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RISS 인기검색어
- 검색키워드
- 저자 : Hyuno Kang (검색결과 6 건)
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Kang, Hyuno,Kim, Na-Young,Kim, Gee-Sung,Ahn, Ki-Heung,Lee, Bong-Hee 한국곤충학회 1997 Entomological Research Vol.27 No.3
The numerical, locational and structural changes of the neurons reacting with an antiserum raised against a neuropeptide, locustatachykinin-I (Lom TK I) were investigated in the ventral ganglia of the common cutworm, Spodoptera litura, during postembryonic development. In the first instar larva, one pair of the Lom TK I- immunoreactive (Lom TK I-IR) neurons are included only in the mesothoracic ganglion of the ventral nerve cord. In the second instar larva, suboesophageal, prothoracic, mesothoracic, metathoracic, and sixth abdominal ganglia contain about 2 to 14 Lom TK I- IR neurons, while all the ganglia of the ventral nerve cord in the third instar larva have increased number of the Lom TK I- IR neurons. Each ganglion of the fourth, fifth and sixth instar larvae includes the largest number of the Lom TK I- IR neurons. Thereafter, however, smaller number of the Lom TK I- IR neurons are included in each ganglion than in late larval stages. Most of the Lom TK I- IR neurons show bilateral localization in each ganglion during postembryonic development, whereas extremly small number of the Lom TK I-IR neurons are unpaired, median neurons in all metathoracic ganglia from the second instar larva to the adult, and the fifth abdominal ganglia of the 3- day- old pupa to the adult. Most of the Lom TK I-IR neurons sre the interneurons, while part of them are afferent or efferent. The extrinsic Lom TK I- IR fibers form two pairs of longitudinal fiber tracts in the ventral nerve cord, especially in each ventral ganglion. The Lom TK I- IR fibers projected from the neurons in various ventral ganglia form the commissural structures between neuropil both sides.
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Roshanzadeh, Amir,Kang, Hyuno,You, Sung-Hwan,Park, Jaehong,Khoa, Nguyen Dang,Lee, Dong-Hyun,Kim, Geun-Joong,Kim, Eung-Sam Elsevier 2019 Biosensors & bioelectronics Vol.146 No.-
<P><B>Abstract</B></P> <P>Nicotinamide adenine nucleotide phosphate (NADPH) has been known to be involved in the multiple pathways of cell metabolism. However, conventional quantification assays for NADPH have required breaking down the cell membranes of around one million cells per assay, and monitoring NADPH flux in living cells has been limited by a few available tools. Here, we visualized NADPH levels in human cervical cancer cells HeLa using metagenome-derived blue fluorescent protein (mBFP), which specifically binds to NADPH and enhances the intrinsic fluorescence of NADPH up to 10-fold when imaged by two-photon microscopy to reduce photodamage. Adding an oxidizing agent such as diamide to HeLa cells that expressed mBFP led to an immediate decrease of intracellular NADPH depending on glucose availability in culture media. Furthermore, inhibiting glucose-6-phosphate dehydrogenase (G6PD) in the pentose phosphate pathway with dehydroandrosterone (DHEA) and knockdown of G6PD transcripts gradually decreased NADPH when diamide was added to living cells. These results demonstrate that introducing a bacterial mBFP gene into mammalian cells is a straightforward approach to monitoring intracellular NADPH flux in real time at the single-cell level. Moreover, this strategy can be expanded to tracking the spatio-temporal changes in NADPH even in single-cell organelles such as mitochondria and chloroplasts, which will allow us to more precisely assess the efficacy of biochemically or biophysically metabolic perturbations in animal and plant cells.</P> <P><B>Highlights</B></P> <P> <UL> <LI> Bacterial mBFP is a functionally reporter protein for the monitoring of NADPH in live mammalian cells. </LI> <LI> mBFP specifically binds to NADPH and enhances the NADPH's fluorescence up to 10-fold in cells. </LI> <LI> mBFP sensor allows a long-term monitoring of intracellular NADPH flux in real time with TPM. </LI> </UL> </P>
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<i>Lactobacillus acidophilus</i> NS1 attenuates diet-induced obesity and fatty liver
Park, Sung-Soo,Lee, Yeon-Joo,Song, Sooyeon,Kim, Boyong,Kang, Hyuno,Oh, Sejong,Kim, Eungseok Journal of Endocrinology, Ltd. [etc.] 2018 The Journal of endocrinology Vol. No.
