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Lee, Hwa Kyoung,Jin, Junyeong,Kim, Sang Il,Kang, Min Jueng,Yi, Eugene C.,Kim, Ji Eun,Park, Jong Bae,Kim, Hyori,Chung, Junho Elsevier 2017 Biochemical and biophysical research communication Vol.493 No.1
<P><B>Abstract</B></P> <P>The proto-oncogene tyrosine kinase ROS1 plays a key role in carcinogenesis through gene rearrangement to form a fusion protein with other genes, in which the C-terminal intracellular region of ROS1 participates. The possibility of wild type ROS1 overexpression through epigenetic regulation has been proposed. Here, we generated an antibody, 3B20, reactive to the N-terminal region of ROS1 to use it for the detection of wild type ROS1 in cancerous tissues. Using immunoblot and immunoprecipitation analyses, we found that 3B20 also reacted with heat shock proteins (Hsp)70s. Using homology searching, ROS1 and Hsp70s were found to share an identical amino acid sequence: DLGT. Using alanine mutagenesis of ROS1, the epitope was found to harbor this sequence. To modify the idiotope with the aim of selecting more specific antibodies, we introduced random mutations into the heavy chain complementarity-determining region 3 and successfully generated an antibody clone, 3B20-G1K, with a point mutation that only reacted with ROS1 in enzyme-linked immunosorbent assays, and in immunoblot and immunoprecipitation analysis. In immunohistochemical analysis using 3B20-G1K, ROS1 was found to be absent in normal lung tissues and was overexpressed in a case of lung adenocarcinoma.</P> <P><B>Highlights</B></P> <P> <UL> <LI> An antibody to N-terminal region of ROS1 was generated. </LI> <LI> Modification of HCDR3 dramatically enhanced the specificity of an anti-ROS1 antibody. </LI> <LI> Full-length wild type ROS1 is not detected in normal lung tissue. </LI> <LI> Full-length wild type ROS1 is overexpressed in 10% of lung adenocarcinoma. </LI> </UL> </P>
Urinary Proteome Profile Predictive of Disease Activity in Rheumatoid Arthritis
Kang, Min Jueng,Park, Yune-Jung,You, Sungyong,Yoo, Seung-Ah,Choi, Susanna,Kim, Dong-Ho,Cho, Chul-Soo,Yi, Eugene C.,Hwang, Daehee,Kim, Wan-Uk American Chemical Society 2014 JOURNAL OF PROTEOME RESEARCH Vol.13 No.11
<P>Current serum biomarkers for rheumatoid arthritis (RA) are not highly sensitive or specific to changes of disease activities. Thus, other complementary biomarkers have been needed to improve assessment of RA activities. In many diseases, urine has been studied as a window to provide complementary information to serum measures. Here, we conducted quantitative urinary proteome profiling using liquid chromatography–tandem mass spectrometry (LC–MS/MS) and identified 134 differentially expressed proteins (DEPs) between RA and osteoarthritis (OA) urine samples. By integrating the DEPs with gene expression profiles in joints and mononuclear cells, we initially selected 12 biomarker candidates related to joint pathology and then tested their altered expression in independent RA and OA samples using enzyme-linked immunosorbent assay. Of the initial candidates, we selected four DEPs as final candidates that were abundant in RA patients and consistent with those observed in LC–MS/MS analysis. Among them, we further focused on urinary soluble CD14 (sCD14) and examined its diagnostic value and association with disease activity. Urinary sCD14 had a diagnostic value comparable to conventional serum measures and an even higher predictive power for disease activity when combined with serum C-reactive protein. Thus, our urinary proteome provides a diagnostic window complementary to current serum parameters for the disease activity of RA.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jprobs/2014/jprobs.2014.13.issue-11/pr500467d/production/images/medium/pr-2014-00467d_0006.gif'></P><P><A href='http://pubs.acs.org/doi/suppl/10.1021/pr500467d'>ACS Electronic Supporting Info</A></P>
김선민,Byoung-Kyu Cho,Byoung Jae Kim,Ha Yun Lee,Errol R. Norwitz,Min Jueng Kang,Seung Mi Lee,박찬욱,Jong Kwan Jun,Eugene C. Yi,박중신 대한의학회 2020 Journal of Korean medical science Vol.35 No.10
