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Kim, Geona,Jo, Yuna,Lee, Byunghyuk,Ali, Laraib Amir,Lee, Boae,Hong, Changwan MDPI 2018 INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES Vol.19 No.11
<P>IL-7 is an essential, nonredundant growth factor for T and B cell generation and maintenance. While IL-7 deficiency results in lymphopenia, overexpression of IL-7 can cause neoplasia in experimental models. IL-7’s involvement in neoplasia has been appreciated through studies of IL-7 transgenic (Tg) mice models and human lymphoma patients. Since we recently found that a soluble form of the common γ-chain (γc) cytokine receptor (sγc) antagonistically regulates IL-7 signaling, IL-7 and sγc double-Tg mice were generated to investigate the effects of sγc overexpression in IL-7-mediated lymphoproliferative disorders (LPDs). The overexpression of sγc prevents IL-7Tg-induced abnormal increase of LN cell numbers and the development of splenomegaly, resulting in striking amelioration of mortality and disease development. These results suggest that modification of γc cytokine responsiveness by sγc molecules might control various γc cytokine-associated hematologic malignancy, and also provide an alternative view to approach antitumor therapy.</P>
Effects of Porcine Seminal Plasma in In Vitro Culture of Embryos
JoonHo Moon,SuJin Kim,JungTaek Kang,SolJi Park,JiYei Choi,JiHyun Lee,Islam M. Saadeldin,HyunJu Oh,JungEun Park,MinJung Kim,GeonA Kim,Eun Jung Park,Jin Choi,Goo Jang,Byeong Chun Lee 한국동물번식학회 2012 Reproductive & developmental biology Vol.36 No.2
Effects of Porcine Seminal Plasma in In Vitro Culture of Embryos
JoonHo Moon,SuJin Kim,JungTaek Kang,SolJi Park,JiYei Choi,JiHyun Lee,Islam M. Saadeldin,HyunJu Oh,JungEun Park,MinJung Kim,GeonA Kim,Eun Jung Park,Jin Choi,Goo Jang,Byeong Chun Lee 한국동물번식학회 2012 Reproductive & Developmental Biology(Supplement) Vol.36 No.2s
Semen can be divided into two parts. One is cellular part which contains sperms the other is liquid part which is called by seminal plasma. The seminal plasma is a nutritive and protective medium for the sperms. Fructose, which is major energy source, is supplied to sperms swim to female oocyte. Alkalic property protects sperms from hostile environment of female reproductive organ. Also, seminal plasma induces tolerance to preexisted immune cells, and changes intra-uterine environment to better conditions for fertilized embryos to implant. However, the effects of seminal plasma in in vitro culture of fertilized embryos are unclear. Second fraction of fresh semen was obtained from a normal farm pig. The semen was centrifuged to remove sperms, and then supernatant was filtrated. The filtered seminal plasma was stored in - 30℃. In this study, electrically activated and chemically activated porcine embryos were employed to investigate the developmental rate after 2 hours treatment of none, 0.1%, 0.5%, and 1% seminal plasma in culture media by two days of activation. Both electrically and chemically activated embryos, cleavage rate and cell numbers of blastocysts were not significant difference within four groups. Blastocyst formation rate of electrically activated embryos also did not show significant difference within any groups. However 0.1% seminal plasma treatment group showed significantly increase of blastocyst formation rate in chemically activated group (None; 24.8%, 0.1%; 31.7%, 0.5%; 19.4, and 1%; 16.5%, respectively. p<0.05).
IL-7 Induces an Epitope Masking of<i>γ</i>c Protein in IL-7 Receptor Signaling Complex
Goh, Tae Sik,Jo, Yuna,Lee, Byunghyuk,Kim, Geona,Hwang, Hyunju,Ko, Eunhee,Kang, Seung Wan,Oh, Sae-Ock,Baek, Sun-Yong,Yoon, Sik,Lee, Jung Sub,Hong, Changwan Hindawi Limited 2017 Mediators of inflammation Vol.2017 No.-
<P>IL-7 signaling via IL-7R<I>α</I>and common<I>γ</I>-chain (<I>γ</I>c) is necessary for the development and homeostasis of T cells. Although the delicate mechanism in which IL-7R<I>α</I>downregulation allows the homeostasis of T cell with limited IL-7 has been well known, the exact mechanism behind the interaction between IL-7R<I>α</I>and<I>γ</I>c in the absence or presence of IL-7 remains unclear. Additionally, we are still uncertain as to how only IL-7R<I>α</I>is separately downregulated by the binding of IL-7 from the IL-7R<I>α</I>/<I>γ</I>c complex. We demonstrate here that 4G3, TUGm2, and 3E12 epitope masking of<I>γ</I>c protein are induced in the presence of IL-7, indicating that the epitope alteration is induced by IL-7 binding to the preassembled receptor core. Moreover, the epitope masking of<I>γ</I>c protein is inversely correlated with the expression of IL-7R<I>α</I>upon IL-7 binding, implying that the structural alteration of<I>γ</I>c might be involved in the regulation of IL-7R<I>α</I>expression. The conformational change in<I>γ</I>c upon IL-7 binding may contribute not only to forming the functional IL-7 signaling complex but also to optimally regulating the expression of IL-7R<I>α</I>.</P>