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RISS 인기검색어
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- 저자 : Ravid, Katya (검색결과 3 건)
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Kang, Taewook,Kim, Jae Ho,Hong, Ingie,Park, Nam Hyun,Park, Nanhyun,Heinsen, Helmut,Lee, Joo-Yong,Ravid, Rivka,Ferrer, Isidro,Yoo, Jong Shin,Kwon, Kyung-Hoon,Park, Young Mok Springer-Verlag 2014 Analytical and Bioanalytical Chemistry Vol.406 No.22
<P>Posttranslational modifications modulate protein function in cells. Global analysis of multiple posttranslational modifications can provide insight into physiology and disease, but presents formidable challenges. In the present study, we used a technique that does not require target enrichment to analyze alterations in the phosphorylation and ubiquitination of proteins from patients with Alzheimer's disease (AD). Guided by our previous findings, we applied three strategies to further our understanding of the dysregulation of posttranslationally modified proteins. We first identified phosphorylation sites by determining peptide pI shifts using OFFGEL. Second, using tandem mass spectrometry, we determined the ubiquitination status of the proteins using an assay for a trypsin digestion remnant of ubiquitination (Gly-Gly). Third, for large-scale discovery, we quantified the global differences in protein expression. Of the proteins expressed in AD tissue at levels of 2.0 or greater compared with controls, 60 were phosphorylated and 56 were ubiquitinated. Of the proteins expressed at levels of 0.5 or lower compared with controls, 81 were phosphorylated and 56 were ubiquitinated. Approximately 98?% of the phosphopeptides exhibited a pI shift. We identified 112 new phosphorylation sites (51.38?%), and 92 new ubiquitination sites (96.84?%). Taken together, our findings suggest that analysis of the alterations in posttranslationally modified proteins may contribute to understanding the pathogenesis of AD and other diseases.</P>
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Chromosome 11-Centric Human Proteome Analysis of Human Brain Hippocampus Tissue
Kwon, Kyung-Hoon,Kim, Jin Young,Kim, Se-Young,Min, Hye Kyeong,Lee, Hyoung-Joo,Ji, In Jung,Kang, Taewook,Park, Gun Wook,An, Hyun Joo,Lee, Bonghee,Ravid, Rivka,Ferrer, Isidro,Chung, Chun Kee,Paik, Young American Chemical Society 2013 Journal of proteome research Vol.12 No.1
<P>Human chromosome 11 is the third gene-rich chromosome having 1304 protein-coding genes. According to the GeneCards, this chromosome contains 240 genes related to diseases, as it is well known as a disease-rich chromosome. Although there are many protein-coding genes, the proteomic identification ratio is rather low. As a model study, human hippocampal tissues from patients suffering from Alzheimer’s disease and epilepsy were prepared to evaluate the gene-centric statistics related to the gene expression and disorders of chromosome 11. A total of 8828 protein coding genes from brain tissues were extensively off-gel fractionated and profiled by a high resolution mass spectrometer with collision induced dissociation and electron transfer dissociation. Five-hundred twenty-three of the proteins from brain tissues were determined to belong to chromosome 11, representing 37% of the proteins reported in the Global Proteome Machine Database. We extracted gene clusters from a specific biological process or molecular function in gene ontology, among which the olfactory receptor genes showed the largest cluster on chromosome 11. Analysis of the proteome data set from the hippocampus provides a significant network associated with genes and proteins and leads to new insights into the biological and genetic mechanisms of chromosome 11-specific diseases such as Alzheimer’s disease.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jprobs/2013/jprobs.2013.12.issue-1/pr3008368/production/images/medium/pr-2012-008368_0004.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/pr3008368'>ACS Electronic Supporting Info</A></P>
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Li, Hong-Mei,Jang, Ji Hye,Jung, Jun-Sub,Shin, Jiseon,Park, Chul O.,Kim, Yeon-Ja,Ahn, Won-Gyun,Nam, Ju-Suk,Hong, Chang-Won,Lee, Jongho,Jung, Yu-Jin,Chen, Jiang-Fan,Ravid, Katya,Lee, H. Thomas,Huh, Won- American Association of Immunologists 2019 Journal of Immunology Vol. No.
<P>G2A is a GPCR abundantly expressed in immune cells. G2A<SUP>−/−</SUP> mice showed higher lethality, higher plasma cytokines, and an impaired bacterial clearance in response to a murine model of sepsis (cecal ligation and puncture), which were blocked by GdCl<SUB>3</SUB>, an inhibitor of Kupffer cells. Anti–IL-10 Ab reversed the impaired bacterial clearance in G2A<SUP>−/−</SUP> mice. Indomethacin effectively blocked both the increased i.p. IL-10 levels and the impaired bacterial clearance, indicating that disturbed PG system is the proximal cause of these phenomena. Stimulation with LPS/C5a induced an increase in <I>Escherichia coli</I> phagocytosis and intracellular cAMP levels in G2A<SUP>+/+</SUP> peritoneal macrophages but not G2A<SUP>−/−</SUP> cells, which showed more PGE<SUB>2</SUB>/nitrite release and intracellular reactive oxygen species levels. Heterologous coexpression of G2A and adenosine receptor type 2b (A2bAR) induced a synergistic increase in cAMP signaling in a ligand-independent manner, with the evidence of physical interaction of G2A with A2bAR. BAY 60-6583, a specific agonist for A2bAR, increased intracellular cAMP levels in Kupffer cells from G2A<SUP>+/+</SUP> but not from G2A<SUP>−/−</SUP> mice. Both G2A and A2bAR were required for antiseptic action of lysophosphatidylcholine. These results show inappropriate activation of G2A<SUP>−/−</SUP> Kupffer cells to septic insults due to an impaired cAMP signaling possibly by lack of interaction with A2bAR.</P>
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