• Korean Security Journal
• /
• no.46
• /
• pp.171-187
• /
• 2016

Human trafficking is a booming underground business and is the fastest growing and criminal activity in today's society. The use of coercion or fraud marks the territory of trafficking. Most people trafficked suffer constant threats, violence, and forced acts while imprisoned by their traffickers. Such human trafficking entails significant problems not only for the victims but also for the economies and community health. Large corporations overseas have also been known to partake in the sex slave industry. Another hidden cost to the global economy is the cost of law enforcement and anti-trafficking measures being implemented. Further, sex Trafficking carries many potential health consequences, one of the biggest risks is HIV infection. That means, sex trafficking is an engine of the global AIDS epidemic with one study portraying nearly fifty six percent of all sex slaves having HIV or AIDS. Therefore, many of people are being infected with HIV and many other diseases every day through contact with the sex slave industry costing millions to society and the global economy. in this study, the author presents a case study of trafficking against Nepalese women. Nepalese women being trafficked are found to have a high prevalence of HIV infection. In conclusion and discussion, a few of solutions needed to be addressed for controling human trafficking for sex slavery suggested.

• Bulletin of the Korean Chemical Society
• /
• v.33 no.9
• /
• pp.3071-3075
• /
• 2012

Human ${\alpha}$-synuclein is the major component of the protein aggregates known as Lewy bodies or Lewy neurites, which define the intracellular lesions of Parkinson's disease. Despite extensive efforts, the physiological function of ${\alpha}$-synuclein has not yet been elucidated in detail. As an approach to defining its function, proteins that interacted with ${\alpha}$-synuclein were screened in phage display assays. The SNARE protein vesicle t-SNARE-interacting protein homologous 1B (VTI1B) was identified as an interacting partner. A selective interaction between ${\alpha}$-synuclein and VTI1B was confirmed by coimmunoprecipitation and GST pull-down assays. VTI1B and ${\alpha}$-synuclein were colocalized in N2a neuronal cells, and overexpression of ${\alpha}$-synuclein changed the subcellular localization of VTI1B to be more dispersed throughout the cytosol. Considering the role played by VTI1B, ${\alpha}$-synuclein is likely to modulate vesicle trafficking by interacting with a SNARE complex.

• BMB Reports
• /
• v.44 no.3
• /
• pp.170-175
• /
• 2011

We identified a bovine $B_{12}$ trafficking chaperone bCblC in Bos taurus that showed 88% amino acid sequence identity with a human homologue. The protein bCblC was purified from E. coli by over-expression of the encoding gene. bCblC bound cyanocobalamin (CNCbl), methylcobalamin (MeCbl) and adenosylcobalamin (AdoCbl) in the base-off states and eliminated the upper axial ligands forming aquo/hydroxocobalamin ($OH_2$/OHCbl) under aerobic conditions. A transition of $OH_2$/OHCbl was induced upon binding to bCblC. Interestingly, bCblC-bound $OH_2$/OHCbl did not react with reduced glutathione (GSH), while the reaction of free$OH_2$/OHCbl with GSH resulted in the formation of glutathionylcobalamin (GSCbl) and glutathione disulfide (GSSG). Furthermore we found that bCblC eliminates the GSH ligand of GSCbl forming $OH_2$/OHCbl. The results demonstrated that bCblC is a $B_{12}$ trafficking chaperone that binds cobalamins and protects $OH_2$/OHCbl from GSH, which could be oxidized to GSSG by free $OH_2$/OHCbl.

• Proceedings of the Korean Institute of Surface Engineering Conference
• /
• 2017.05a
• /
• pp.81-81
• /
• 2017

Nanotechnology is of great importance to molecular biology and medicine because life processes are maintained by the action of a series of molecular nanomachines in the cell machinery. Recent advances in nanoscale materials that possess emergent physical properties and molecular organization hold great promise to impact human health in the diagnostic and therapeutic arenas. In order to be effective, nanomaterials need to navigate the host biology and traffic to relevant biological structures, such as diseased or pathogenic cells. Moreover, nanoparticles intended for human administration must be designed to interact with, and ideally leverage, a living host environment. Inspired by nature, we use peptides to transfer biological trafficking properties to synthetic nanoparticles to achieve targeted delivery of payloads. In this talk, development of nanoscale materials will be presented with a particular focus on applications to three outstanding health problems: bacterial infection, cancer detection, and traumatic brain injury. A biodegradable nanoparticle carrying a peptide toxin trafficked to the bacterial surface has antimicrobial activity in a pneumonia model. Trafficking of a tumor-homing nanoprobes sensitively detects cancer via a high-contrast time-gated imaging system. A neuron-targeted nanoparticle carrying siRNA traffics to neuronal populations and silences genes in a model of traumatic brain injury. Unique combinations of material properties that can be achieved with nanomaterials provide new opportunities in translational nanomedicine. This framework for constructing nanomaterials that leverage bio-inspired molecules to traffic diagnostic and therapeutic payloads can contribute on better understanding of living systems to solve problems in human health.