<P>Obesity is a major threat to public health, and it is strongly associated with insulin resistance and fatty liver disease. Here, we demonstrated that administration of Lactobacillus acidophilus NS1 (LNS1) significantly reduced obesity and hepatic lipid accumulation, with a concomitant improvement in insulin sensitivity, in high-fat diet (HFD)-fed mice. Furthermore, administration of LNS1 inhibited the effect of HFD feeding on the SREBP-1c and PPAR alpha signaling pathways and reduced lipogenesis with an increase in fatty acid oxidation in ex vivo livers from HFD-fed mice. These LNS1 effects were confirmed in HepG2 cells and ex vivo livers by treatment with LNS1 culture supernatant (LNS1-CS). Interestingly, AMPK phosphorylation and activity in the liver of HFD-fed mice were increased by administration of LNS1. Consistently, chemical inhibition of AMPK with compound C, a specific inhibitor of AMPK, dramatically reduced the effect of LNS1-CS on lipid metabolism in HepG2 cells and ex vivo livers by modulating the SREBP-1c and PPAR alpha signaling pathways. Furthermore, administration of LNS1 to HFD-fed mice significantly improved insulin resistance and increased Akt phosphorylation in the liver, white adipose tissue and skeletal muscle. Together, these data suggest that LNS1 may prevent diet-induced obesity and related metabolic disorders by improving lipid metabolism and insulin sensitivity through an AMPK. SREBP-1c/PPAR alpha signaling pathway.</P>
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Park, Junghee,Han, Ji-Hye,Myung, Seung-Hyun,Kang, Hyuno,Cho, Ju-Yeon,Kim, Tae-Hyoung Academic Press 2019 Biochemical and biophysical research communication Vol. No.
<P><B>Abstract</B></P> <P>Noxa is a weak apoptosis activator consisting of a BH3 domain and a mitochondrial-targeting domain (MTD). BH3 binds Mcl-1 and Bcl2A1 and inactivates their anti-apoptotic activities, while MTD delivers BH3 to mitochondria. Previously we revealed that MTD may also function as an inducer of necrosis via conjugation with octa-arginine, which induces cytosolic Ca<SUP>2+</SUP> influx from mitochondria. However, the mechanism(s) underlying this process has not been elucidated yet. Here, we show that calcium influx induced by an MTD peptide fused with octa-arginine residue (R8:MTD) originates not only from mitochondria but also from the extracellular space. However, calcium spikes were not sufficient for necrosis. R8:MTD induced mitochondrial permeability transition pore opening, fragmentation, and swelling. These mitochondrial events induced by MTD appeared to be necessary for necrosis induction, since DIDS, a VDAC inhibitor, inhibited the mitochondrial swelling and cell death induced by MTD. We show that R8:MTD disrupted endoplasmic reticulum (ER) structures but not peroxisomes or Golgi, indicating that R8:MTD causes necrosis by inducing ER events as well.</P> <P><B>Highlights</B></P> <P> <UL> <LI> MTD peptide fused with 8-arginine (R8:MTD) induced necrotic cell death. </LI> <LI> R8:MTD induced Ca<SUP>2+</SUP> influx from mitochondria and extracellular space. </LI> <LI> MTD interacted with VDAC, and induced mitochondrial catastrophe. </LI> <LI> VDAC inhibitor DIDS inhibited cell death and mitochondrial disruption. </LI> <LI> R8:MTD disrupted ER where VDAC was expressed. </LI> </UL> </P>
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