• Title/Summary/Keyword: outer membrane proteins

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Plastoglobule in chloroplast and its role in prenylquinone metabolism (엽록체 지질 소기관의 기능과 지질대사에서의 역할)

  • Kim, Hyun Uk;Kim, Eun-Ha;Lee, Kyeong-Ryeol;Jung, Su-Jin;Roh, Kyung Hee;Kim, Jong-Bum
    • Journal of Plant Biotechnology
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    • v.40 no.3
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    • pp.125-134
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    • 2013
  • Lipid droplets called plastoglobules are present in all plastid types. In chloroplasts, they are surrounded by the outer lipid monolayer from and connected to thylakoid membrane. The plastoglobule core contains the neutral lipids, which includes prenylquinones, triacylglycerols, and carotenoids. During stress and various developmental stages such as senescence, the size and number of plastoglobules increase due to the accumulation of lipids. Plastoglobules proteome revealed the presence of metabolic enzymes as well as structural proteins, plastoglobulins/fibrillins. Among the metabolic enzymes, the tocopherol cyclase, VTE1 and the NADPH quinine dehydrogenase, NDC1 have demonstrated that these participate in isoprenoid lipid metabolic pathways at the plastoglobule, notably in the metabolism of prenylquinones (tocopherol, plastoquinol and phylloquinone).

Motility and Chemotaxis in the Lyme Spirochete Borrelia burgdorferi: Role in Pathogenesis (라임병 원인 스피로헤타 Borrelia burgdorferi의 운동성과 주화성: 발병기전에서의 역할)

  • Yoo, Ah Young;Kang, Ho Young;Moon, Ki Hwan
    • Journal of Life Science
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    • v.28 no.5
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    • pp.627-637
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    • 2018
  • Motility and chemotaxis are crucial for disease development in many motile pathogens, including spirochetes. In many bacteria, motility is provided by flagella rotation, which is controlled by a chemotaxis-signal-transduction system. Thus, motility and chemotaxis are inextricably linked. Spirochetes are a unique group of bacteria with distinctive flat-wave morphology and corkscrew-like locomotion. This unusual motility pattern is believed to be important for efficient motility within the dense tissues through which these spirochetes preferentially disseminate in a host. Unlike other externally flagellated bacteria-where flagella are in the ambient environment-the flagella of spirochetes are enclosed by the outer membrane and thus are called periplasmic flagella or endoflagella. Although motilityand chemotaxis-associated genes are well studied in some bacteria, the knowledge of how the spirochete achieves complex swimming and the roles of most of the putative spirochetal chemotaxis proteins are still elusive. Recently, cutting-edge imaging methods and unique genetic manipulations in spirochetes have helped to unravel the mystery of motility and chemotaxis in spirochetes. These contemporary advances in understanding the motility and chemotaxis of spirochetes in a host's persistence and disease process are highlighted in this review.

Helicobacter pylori Chaperone-Like Protein CagT Plays an Essential Role in the Translocation of CagA into Host Cells

  • Ding, Honglei;Zeng, Hao;Huang, Linping;Dong, Yandong;Duan, Yijun;Mao, Xuhu;Guo, Gang;Zou, Quanming
    • Journal of Microbiology and Biotechnology
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    • v.22 no.10
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    • pp.1343-1349
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    • 2012
  • Most of the Helicobacter pylori strains containing the cag pathogenicity island (PAI) have been associated with more severe gastric disease in infected humans. The cag PAI is composed of 27 proteins, and some of the components are required for CagA translocation into host cells as well as induction of proinflammatory cytokines, such as interleukin-8 (IL-8); however, the exact function of most of the components remains unknown or poorly characterized. In this study, we demonstrated that CagT (HP0532), which is an essential structural component of the cag PAI apparatus, plays an important role in the translocation of CagA into host epithelial cells. In addition to being located on the bacterial surface, CagT is also partially localized in the inner membrane, where it acts as a chaperone-like protein and promotes CagA translocation. However, CagT secretion was not detected by immunoprecipitation analysis of cell culture supernatants. Meanwhile, CagT was related to the introduction of IL-8 of the host cell. These results suggest that CagT is expressed on both the inner and outer bacterial membranes, where it serves as a unique type IV secretion system component that is involved in CagA secretion and cag PAI apparatus assembly.