• BMB Reports
• /
• v.46 no.3
• /
• pp.169-174
• /
• 2013

The human $B_{12}$ trafficking chaperone hCblC is well conserved in mammals and non-mammalian eukaryotes. However, the C-terminal ~40 amino acids of hCblC vary significantly and are predicted to be deleted by alternative splicing of the encoding gene. In this study, we examined the thermostability of the bovine CblC truncated at the C-terminal variable region (t-bCblC) and its regulation by glutathione. t-bCblC is highly thermolabile ($T_m={\sim}42^{\circ}C$) similar to the full-length protein (f-bCblC). However, t-bCblC is stabilized to a greater extent than f-bCblC by binding of reduced glutathione (GSH) with increased sensitivity to GSH. In addition, binding of oxidized glutathione (GSSG) destabilizes t-bCblC to a greater extent and with increased sensitivity as compared to f-bCblC. These results indicate that t-bCblC is a more sensitive form to be regulated by glutathione than the full-length form of the protein.

• Journal of the Korea Institute of Information Security & Cryptology
• /
• v.26 no.2
• /
• pp.397-404
• /
• 2016

Illegal and harmful contents on the Internet has been an issue and been increased in Korea. They are often posted on the billboard and website of small enterprise and government office. Those illegal and harmful contents can relate to crime and suspicious activity, so, we need a detection system. However, to date the detection itself has been conducted manually by a person. In this paper, we develop an automated URL detection scheme for detecting a drug trafficking by using Google. This system works by analyzing the frequently used keywords in a drug trafficking and generate a keyword dictionary to store words for future search. The suspected drug trafficking URL are automatically collected based on the keyword dictionary by using Google search engine. The suspicious URL can be detected by classifying and numbering each domain from the collection of the suspected URL. This proposed automated URL detection can be an effective solution for detecting a drug trafficking, also reducing time and effort consumed by human-based URL detection.

• Molecules and Cells
• /
• v.44 no.10
• /
• pp.758-769
• /
• 2021

Calcium homeostasis modulator 1 (CALHM1) is a membrane protein with four transmembrane helices that form an octameric ion channel with voltage-dependent activation. There are four conserved cysteine (Cys) residues in the extracellular domain that form two intramolecular disulfide bonds. We investigated the roles of C42-C127 and C44-C161 in human CALHM1 channel biogenesis and the ionic current (I_CALHM1). Replacing Cys with Ser or Ala abolished the membrane trafficking as well as I_CALHM1. Immunoblotting analysis revealed dithiothreitol-sensitive multimeric CALHM1, which was markedly reduced in C44S and C161S, but preserved in C42S and C127S. The mixed expression of C42S and wild-type did not show a dominant-negative effect. While the heteromeric assembly of CALHM1 and CALHM3 formed active ion channels, the co-expression of C42S and CALHM3 did not produce functional channels. Despite the critical structural role of the extracellular cysteine residues, a treatment with the membrane-impermeable reducing agent tris(2-carboxyethyl) phosphine (TCEP, 2 mM) did not affect I_CALHM1 for up to 30 min. Interestingly, incubation with TCEP (2 mM) for 2-6 h reduced both I_CALHM1 and the surface expression of CALHM1 in a time-dependent manner. We propose that the intramolecular disulfide bonds are essential for folding, oligomerization, trafficking and maintenance of CALHM1 in the plasma membrane, but dispensable for the voltage-dependent activation once expressed on the plasma membrane.

