http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
Jeong, Jee-Yeong,Kim, Jiwook,Kim, Bokyoum,Kim, Joowon,Shin, Yusom,Kim, Judeok,Ryu, Siejeong,Yang, Yu-Mi,Song, Kyoung Seob Hindawi Publishing Corporation 2016 MEDIATORS OF INFLAMMATION Vol.2016 No.-
<P>Mucus secretion is often uncontrolled in many airway inflammatory diseases of humans. Identifying the regulatory pathway(s) of mucus gene expression, mucus overproduction, and hypersecretion is important to alleviate airway inflammation in these diseases. However, the regulatory signaling pathway controlling mucus overproduction has not been fully identified yet. In this study, we report that the ATP/P2Y<SUB>2</SUB> complex secretes many cytokines and chemokines to regulate airway inflammation, among which IL-1 receptor antagonist (IL-1ra) downregulates<I> MUC5AC</I> gene expression via the inhibition of G<I>α</I>q-induced Ca<SUP>2+</SUP> signaling. IL-1ra inhibited IL-1<I>α</I> protein expression and secretion, and vice versa. Interestingly, ATP/P2Y<SUB>2</SUB>-induced IL-1ra and IL-1<I>α</I> secretion were both mediated by PLC<I>β</I>3. A dominant-negative mutation in the PDZ-binding domain of PLC<I>β</I>3 inhibited ATP/P2Y<SUB>2</SUB>-induced IL-1ra and IL-1<I>α</I> secretion. IL-1<I>α</I> in the presence of the ATP/P2Y<SUB>2</SUB> complex activated the ERK1/2 pathway in a greater degree and for a longer duration than the ATP/P2Y<SUB>2</SUB> complex itself, which was dramatically inhibited by IL-1ra. These findings suggest that secreted IL-1ra exhibits a regulatory effect on ATP/P2Y<SUB>2</SUB>-induced<I> MUC5AC</I> gene expression, through inhibition of IL-1<I>α</I> secretion, to maintain the mucus homeostasis in the airway. Therefore, IL-1ra could be an excellent modality for regulating inflamed airway microenvironments in respiratory diseases.</P>
Recombinant Interferon-${\alpha}$ Cross-linked with Thymosin ${\alpha}$1 is Biologically Active
Jeong, Jee-Yeong,Chung, Hye-Shin Korean Society for Biochemistry and Molecular Biol 1996 Journal of biochemistry and molecular biology Vol.29 No.4
Partially reduced interferon-a ($IFN-{\alpha}$) was cross-linked with thymosin ${\alpha}1$ ($T{\alpha}1$) using sulfo-succinimidyl (4-iodoacetyl) amino benzoate (SIAB), a bifunctional cross-linking reagent. The partially reduced $IFN-{\alpha}$ optimal for the cross-linking reaction was obtained by incubating native $IFN-{\alpha}$ with 0.5 mM DTT at $30^{\circ}C$ for 60~100 min. $T{\alpha}1$ was activated by incubating with sulfo-SIAB at $37^{\circ}C$ for 30 min to produce $T{\alpha}1-IAB$. The $T{\alpha}1-IFN-{\alpha}$ cross-linking was achieved by the reaction of the partially reduced $IFN-{\alpha}$ with $T{\alpha}1-IAB$. This cross-linking was between the sulfhydryl group of Cys1 in $IFN-{\alpha}$ and the N-terminal amino group of $T{\alpha}1$ through acetyl amino benzoate as a spacer. The immunological activity of the cross-linked molecule showed the same extent as that of $T{\alpha}1$, and most of the antiviral activity was retained compared to that of the partially reduced $IFN-{\alpha}$.
( Jee Yeong Jeong ),( Jin Rong Zhou ),( Chong Gao ),( Laurie Feldman ),( Arthur J. Sytkowski ) 생화학분자생물학회(구 한국생화학분자생물학회) 2014 BMB Reports Vol.47 No.7
In the present study, we demonstrate that ectopic expression of 56-kDa human selenium binding protein-1 (hSP56) in PC-3 cells that do not normally express hSP56 results in a marked inhibition of cell growth in vitro and in vivo. Down-regulation of hSP56 in LNCaP cells that normally express hSP56 results in enhanced anchorage-independent growth. PC-3 cells expressing hSP56 exhibit a significant reduction of hypoxia inducible protein (HIF)-1α protein levels under hypoxic conditions without altering HIF-1α mRNA (HIF1A) levels. Taken together, our findings strongly suggest that hSP56 plays a critical role in prostate cells by mechanisms including negative regulation of HIF-1α, thus identifying hSP56 as a candidate anti-oncogene product. [BMB Reports 2014; 47(7): 411-416]
Recombinant Interferon - α Cross - linked with Thymosin α1 is Biologically Active
Jeong, Jee Yeong,Chung, Hye Shin 생화학분자생물학회 1981 BMB Reports Vol.29 No.4
Partially reduced interferon-α (IFN-α) was cross-linked with thymosin α1 (Tα1) using sulfo-succinimidyl (4-iodoacetyl) amino benzoate (SIAB), a bifunctional cross-linking reagent. The partially reduced IFNa optimal for the cross-linking reaction was obtained by incubating native IFN-α with 0.5 mM DTT at 30℃ for 60-100 min. Tα1 was activated by incubating with sulfo-SIAB at 37℃ for 30 min to produce Tα1-IAB. The Tα1-IFN-α cross-linking was achieved by the reaction of the partially reduced IFN-α with Tα1-IAB. This cross-linking was between the sulfhydryl group of Cysl in IFN-α and the N-terminal amino group of Tα1 through acetyl amino benzoate as a spacer. The immunological activity of the cross-linked molecule showed the same extent as that of Tα1, and most of the antiviral activity was retained compared to that of the partially reduced IFN-α.
