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  1. Home
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Browsing by Subject "Exocytosis"

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    Membrane trafficking and exocytosis are upregulated in port wine stain blood vessels
    (Universidad de Murcia. Departamento de Biología Celular e Histología, 2019) Yin, Rong; Rice, Shawn J.; Wang, Jinwei; Gao, Lin; Tsai, Joseph; Anvari, Radean T.; Zhou, Fang; Liu, Xin; Wang, Gang; Tang, Yuxin; Mihm Jr, Martin C.; Belani, Chandra P.; Chen, Dong Bao; Nelson, J. Stuart; Tan, Wenbin
    Introduction. Port wine stain (PWS) is characterized as a progressive dilatation of immature venule-like vasculatures which result from differentiation-impaired endothelial cells. In this study, we aimed to identify the major biological pathways accounting for the pathogenesis of PWS. Methods. Sequential windowed acquisition of all theoretical fragment ion mass spectra (SWATH-MS) was used to identify differentially expressed proteins in PWS lesions, followed by confirmative studies with immunohistochemistry, immunoblot and transmission electron microscopy (TEM). Results. 107 out of 299 identified proteins showed differential expressions in PWS lesions as compared to normal skin, mainly involving the functions of biosynthesis, membrane trafficking, cytoskeleton and cell adhesion/migration. The confirmative studies showed that expressions of membrane trafficking/ exocytosis related proteins such as VAT1, IQGAP1, HSC70, clathrin, perlecan, spectrin α1 and GDIR1 were significantly increased in PWS blood vessels as compared to normal ones. Furthermore, TEM studies showed there is a significant upregulation of extracellular vesicle exocytosis from PWS blood vessels as compared to control. Conclusions. The biological process of membrane trafficking and exocytosis is enhanced in PWS blood vessels. Our results imply that the extracellular vesicles released by lesional endothelial cells may act as potential intercellular signaling mediators to contribute to the pathogenesis of PWS.
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    Rab3D a regulator of exocytosis in non-neuronal cells
    (Murcia : F. Hernández, 2002) Millar, A.L.; Pavlos, N.J.; Xu, J.; Zheng, M.H.
    Rab3D, a small Ras-like GTPase, is a key regulator of intracellular vesicle transport during exocytosis. It has been shown that Rab3 GTPases are abundant in cells with regulated secretory pathways and are thought to confer the specificity of docking and fusion during regulated exocytosis. Unlike other Rab3 isoforms, Rab3D is enriched in a number of nonneuronal tissues and is localised to secretory granules in the cytoplasm of these cells. The structure of Rab3D exhibits all of the conserved domains from the Rab family and also contains hypervariable N- and Cterminal regions. Rab3D undergoes post-translational isoprenylation and cycles between GDP- and GTPbound forms. Apart from the factors involved in the Rab activation cycle, few Rab3D effector proteins have been identified to date. Nevertheless, it has long been suggested that Rab3D plays a role in regulated exocytotic processes as well as apically directed transcytosis. This review summarises the recent work on the biological function, structural integrity and molecular interactions of Rab3D in non-neuronal cells.

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