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Hãy vào Tìm chi tiết nếu chưa tìm thấy kết quả thoả mãn.
3 kết quả thoả mãn.

1 
Võ Thanh Tú; TS. Nguyễn Đình Lân (hướng dẫn), Trường ĐHSP Tp. HCM, 2011. application/octet-stream, 0 kB.

2 
Lin li; Konstantin V. Kandror (approver), ProQuest Information and Learning Company, 2007. application/octet-stream, 0 kB.
  Small GLUT4-containing vesicles represent the major insulin-responsive compartment in fat and skeletal muscle cells. These vesicles derive from the perinuclear "donor" compartment that represents recycling endosomes and/or trans-Golgi reticulum. However, the molecular mechanism of the formation of these vesicles is not yet known. In order to address the problem of GLUT4 targeting to the perinuclear "donor'' compartment, we created several "gain of function" chimeric molecules between GLUT4 and cellugyrin, a four transmembrane protein that shares a part of the intracellular trafficking route with GLUT4, but is excluded from insulin-responsive vesicles. Cellugyrin with the carboxy-terminal tail substituted by that of GLUT4 was localized in the perinuclear "donor" compartment, but its targeting to the insulin-responsive vesicles was inefficient. In contrast, GLUT4 with the carboxy-terminal tail substituted by that of cellugyrin no longer concentrated in the perinuclear "donor'' compartment, but retained its vesicular localization and insulin responsiveness. We conclude that the C-terminus of GLUT4 is responsible for its targeting to the perinuclear "donor'' compartment but is not sufficient for protein entry into insulin-responsive vesicles. We also studied the role of the newly discovered family of monomeric adaptor proteins, GGA, in the formation of insulin-responsive vesicles. Double immunostaining suggests that GGA and GLUT4 co-localize specifically in the perinuclear "donor" compartment. Using the techniques of immunoadsorption as well as GST pull down assay we found that GLUT4-containing vesicles interact with GGA adaptors in vitro and the interaction may be mediated by the putative sorting receptor, sortilin, that represents a major component protein of GLUT4-containing vesicles. In addition, recombinant dominant negative GGA inhibits formation of insulin-responsive vesicles in a reconstitution system in vitro. This inhibitory effect was recapitulated in the 3T3-L1 cell line stably expressing low levels of dominant negative GGA. Thus, our data suggest that GGA adaptors are directly responsible for the formation of insulin-responsive GLUT4-containing vesicles.

3 
Đậu Thị Huế; PGS.TS. Mỵ Vinh Quang (hướng dẫn), Trường ĐHSP Tp. HCM, 2013. application/octet-stream, 0 kB.