Immunocytochemical Localization of Parvalbumin and Calbindin-D 28K in Monkey Dorsal Lateral Geniculate Nucleus (원숭이 외측슬상체배측핵에서 칼슘결합단백 Parvalbumin과 Calbindin-D 28K의 분포)

  • Ko, Seung-Hee;Bae, Choon-Sang;Park, Sung-Sik
    • Applied Microscopy
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    • v.24 no.4
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    • pp.61-77
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    • 1994
  • The calcium-binding proteins (CaBP), parvalbumin (PV) and calbindin-D 28K (calbindin) are particularly abundant and specific in their distribution, and present in different subsets of neurons in many brain regions. Although their physiological roles in the neurons have not been elucidated, they are valuable markers of neuronal subpopulations for anatomical and developmental studies. This study is designed to characterize dorsal lateral geniculate nucleus (dLGN) neurons and axon terminals in terms of differential expression of immunoreactivity (IR) for two well-known CaBPs, PV and calbindin. The experiments were carried out on 6 adult monkeys. Monkeys were perfused under deep Nembutal anesthesia with 2% paraformaldehyde and 0.2% glutaraldehyde in 0.1M phosphate buffer. After removal, the brains were postfixed for 6-8 hr in 2% paraformaldehyde at $4^{\circ}C$ and infiltrated with 30% sucrose at $4^{\circ}C$. Thereafter, they were frozen in dry ice. Serial sections of the thalamus, at $20{\mu}m$, were made in the frontal plane with a sliding microtome. The sections were stained for PV and calbindin with indirect immunocytochemical methods. For electron microscopy, after infiltration with 30% sucrose the blocks of thalamus were serially sectioned at $50{\mu}m$ with a Vibratome in the coronal plane and stained immediately by indirect ABC methods without Triton X-100 in incubation medium. Stained sections were postfixed in 0.2% osmium tetroxide, dehydrated and flat-embedded in Spurr resin. The block was then trimmed to contain only a selected lamina or interlaminar space. The dLGN proper showed strong PV IR in fibers in all laminae and interlaminar zones. Particularly dense staining was noted in layers 1 and 2 that contain many stained fibers from optic tract. Neuronal cell body stained with PV was concentrated only in the laminae. In these laminae staining was moderate in cell bodies of all large and medium-sized neurons, and was strong in cell bodies of some small neurons together with their processes. Calbindin IR was marked in the neuronal cell body and neuropil in the S layers and interlaminar zones whereas moderate in the neuropil throughout the nucleus. Regional difference in distribution of PV and calbindin IR cell is distinct; the former is only in the laminae and the latter in both the S layer and interlaminar space. The CaBP-IR elements were confined to about $10{\mu}m$ in depth of Vibratome section. The IR product for CaBP was mainly associated with synaptic vesicle, pre- and post-synaptic membrane, and outer mitochondrial membrane and along microtubule. PV-IR was noted in various neuronal elements such as neuronal soma, dendrite, RLP, F, PSD and some myelinated or unmyelinated axons, and was not seen in the RSD and glial cells. Only a few neuronal components in dLGN was IR for calbindin and its reaction product was less dense than that of PV, and scattered throughout cytoplasm of soma of some relay neurons, and was also persent in some dendrite, myelinated axons and RLP. The RSD, F, PSD and glial elements were always non-IR for calbindin. Calbindin labelled RLP were presynaptic to unlabeled dendrite or dendritic spine and PSD. Calbindin-labeled dendrite of various sizes were always postsynaptic to unlabeled RSD, RLP or F. From this study it is suggested that dLGN cells of different functional systems and their differential projection to the visual cortex can be distinguished by differential expression of PV and calbindin.

