• The Korean Journal of Zoology
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• v.28 no.2
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• pp.85-98
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• 1985

The present study was carried out light and electron microscopic analysis of the structures of the tritocerebral neurons in butterfly (Pieris rapae Linne) from Insecta. We have summarized our morphological analyses as follows: In insecta, tritocerebrum of butterfly shows tentatively classified 6 neuronal types without any arrangement of cell layers. Type I cells with long oval or spindle shape are the largest out of 6 kinds. The nucleus contains a small amount of chromatin. In the large volume of cytoplasm there contained rich cell organelles except granular endoplasmic reticulum. Type II cells are smaller than type I neurons, but their ultrastructural features are similar to type I neuron. They have well-developed granular endoplasmic reticulum. Type III cells are spherical or triangular and smaller than type I neuron with spherical nuclei. Cell organelles are mostly prominent, esp., mitochondria, ribosomes and fine fibrils which are arranged in periphery of the cytoplasm.

• The Korean Journal of Zoology
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• v.11 no.1
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• pp.5-12
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• 1968

The membrane structures were electron microscopically studied in the elongating lens fibers of the regenerating lens of adult Triturus pyrrhogaster. Observations were focused on the endoplasmic reticulum and mitochondria. The endoplasmic reticulum developed in the vicinity of the nucleus with active blebbing of the outer membrane. At the same time, the concentration of mitochondria around the rough-surfaced endoplasmic reticulum near by the nucleus was always observed. Both endoplasmic reticulum and mitochondrion undergo disintegration in the apical portion apart from the nucleus. Some considerations were discussed with reference to published data.

• The Korean Journal of Zoology
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• v.12 no.4
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• pp.114-122
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• 1969

Electron microscopic examination of the liver and heart tissues of methylene blue-treated rats before gamma-irradiation was observed in this study. 1. It was observed severe alteration and degeneration of organelles: accumulation of glycogen particles, severe swollen mitochondria, and broken endoplasmic reticulum in liver tissue of saline-treated rat(control) opposed by emthylene blue-treated rat at 64 and 212 hours following gamma-irradiation. 2. Heart muscles of both methylene blue-treated and saline-treated rats showed no significant alterations, but it was observed that slightly elongated mitochondria with broken cristae and some of vacuoles as well as increased glycogen particles in sarcoplasmic reticulum at 212 hours following gamma-irradiation. 3. It may be considered that methylene blue greatly reduces the sensitivities of rats to gamma-irradiation.

• Herbal Formula Science
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• v.26 no.4
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• pp.307-318
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• 2018

Objectives : Endoplasmic reticulum (ER) stress designates cellular responses to the accumulation of misfolded and unfolded proteins in ER, which is related to a variety of liver diseases. Present study investigated the inhibitory effects of Litsea japonica flesh water extract (LJE) aganist ER stress. Methods : After HepG2 cells were pretreated with LJE and subsequently exposed to tunicamycin (Tm) or thapsigargin (Tg), expression of C/EBP homologous protein (CHOP), glucose regulated protein 78 kDa (GRP78), asparagine synthetase (ASNS), and endoplasmic reticulum DnaJ homologue 4 (ERDJ4) were determined by immunoblot and real-time PCR analysis. Three canonical signaling pathways in response to ER stress were examined to explore molecular mechanisms involved. Results : Pretreatment of 1 mg/mL LJE inhibited Tm- or Tg-induced CHOP expression, while L. japonica fruit water extract did not. In addition, LJE decreased the levels of GRP78, ASNS, and ERDJ4 mRNA by Tm. Moreover, phosphorylations of eukaryotic translation initiation factor $2{\alpha}$ and inositol-requiring enzyme 1, expression of nuclear form of activating transcription factor $6{\alpha}$, and transactivation of ER stress response element- and unfolded protein response element-harboring luciferase activities were inhibited by LJE pretreatment. Conclusions : Present results suggest that LJE would be a candidate to prevent or treat ER stress-mediated liver injuries.

• Proceedings of the Korean Society of Life Science Conference
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• 2005.09a
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• pp.25-26
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• 2005

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2001.10a
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• pp.30-32
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• 2001

no Abstract, See Full Text

• Proceedings of the Korean Society of Life Science Conference
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• 2006.09a
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• pp.21-21
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• 2006

• Molecules and Cells
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• v.42 no.6
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• pp.501-501
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• 2019

• YAKHAK HOEJI
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• v.38 no.1
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• pp.12-19
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• 1994

Capsaicin(8-methyl-N-vanillyl-6-nonenamide) is the principal pungent component of Capsicum fruits. This work is directed to the capsaicin-hydrolyzing enzyme playing a key role in the rate limiting and critical step of capsaicin metabolism. In order to get precise information on the enzyme's subcellular location, rat liver homogenate was divided into six subcellular fractions by differential centrifugation technique: crude nuclear pellet, PNS(post nuclear supernatant) fraction, lysosomal pellet, cytosol, Tris wash fraction, micrisomes. Capsaicin-hydrolysing enzyme activity was analysed by high performance liquid chromatography(HPLC). This enzyme was found at the highest specific activity in the microsomal fraction and co-distributed with marker enzymes of the endoplasmic reticulum, NADPH-cytochrome c reductase and nucleoside diphosphatase. This is compatible with the result of ninhydrin color reaction of vanillylamine, primary metabolite of capsaicin hydrolysis, on thin layer chromatography(TLC). This enzyme is most active at pH $8.0{\sim}9.0$. Definite subcellular location of this enzyme will make it easy to proceed with further study.

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2003.10a
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• pp.78-79
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• 2003

To further understanding of the role of calreticulin in insects, we have isolated a cDNA of calreticulin from silkworm, Bombyx mori. The cDNA encodes a 398 amino acid residues of B. mori calreticulin with endoplasmic reticulum retentional HDEL motif at its C-terminus, and a predicted molecular mass of 45801 Da. The B. mori calreticulin shows high protein homology with those of G mellonella (88%), A. aegypti (71%) and H. sapiens (63%). (omitted)