• Ocean and Polar Research
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• v.34 no.2
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• pp.137-149
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• 2012

Hemocyte parameters of the wild Pacific oyster Crassostrea gigas inhabiting intertidal zones in small bays (Gwangyang and Jinhae Bay) on the southern coast of Korea were evaluated using flow cytometry and neutral red retention (NRR) assay. Morphological features, cell count, mortality, DNA damage, phagocytosis, and lysosomal membrane stability of hemocytes were analyzed. Three types of hemocytes were identified in the oyster hemolymph: granulocytes, hyalinocytes, and blast-like cells. Immune related functions of hemocyte including phagocytosis and lysosomal membrane stability were significantly different among the study areas (P<0.05), while cell count, mortality, and DNA damage of hemocytes were not significantly different. In Gwangyang Bay, phagocytosis of granulocytes and lysosomal membrane stability of oyster hemocytes inhabiting inside bay were significantly lower than those of oyster hemocytes in outside bay (P<0.05), indicating that oysters in inside bay of Gwangyang were relatively suppressed the immunological function in hemocytes. Contrary to Gwangyang Bay, immune parameters of oyster hemocytes in Jinhae Bay not showed the difference between sampling sites. In conclusion, flow cytometry and NRR assay using oyster hemocyte has a powerful tool to investigate the cell level in a short time due to no-preprocessing of material.

• Fisheries and Aquatic Sciences
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• v.5 no.4
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• pp.263-270
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• 2002

The Pacific oysters, Crassostrea gigas, were stressed with different concentrations of benzo(a) pyrene and depurated to determine the hemocyte lysosomal membrane stability and hydrolytic enzymatic activity as a biomarker candidate to the chemical, using NRR (neutral red retention) and API ZYM System, respectively. The membrane damage measured as NRR decrease was significant with the increase of chemical concentration and exposure time (P<0.05), providing a possible tool for biomarker. Interestingly, the control showed intrinsic stress probably due to captive life in the laboratory, and a recovering trend was also found during the depuration. The benzo(a)pyrene-exposed oysters showed increased enzyme activities in alkaline phosphatase, esterase (C4), acid phosphatase, naphthol-AS-BI-phospho­hydrolase, $\beta$-galactosidase, $\beta$-glucuronidase, and N-acetyl- $\beta$-glucosaminidase. Of them, only two enzymes, acid phosphatase and alkaline phosphatase, showed some potential available for the generation of enzymatic biomarker in the oyster. The results are suggestive of the potential availability of the cellular and enzymatic properties as a biomarker. However, considering that a robust biomarker should be insensitive to natural stress coming from normal physiological variation, but sensitive to pollutants, a concept of intrinsic stress the animal possesses should be taken into consideration. This reflects the necessity of further research on the intrinsic stress affecting the cellular and enzymatic properties of the chemical­stressed oysters prior to using the data as a biomarker.

• Ocean and Polar Research
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• v.34 no.2
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• pp.151-163
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• 2012

Digestive cells of the bivalves have a highly developed lysosomal system and the system is known to be sensitive to changes in environmental qualities. In this study, we measured lysosomal responses of the digestive cells in wild oyster, Crassostrea gigas using frozen section. Oysters were collected in June 2010 from intertidal areas in the inner and outer bay of Gwangyang off the south coast of Korea. From the tissue sections, we measured the digestive cell lysosomal membrane stability (LMS), level of neutral lipids (NL), lipofuscin (LF) and the digestive gland atrophy (DGA). The DGA and condition index of oysters from the inner bay were significantly lower (P<0.05). The statistical test indicated that LMS levels of oysters in the inner bay and the outer bay were not significantly different since a shorter activity was displayed by oysters from the inner bay than that of oysters in outer bay. The LF deposition level of the oysters in the inner bay displayed significantly higher levels than the outer bay (P<0.05). In contrast, the NL accumulation measured from oysters in outer bay was significantly higher than the level observed in the inner bay (P<0.05). Different levels of DGA and LF that were observed in the inner and outer bays were thought to be associated to different level of environmental contamination and these two assays are considered to be good biomarkers.

• Proceedings of the Korean Society of Fisheries Technology Conference
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• 2003.05a
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• pp.389-390
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• 2003

리소즘은 가수분해효소와 같은 각종 효소를 저장하고 있고, 이러한 효소는 지방, 지질 및 단백질에 특이적으로 반응하여 세포내로 들어오는 이들 물질을 분해하는 기능을 담당한다. 또한 리소좀은 여러 가지 Xenobiotics에도 반응하는 것으로 알려지고 있다(Lowe et al., 1995, Shepard and Bradley, 2000), 리소즘막의 손상은 결국 Xenobiotic의 세포내 출입의 조절능을 상실하게 되고, 나아가 ATP-dependent proton pump의 손상을 일으키게 된다(Lowe et al., 1992). (중략)

• Molecules and Cells
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• v.41 no.4
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• pp.320-330
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• 2018

${\delta}$-Catenin, a member of the p120-catenin subfamily of armadillo proteins, reportedly increases during the late stage of prostate cancer. Our previous study demonstrates that ${\delta}$-catenin increases the stability of EGFR in prostate cancer cell lines. However, the molecular mechanism behind ${\delta}$-catenin-mediated enhanced stability of EGFR was not explored. In this study, we hypothesized that ${\delta}$-catenin enhances the protein stability of EGFR by inhibiting its lysosomal degradation that is mediated by c-casitas b-lineage lymphoma (c-Cbl), a RING domain E3 ligase. c-Cbl monoubiquitinates EGFR and thus facilitates its internalization, followed by lysosomal degradation. We observed that ${\delta}$-catenin plays a key role in EGFR stability and downstream signaling. ${\delta}$-Catenin competes with c-Cbl for EGFR binding, which results in a reduction of binding between c-Cbl and EGFR and thus decreases the ubiquitination of EGFR. This in turn increases the expression of membrane bound EGFR and enhances EGFR/Erk1/2 signaling. Our findings add a new perspective on the role of ${\delta}$-catenin in enhancing EGFR/Erk1/2 signaling-mediated prostate cancer.