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Expression of UT-A in Rat Kidney: Ultrastructural Immunocytochemistry (흰쥐 콩팥에서 요소운반체-A의 발현: 미세구조적 면역세포화학법)

  • Lim, Sun-Woo;Jung, Ju-Young;Kim, Wan-Young;Han, Ki-Hwan;Cha, Jung-Ho;Chung, Jin-Woong;Kim, Jin
    • Applied Microscopy
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    • v.32 no.2
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    • pp.91-105
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    • 2002
  • Urea transport in the kidney is mediated by a family of transporter proteins that includes renal urea transporters (UT-A) and erythrocyte urea transporters (UT-B). The cDNA of five isoforms of rat UT-A, UTA1, UT-A2, UT-A3, UT-A4, and UT-A5 have been cloned. The purpose of this study was to examine the expression of UT-A (L194), which marked UT-A1, UT-A2 and UT-A4. Male Sprague-Dawley rats, weighing approximately 200 g, were divided into three group: control rats had free access to water, dehydrated rats were deprived of water for 3 d, and water loaded rats had free access to 3% sucrose water for 3 d before being killed. The kidneys were preserved by in vivo perfusion through the abdominal aorta with the 2% paraformaldehyde-lysine- periodate (PLP) or 8% paraformaldehyde solution for 10 min. The sections were processed for immunohistochemical studies using pre-embedding immunoperoxidase method and immunogold method. In the normal rat kidney, UT-A1 was expressed intensely in the cytoplasm of the inner medullary collecting duct (IMCD) cell and UT-A2 was expressed on the plasma membrane of the terminal portion of the shortloop descending thin limb (DTL) cells (type I epithelium) and of the long-loop DTL cells (type II epithelium) in the initial part of the inner medulla. Immunoreactivity for UT-A1 in the IMCD cells, was decreased in dehydrated animals whereas strongly increased in water loaded animals compared with control animals. In the short-loop DTL, immunoreactivity for UT-A2 was increased in intensity in both dehydrated and water loaded groups. However, in the long-loop DTL of the outer part of the inner medulla, immunoreactivity for UT-A2 was markedly increase in intensity in dehydrated group, but not in water loaded group. In conclusion, in the rat kidney, UT-A1 is located in the cytoplasm of IMCD cells, whereas UT-A2 is located in the plasma membrane of both the short-and long-loop DTL cells. Immunohistochemistry studies revealed that UT-A1 and UT-A2 may have a different role in urea transport and are regulated by different mechanisms.

Effect of Phytoncide on Porphyromonas gingivalis (P. gingivalis에 대한 피톤치드의 항균효과)

  • Kim, Sun-Q;Shin, Mi-Kyoung;Auh, Q-Schick;Lee, Jin-Yong;Hong, Jung-Pyo;Chun, Yang-Hyun
    • Journal of Oral Medicine and Pain
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    • v.32 no.2
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    • pp.137-150
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    • 2007
  • Trees emit phytoncide into atmosphere to protect them from predation. Phytoncide from different trees has its own unique fragrance that is referred to as forest bath. Phytoncide, which is essential oil of trees, has microbicidal, insecticidal, acaricidal, and deodorizing effect. The present study was performed to examine the effect of phytoncide on Porphyromonas gingivalis, which is one of the most important causative agents of periodontitis and halitosis. P. gingivalis 2561 was incubated with or without phytoncide extracted from Hinoki (Chamaecyparis obtusa Sieb. et Zucc.; Japanese cypress) and then changes were observed in its cell viability, antibiotic sensitivity, morphology, and biochemical/molecular biological pattern. The results were as follows: 1. The phytoncide appeared to have a strong antibacterial effect on P. gingivalis. MIC of phytoncide for the bacterium was determined to be 0.008%. The antibacterial effect was attributed to bactericidal activity against P. gingivalis. It almost completely suppressed the bacterial cell viability (>99.9%) at the concentration of 0.01%, which is the MBC for the bacterium. 2. The phytoncide failed to enhance the bacterial susceptibility to ampicillin, cefotaxime, penicillin, and tetracycline but did increase the susceptibility to amoxicillin. 3. Numbers of electron dense granules, ghost cell, and vesicles increased with increasing concentration of the phytoncide, 4. RT-PCR analysis revealed that expression of superoxide dismutase was increased in the bacterium incubated with the phytoncide. 5. No distinct difference in protein profile between the bacterium incubated with or without the phytoncide was observed as determined by SDS-PAGE and immunoblot. Overall results suggest that the phytoncide is a strong antibacterial agent that has a bactericidal action against P. gingivalis. The phytoncide does not seem to affect much the profile of the major outer membrane proteins but interferes with antioxidant activity of the bacterium. Along with this, yet unknown mechanism may cause changes in cell morphology and eventually cell death.