• Journal of the Korea Academia-Industrial cooperation Society
• /
• v.12 no.1
• /
• pp.312-317
• /
• 2011

Vanilloid receptor TRPV1 (known as capsaicin channel, transient receptor potential vanilloid 1) is known to be a key protein in the pain signal transduction. However, the proteins controlling the activity of the channel are not much known yet. Recently mouse Rab11-FIP3 (Rab11-family interaction protein 3) was found and reported to interact with rat TRPV1. Rab11 has been shown to play a key role in a variety of cellular processes including plasma membrane recycling, phagocytosis, and transport of secretory proteins from the trans-Golgi network. Therefore, Rab11-FIP3 was proposed to be involved in the membrane trafficking of TRPV1. In this study, the unreported rat Rab11-FIP3 was yet cloned in order to show the specific interaction of the TRPV1 and Rab11-FIP3 in the same species of rat and to examine the membrane trafficking of TRPV1. The result showed that rat Rab11-FIP3 is expected to have 489 amino acids and showed 80% identity with that of human and over 90% identity with that of mouse. Rab11-FIP3 was found to be expressed in heart, brain, kidney, testis using northern and western blot analyses. We also found that rat Rab11-FIP3 was colocalized with rat TRPV1 but not with TRPV2 of same family in the rat brain by using immunohistochemistry showing that two proteins interact specifically, suggesting the role of Rab11-FIP3 in the membrane trafficking.

• BMB Reports
• /
• v.51 no.9
• /
• pp.425-426
• /
• 2018

As highly conserved signaling cascades of multicellular organisms, Wnt and Hippo pathways control a wide range of cellular activities, including cell adhesion, fate determination, cell cycle, motility, polarity, and metabolism. Dysregulation of those pathways are implicated in many human diseases, including cancer. Similarly to ${\beta}-catenin$ in the Wnt pathway, the YAP transcription co-activator is a major player in Hippo. Although the intracellular dynamics of YAP are well-known to largely depend on phosphorylation by LATS and AMPK kinases, the molecular effector of YAP cytosolic translocation remains unidentified. Recently, we reported that the Dishevelled (DVL), a key scaffolding protein between canonical and non-canonical Wnt pathway, is responsible for nuclear export of phosphorylated YAP. The DVL is also required for YAP intracellular trafficking induced by E-cadherin, ${\alpha}-catenin$, or metabolic stress. Note that the p53/LATS2 and LKB1/AMPK tumor suppressor axes, commonly inactivated in human cancer, govern the reciprocal inhibition between DVL and YAP. Conversely, loss of the tumor suppressor allows co-activation of YAP and Wnt independent of epithelial polarity or contact inhibition in human cancer. These observations provide novel mechanistic insight into (1) a tight molecular connection merging the Wnt and Hippo pathways, and (2) the importance of tumor suppressor contexts with respect to controlled proliferation and epithelial polarity regulated by cell adhesion.

• The Korean Journal of Physiology and Pharmacology
• /
• v.5 no.5
• /
• pp.367-371
• /
• 2001

The chromosome 7-linked long QT syndrome (LQT2) is caused by mutations in the human ether-a- go-go-related gene (HERG) that encodes the rapidly activating delayed rectifier $K^+$ current, $I_{Kr},$ in cardiac myocytes. Different types of mutations have been identified in various locations of HERG channel. One of the mechanisms for the loss of normal channel function is due to membrane trafficking of channel protein. The decreased channel function in some deletion mutants appears to be due to loss of coupling with wild type HERG to form the functional channel as the tetramer. Most of missense mutants with few exceptions could interact with wild type HERG to form functional tetramer and caused dominant negative suppression with co-injection with wild type HERG showing variable effects on current amplitude, voltage dependence, and kinetics of activation and inactivation. Two missense mutants at pore regions of HERG found in Japanese LQT2 (A614V and V630L) showed accentuated inward rectification due to a negative shift in steady-state inactivation and fast inactivation. One mutation in S4 region (R534C) produced a negative shift in current activation, indicating the S4 serving as the voltage sensor and accelerated deactivation. The C-terminus mutation, S818L, could not express the current by mutant alone and did not show dominant negative suppression with co-injection of equal amount of wild type cRNA. Co-injection of excess amount of mutant with wild type produced dominant negative suppression with a shift in voltage dependent activation. Therefore, multiple mechanisms are involved in different mutations and functional abnormality in LQT2. Further characterization with the interactions between various mutants in HERG and the regulatory subunits of the channels (MiRP1 and minK) is to be clarified.