selected peptide with multiple non-related proteins. In this Viewpoint article, we discuss some simple measures that can increase our confidence in the accuracy of SRM scans used in proteomic experiments. At least in embryonic samples from porcine species, these measures were found to be useful in validating MS-identified differentially expressed proteins. Among the nine proteins analyzed by SRM assay, all the proteins that were found to be up- or down-regulated in MS experiment were also faithfully up- or down-regulated in SRM assay.</P>