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Your search keyword '"Cha, In-Ho"' showing total 13 results
Start Over Author "Cha, In-Ho" Journal journal of biological chemistry
13 results on '"Cha, In-Ho"'

1. Ephrin receptor A10 monoclonal antibodies and the derived chimeric antigen receptor T cells exert an antitumor response in mouse models of triple-negative breast cancer

Author

Cha, Jong-Ho, Chan, Li-Chuan, Wang, Ying-Nai, Chu, Yu-Yi, Wang, Chie-Hong, Lee, Heng-Huan, Xia, Weiya, Shyu, Woei-Cherng, Liu, Shih-Ping, Yao, Jun, Chang, Chiung-Wen, Cheng, Fan-Ru, Liu, Jielin, Lim, Seung-Oe, Hsu, Jennifer L., Yang, Wen-Hao, Hortobagyi, Gabriel N., Lin, Chunru, Yang, Liuqing, Yu, Dihua, Jeng, Long-Bin, and Hung, Mien-Chie

Published
2022
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12. Catalytic properties of the cloned amylase from Bacillus licheniformis

Author

Jung-Ryul Kim, In-Cheol Kim, Cha Jae-Ho, Kwan-Hwa Park, Tae-Kyou Cheong, Byung-Cheol Seo, Dae Sil Lee, So-Young Jang, and Yang Do Choi

Subjects
biology, EcoRI, Pullulan, Cell Biology, Maltose, biology.organism_classification, Biochemistry, PANOSE, chemistry.chemical_compound, chemistry, Cyclomaltodextrinase, Maltotriose, biology.protein, Amylase, Bacillus licheniformis, Molecular Biology
Abstract

A gene encoding a new amylolytic enzyme of Bacillus licheniformis (BLMA) has been cloned, and we characterized the enzyme expressed in Escherichia coli. The genomic DNA of B. licheniformis was double-digested with EcoRI and BamHI and ligated the pBR322. The transformed E. coli was selected by its amylolytic activity, which carries the recombinant plasmid pIJ322 containing a 3.5-kilobase fragment of B. licheniformis DNA. The purified enzyme encoded by pIJ322 was capable of hydrolyzing pullulan and cyclodextrin as well as starch. It was active over a pH range of 6-8 and its optimum temperature was 50 degrees C. The molecular weight of the enzyme was 64,000, and the isoelectric point was 5.4. It degraded soluble starch by cleaving maltose units preferentially but did not attack alpha-1,6-linkage. The enzyme also hydrolyzed pullulan to panose units exclusively. In the presence of glucose, however, it transferred the panosyl moiety to glucose with the formation of alpha-1,6-linkage. The specificity of transferring activity is evident from the result of the maltosyl-transferring reaction which produces isopanose from maltotriose and glucose. The molecular structure of the enzyme deduced from the nucleotide sequence of the clone maintains limited similarity in the conserved regions to the other amylolytic enzymes.

Published
1992
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13. Sp1 Is Up-regulated in Cellular and Transgenic Models of Huntington Disease, and Its Reduction Is Neuroprotective.

Author

Zhihua Qiu, Norflus, Fran, Singh, Bhupinder, Swindell, Mary K., Buzescu, Rodica, Bejarano, Michelle, Chopra, Raman, Zucker, Birgit, Benn, Caroline L., Dirocco, Derek P., Cha, Jang-Ho J., Ferrante, Robert J., and Hersch, Steven M.

Subjects
*TRANSCRIPTION factors, *HUNTINGTON disease, *PROTEINS, *CELL death, *TRANSGENIC mice
Abstract

Interactions between mutant huntingtin (Htt) and a variety of transcription factors including specificity proteins (Sp) have been suggested as a central mechanism in Huntington disease (HD). However, the transcriptional activity induced by Htt in neurons that triggers neuronal death has yet to be fully elucidated. In the current study, we characterized the relationship of Sp1 to Htt protein aggregation and neuronal cell death. We found increased levels of Sp1 in neuronal-like PC12 cells expressing mutant Htt, primary striatal neurons, and brain tissue of HD transgenic mice. Sp1 levels were also elevated when 3-nitropropionate (3-NP) was used to induce cell death in PC12 cells. To assess the effects of knocking down Sp1 in HD pathology, we used Sp1 siRNA, a heterozygous Sp1 knock-out mouse, and mithramycin A, a DNA-intercalating agent that inhibits Sp1 function. The three approaches consistently yielded reduced levels of Sp1 which ameliorated toxicity caused by either mutant Htt or 3-NP. In addition, when HD mice were crossed with Sp1 heterozygous knock-out mice, the resulting offspring did not experience the loss of dopamine D2 receptor mRNA characteristic of HD mice, and survived longer than their HD counterparts. Our data suggest that enhancement of transcription factor Sp1 contributes to the pathology of HD and demonstrates that its suppression is beneficial. [ABSTRACT FROM AUTHOR]

Published
2006
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