Quality Characteristics of Glycyrrhiza Varieties with Thermal Treatment
Gwi Yeong Jang(장귀영),Hyung Don Kim(김형돈),Su Ji Choi(최수지),Je Hun Choi(최재훈),Seung Eun Lee(이승은),Yun Jeong Jee(지윤정),Jeong Hoon Lee(이정훈),Heon Sang Jeong(정헌상),Dong Hwi Kim(김동휘),Kyung Hye Seo(서경혜) 한국약용작물학회 2019 한국약용작물학회 학술대회논문집 Vol.2019 No.1
Jeong, Young-Hee,Kim, Yeong Ji,Kim, Eun Young,Kim, Se Eun,Kim, Jiwoo,Park, Min Jee,Lee, Hong-Gu,Park, Se Pill,Kang, Man-Jong Cambridge University Press 2016 Zygote Vol.24 No.3
<B>Summary</B><P>Many transgenic domestic animals have been developed to produce therapeutic proteins in the mammary gland, and this approach is one of the most important methods for agricultural and biomedical applications. However, expression and secretion of a protein varies because transgenes are integrated at random sites in the genome. In addition, distal enhancers are very important for transcriptional gene regulation and tissue-specific gene expression. Development of a vector system regulated accurately in the genome is needed to improve production of therapeutic proteins. The objective of this study was to develop a knock-in system for expression of human fibroblast growth factor 2 (FGF2) in the bovine β-casein gene locus. The F2A sequence was fused to the human <I>FGF2</I> gene and inserted into exon 3 of the β-casein gene. We detected expression of human <I>FGF2</I> mRNA in the HC11 mouse mammary epithelial cells by RT-PCR and human FGF2 protein in the culture media using western blot analysis when the knock-in vector was introduced. We transfected the knock-in vector into bovine ear fibroblasts and produced knock-in fibroblasts using the clustered regularly interspaced short palindromic repeats (CRISPR)/Cas9 system. Moreover, the CRISPR/Cas9 system was more efficient than conventional methods. In addition, we produced knock-in blastocysts by somatic cell nuclear transfer using the knock-in fibroblasts. Our knock-in fibroblasts may help to create cloned embryos for development of transgenic dairy cattle expressing human FGF2 protein in the mammary gland via the expression system of the bovine β-casein gene.</P>
Jeong-Soon Kim,Sang-Nag Ahn,Sung-Jun Hong,Jin-Hyeuk Kwon,Yeong-Ki Kim,Hyeong-Jin Jee,Chang-Ki Shim 韓國作物學會 2011 Korean journal of crop science Vol.56 No.4
The objective of this study was to determine the genetic diversities of major rice blast resistance genes among 84 accessions of aromatic rice germplasm. Eighty four accessions were characterized by a dominant 11 set of PCR-based SNP and CAPS marker, which showed the broad spectrum resistance and closest linkage to seven major rice blast resistance (R) genes, Pia, Pib, Pii, Pi5 (Pi3), Pita (Pita-2), and Pi9 (t). The allele specific PCR markers assay genotype of SCAR and STS markers was applied to estimate the presence or absence of PCR amplicons detected with a pair of PCR markers. One indica accession, Basmati (IT211194), showed the positive amplicons of five major rice blast resistance genes, Pia, Pi5 (Pi3), Pib, Pi-ta (Pi-ta2), and Pik-5 (Pish). Among 48 accessions of the PCR amplicons detected with yca72 marker, only five accessions were identified to Pia gene on chromosome 11. The Pib gene was estimated with the NSb marker and was detected in 65 of 84 accessions. This study showed that nine of 84 accessions contained the Pii gene and owned Pi5 (Pi3) in 42 of 84 accessions by JJ817 and JJ113-T markers, which is coclosest with Pii on chromosome 9. Only six accessions were detected two alleles of the Pita or Pita-2 genes. Three of accessions were identified as the Pi9 (t) gene locus.