라틴아메리카에서 활동하는 중국의 세 행위자: 정부, 준정부기관, 기업

원제와 출처: Yang Zhimin, Los actores del desembarco chino en América Latina, Nueva Sociedad, No. 259, septiembre-octubre de 2015, pp. 45-54.지난 20년 동안 이루어진 중국의 라틴아메리카·카리브 해 진출은 세계적인 관심을 불러일으켰다. 특히, 갈수록 긴밀해지는 중국과 라틴아메리카의 경제적 유대는 뜨거운 토론의 주제가 되었다. 중국이 전 세계 어느 곳에서나 마찬가지로 라틴아메리카에서 갈수록 중요한 역할을 하고 있다는 사실은 의심의 여지가 없다. 또 지난 35년간 연평균 10%의 경제성장률을 유지하는 세계 최대의 수출대국이자 세계 제2의 경제 대국으로서 중국은 라틴아메리카 경제에 중요한 행위자로 간주되고 있다. 오늘날 중국은, 규모로 보아 라틴아메리카의 둘째가는 교역대상국이자 셋째가는 투자국이다. 중국은 앞으로도 라틴아메리카와 더욱 긴밀한 경제 관계를 유지할 것이다. 왜냐하면 중국 정부가 라틴아메리카와 경제협력 수준을 높이기 위해 특별한 조치를 했을 뿐 아니라 중국과 라틴아메리카·카리브 해 국가 공동체 포럼(China-CELAC Forum)을 통해 경제협력의 새로운 기반을 구상했기 때문이다

PCSK9이 LDL receptor의 재활용을 억제하는데 에는 CAP1과의 결합이 필수적 이다: CAP1 결손쥐 분석의 결과

학위논문 (박사)-- 서울대학교 융합과학기술대학원 분자의학 및 바이오제약학과, 2017. 8. 김효수.Introduction: Proproteinconvertase subtilisin/kexin type 9 (PCSK9) regulates low density lipoprotein receptor (LDLR) expression on liver cells mediating its lysosomal degradation. Therefore, PCSK9 has emerged as an important target of lowering LDL-cholesterol and also treatment of atherosclerotic cardiovascular diseases. However, the precise mechanism how PCSK9 mediates LDLR internalization and degradation has not yet been elucidated. Interestingly, the fully folded C-terminal Cysteine-histidine rich domain (CHRD) structure of PCSK9 has a distinct structural similarity to the resistin homotrimer. CHRD of PCSK9 does not interact directly with the LDL receptor, but the CHRD is nevertheless required for PCSK9 mediated LDLR degradation. Previously, we identified adenylyl cyclase-associated protein 1 (CAP1) as a functional receptor for human resistin and clarified its intracellular signaling pathway to modulate inflammatory action of monocytes. We showed PCSK9 directly interacts with CAP1 in vitro and in vivo. Furthermore, interaction between PCSK9 CHRD and CAP1 SH3 domain is crucial for LDLR degradation. High-fed mice deficient CAP1 (CAP1-/+) significantly display decreased low-density lipoprotein cholesterol levels in serum and increased LDLR protein in liver without significant change in its mRNA level. We also found that binding between CAP1 and PCSK9 occurs in lipid-raft on 30 minutes after treatment of PCSK9. Caveolin 1 knockdown in HepG2 cells did not show a decrease in LDLR. In contrast, clathrin knockdown cells caused the degradation of LDLR in a treatment of PCSK9 dose-dependent manner. Taken together, we suggested that PCSK9/CAP1 axis stimulates LDLR internalization for degradation in caveolae lipid raft dependent pathway, distinct from clathrin-dependent pathway for LDLR recycling. Methods: In this study, we analyzed that CAP1 dependent PCSK9-LDLR degradation, endocytosis mechanism in transient CAP1 knockdown human hepatic cells (HepG2) and TALEN-mediated CAP1-/+ mouse. Results: CAP1-SH3 domain binds to PCSK9 directly. CAP1-PCSK9 complex increased LDLR degradation through lysosomal pathway. CAP1 targeting siRNA in HepG2 cells resulted in abolished LDLR degradation. These pathways are mainly showed caveolin 1 rich lipid-raft. Although caveolin 1 knockdown HepG2 cells abolished LDLR degradation treated PCSK9. In addition, lipoprofile analysis in CAP1-/+ mouse showed that LDL cholesterol physiological level in high-fed mice was decreased than wild type mice. Supportive results were obtained with an in vitro, in vivo system. Conclusions: The sorting of PCSK9 to the CAP1-LDLR is required for caveolae lipid raft to promote lysosomal LDLR degradation. This study provides valuable insights into mechanism regulating cholesterol homeostasis and LDLR degradation.Introduction 1 Material and Methods 5 Results 20 Discussion 51 Reference 58 Abstract in Korean 66Docto