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Magnetic Nanoparticles for Organelle Separation
Published in Nguyễn T. K. Thanh, Clinical Applications of Magnetic Nanoparticles, 2018
Mari Takahashi, Shinya Maenosono
Chen et al.15 also investigated endosomal transport. Rab proteins regulate many steps of membrane trafficking, and two Rab proteins are important for transport by late endosomes. Rab9 regulates membrane trafficking from late endosomes to the trans-Golgi network (TGN), while Rab7 regulates membrane trafficking from late endosomes to lysosomes. It was confirmed that Rab7 association with late endosomes was increased by threefold in NPC1 mice compared with Wt mice, while no difference was observed in Rab9 association. These results indicate that the association–dissociation equilibrium of Rab7 is disturbed in NPC1 mouse late endosomes. In addition, the band of NPC2 protein observed for NPC1 mouse late endosomes was much broader than that for Wt mouse late endosomes. They attributed this broadening of the NPC2 band to variations in NPC2 glycosylation. Based on these results, it is thought that NPC2 protein is also compromised in NPC1 mice, presumably because of an interaction between NPC1 protein and NPC2 protein.
Differential Protein Expression Following JP-8 Jet Fuel Exposure
Published in Mark L. Witten, Errol Zeiger, Glenn D. Ritchie, Jet Fuel Toxicology, 2010
Frank A. Witzmann, Mark L. Witten
In a related subcellular system, renal vesicular trafficking activities involve small GTPases of the Rab subfamily whose membrane associations and dissociations are regulated by GDP-dissociation inhibitor proteins such as Rab GDI-beta. The expression of this renal cytoplasmic protein was increased by JP-8 exposure, a response that could conceivably hinder protein secretion by sequestering membrane-associated Rab GTPases in the cytoplasm [12, 17]. Because Rab GDI complexes are also required for vesicular transport from the endoplasmic reticulum (ER) to the Golgi stack, the increase in Rab GDI-beta could imply decreased vesicular transport of newly synthesized proteins to the Golgi apparatus. This response is supported by the observed decrease in annexin VI, a protein that promotes interactions between membranes that are destined to undergo fusion.
Ultrasound-assisted green synthesis of triazole-based azomethine/thiazolidin-4-one hybrid inhibitors for cancer therapy through targeting dysregulation signatures of some Rab proteins
Published in Green Chemistry Letters and Reviews, 2023
Aboubakr H. Abdelmonsef, Ahmed M. El-Saghier, Asmaa M. Kadry
Cancer is characterized by uncontrolled cell growth with metastasizes to other organs inside the body (1). Rab proteins are widely expressed in various human cancers (2–4). They are essential regulators of cell cycle progression and are responsible for gene expression (5). Rab proteins work as sensitive molecular switch existing either in an active GDP-bound form or an active GTP-bound form. Exchange from GDP to GTP is catalyzed by the guanidine exchange factor (GEF), leading to activation in response to various upstream signals. On the other hand, GTPase-activating protein (GAP) increases the intrinsic GTPase activity, resulting in the inactivation of the protein (3,4,6). The upregulation of the selected Rab proteins namely Rab2a, Rab25, Rab5, and Rab35 is linked with various human cancers such as breast, ovarian, lung, and leukemia, respectively (5,7,8). Therefore, targeting Rab proteins is an important strategy for the prevention and treatment of cancer.