Background: Twin-to-twin transfusion syndrome (TTTS) is a serious complication of monochorionic twin pregnancies. It results from disproportionate blood supply to each fetus caused by abnormal vascular anastomosis within the placenta. Amniotic fluid (AF) is an indicator reflecting the various conditions of the fetus, and an imbalance in AF volume is essential for the antenatal diagnosis of TTTS by ultrasound. In this study, two different mass spectrometry quantitative approaches were performed to identify differentially expressed proteins (DEPs) within matched pairs of AF samples. Methods: We characterized the AF proteome in pooled AF samples collected from donor and recipient twin pairs (n = 5 each) with TTTS by a global proteomics profiling approach and then preformed the statistical analysis to determine the DEPs between the two groups. Next, we carried out a targeted proteomic approach (multiple reaction monitoring) with DEPs to achieve high-confident TTTS-associated AF proteins. Results: A total of 103 AF proteins that were significantly altered in their abundances between donor and recipient fetuses. The majority of upregulated proteins identified in the recipient twins (including carbonic anhydrase 1, fibrinogen alpha chain, aminopeptidase N, alpha-fetoprotein, fibrinogen gamma chain, and basement membrane-specific heparan sulfate proteoglycan core protein) have been associated with cardiac or dermatologic disease, which is often seen in recipient twins as a result of volume overload. In contrast, proteins significantly upregulated in AF collected from donor twins (including IgGFc-binding protein, apolipoprotein C-I, complement C1q subcomponent subunit B, apolipoprotein C-III, apolipoprotein A-II, decorin, alpha-2-macroglobulin, apolipoprotein A-I, and fibronectin) were those previously shown to be associated with inflammation, ischemic cardiovascular complications or renal disease. Conclusion: In this study, we identified proteomic biomarkers in AF collected from donor and recipient twins in pregnancies complicated by TTTS that appear to reflect underlying functional and pathophysiological challenges faced by each of the fetuses.
Cha, Moon‐,Yong,Kwon, Yoo‐,Wook,Ahn, Hyo‐,Suk,Jeong, Hyobin,Lee, Yong Yook,Moon, Minho,Baik, Sung Hoon,Kim, Dong Kyu,Song, Hyundong,Yi, Eugene C.,Hwang, Daehee,Kim, Hyo‐,Soo,Mo John Wiley and Sons Inc. 2017 Stem cells translational medicine Vol.6 No.1
<P><B>Abstract</B></P><P>Transplantation of stem cells into the brain attenuates functional deficits in the central nervous system via cell replacement, the release of specific neurotransmitters, and the production of neurotrophic factors. To identify patient‐specific and safe stem cells for treating Alzheimer's disease (AD), we generated induced pluripotent stem cells (iPSCs) derived from mouse skin fibroblasts by treating protein extracts of embryonic stem cells. These reprogrammed cells were pluripotent but nontumorigenic. Here, we report that protein‐iPSCs differentiated into glial cells and decreased plaque depositions in the 5XFAD transgenic AD mouse model. We also found that transplanted protein‐iPSCs mitigated the cognitive dysfunction observed in these mice. Proteomic analysis revealed that oligodendrocyte‐related genes were upregulated in brains injected with protein‐iPSCs, providing new insights into the potential function of protein‐iPSCs. Taken together, our data indicate that protein‐iPSCs might be a promising therapeutic approach for AD. S<SMALL>TEM</SMALL> C<SMALL>ELLS</SMALL> T<SMALL>RANSLATIONAL</SMALL> M<SMALL>EDICINE</SMALL><I>2017;6:293–305</I></P>
Kim, Kristine M.,Yi, Eugene C.,Kim, Youngsoo Elsevier 2012 Methods Vol.56 No.2
<P><B>Abstract</B></P><P>Protein receptor–ligand interactions play important roles in mediating enzyme catalysis, signal transduction, and other protein functions. Immunoaffinity purification followed by mass spectrometry analysis is a common method for identifying protein receptor–ligand complexes. However, it is difficult to distinguish between specific protein binding partners and non-specifically bound proteins that co-purify with the complex. In addition, weakly interacting binding partners may dissociate from the protein receptor–ligand complexes during immunoaffinity purification. The combination of chemical crosslinking, affinity purification, and differential mass spectrometry analysis provides a direct method for capturing stable, weak, and transient protein interactions that occur <I>in vivo</I> and <I>in vitro</I>. This approach enables the identification of functional receptor–ligand binding partners with high confidence. Herein, we describe a differential mass spectrometry approach coupled with <I>in situ</I> chemical crosslinking and immunoaffinity purification for identifying receptor–ligand binding partners. In particular, we identified a functional, counter-ligand structure of the natural killer cell p30-related protein.</P>