• Molecules and Cells
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• v.43 no.6
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• pp.501-508
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• 2020

In eukaryotes, membraneous cellular compartmentation essentially requires vesicle trafficking for communications among distinct organelles. A donor organelle-generated vesicle releases its cargo into a target compartment by fusing two distinct vesicle and target membranes. Vesicle fusion, the final step of vesicle trafficking, is driven intrinsically by complex formation of soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs). Although SNAREs are well-conserved across eukaryotes, genomic studies revealed that plants have dramatically increased the number of SNARE genes than other eukaryotes. This increase is attributed to the sessile nature of plants, likely for more sensitive and harmonized responses to environmental stresses. In this review, we therefore try to summarize and discuss the current understanding of plant SNAREs function in responses to biotic and abiotic stresses.

• Molecules and Cells
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• v.43 no.4
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• pp.313-322
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• 2020

Eukaryotes transport biomolecules between intracellular organelles and between cells and the environment via vesicle trafficking. Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNARE proteins) play pivotal roles in vesicle and membrane trafficking. These proteins are categorized as Qa, Qb, Qc, and R SNAREs and form a complex that induces vesicle fusion for targeting of vesicle cargos. As the core components of the SNARE complex, the SNAP25 Qbc SNAREs perform various functions related to cellular homeostasis. The Arabidopsis thaliana SNAP25 homolog AtSNAP33 interacts with Qa and R SNAREs and plays a key role in cytokinesis and in triggering innate immune responses. However, other Arabidopsis SNAP25 homologs, such as AtSNAP29 and AtSNAP30, are not well studied; this includes their localization, interactions, structures, and functions. Here, we discuss three biological functions of plant SNAP25 orthologs in the context of AtSNAP33 and highlight recent findings on SNAP25 orthologs in various plants. We propose future directions for determining the roles of the less well-characterized AtSNAP29 and AtSNAP30 proteins.

• Proceedings of the Korean Society of Developmental Biology Conference
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• 2005.07a
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• pp.38-38
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• 2005

• Proceedings of the Korean Society of Developmental Biology Conference
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• 2005.10a
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• pp.117-117
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• 2005

• Proceedings of the Korean Society of Embryo Transfer Conference
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• 2005.10a
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• pp.117-117
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• 2005

• Proceedings of the Korean Society of Developmental Biology Conference
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• 2005.10a
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• pp.42-43
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• 2005

• Proceedings of the Korean Society of Embryo Transfer Conference
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• 2005.10a
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• pp.42-43
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• 2005

• Journal of Nutrition and Health
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• v.39 no.4
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• pp.323-330
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• 2006

Peripheral insulin resistance in obese/type II diabetes animals results from an impairment of insulin-stimulated glucose uptake into skeletal muscle. Insulin stimulate the translocation of GLUT4 from intracellular location to the plasma membrane. Soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) is implicated in mediation of fusion of GLUT4-containing vesicle with the plasma membrane. Present study investigated regulatory effects of Rhodiola sachalinensis administration and exercise training on the expression of GLUT4 protein and SNAREs protein in skeletal muscles of obese Zucker rats. Experimental animals were randomly assigned into one of five groups ; lean control(LN), obese control(OB), exercise-treated(EXE), Rhodiola sachalinensis-treated(Rho), combine of Rho & EXE (Rho-EXE). All animals of exercise training (EXE, Rho-EXE) performed treadmill running for 8 weeks, and animals of Rho groups (Rho, Rho-EXE) were dosed daily by gastric gavage during the same period. After experiment, blood were taken for analyses of glucose, insulin, and lipids levels. Mitochondrial oxidative enzyme (citrate synthase, CS ; $\beta$-hydroxyacyl-CoA dehydrogenase, $\beta$-HAD) activity were analysed. Skeletal muscles were dissected out for analyses of proteins (GLUT4, VAMP2, syntaxin4, SNAP23). Results are as follows. Exercise and/or Rhodiola sachalinensis administration significantly reduced body weight and improved blood lipids (TG, FFA), and increased insulin sensitivity. Endurance exercise significantly increased the activity of mitochondrial enzymes and the expression of GLUT4 protein, however, administration of Rhodiola sachalinensis did not affect them. The effect of exercise and/or Rhodiola sachalinensis administration on the expression of SNARE proteins was unclear. Our study suggested that improvement insulin sensitivity by exercise and/or Rhodiola sachalinensis administration in obese Zucker rats is independent of expression of SNARE proteins.

• Journal of Chest Surgery
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• v.32 no.7
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• pp.668-670
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• 1999

The most important indication for the removal of the lead-electrode system is the presence of an infection. When an infection occurs, the entire pacemaker system including the impluse generator and lead-electrode system should be removed. The entrapped electrode can be removed by a continous traction, by the use of forceps, snares or baskets, by the use of a locking stylet or a dilator sheath, and by an operation. We report a case that underwent a removal of an entrapped transvenous pacemaker electrode by the use of snaring technique.

• Journal of Chest Surgery
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• v.28 no.4
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• pp.404-408
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• 1995

Infection, although uncommon, can be the most lethal of all potential complication after transvenous pacemaker implantation. When infection is present, removal of the electrode is the only successful means of therapy. The entrapped electrode can be removed by continuous traction, by use of endoscopic forceps and snares, and by operation. We report 2 cases of removal of infected transvenous pacemaker successfully. In one case of staphylococcus aureus endocarditis associated with a retained pacemaker electrode, the electrode was removed by hand traction. The other case of skin infection of generator pocket, the electrode removed by orthopedic pulley system. Consequently, we recommended removal of all hardware if there is infection of the pacemaker system.