• Korean Journal of Fisheries and Aquatic Sciences
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• v.18 no.3
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• pp.195-205
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• 1985

As a part of investigation to use the Anatrctic krill, Euphausia superba, more effectively as a food source, processing conditions, utilizations and storage stability of krill paste (intermediate product of krill) were examined and also chemical compositions of krill paste were analyzed. Frozen raw krill was chopped, agitated with $25\%$ of water to the minced krill and then centrifuged to separate the liquid fraction from the residue. This liquid fraction was heated at $98^{\circ}C$ for 20 min. to coagulate the proteins of krill, and it was filtered to separate the protein fraction. Krill paste was prepared with grinding the protein fraction, adding $0.2\%$ of polyphosphate and $0.3\%$ of sodium erythorbate to the krill paste for enhancing of functional properties and quality stability. The krill paste was packed in a carton box, and then stored at $-30^{\circ}C$. Chemical compositions of krill paste were as follows : moisture $78\%$, crude protein $12.9\%$, crude lipid $5.9\%$, and the contents of hazardous elements of krill paste as Hg 0.001 ppm, Cd 1.15 ppm, Zn 9.1 ppm, Pb 0.63 ppm and Cu 11.38ppm were safe for food. The amino acid compositions of krill paste showed relatively high amount of taurine, glutamic acid, aspartic acid, leucine, lysine and arginine, which occupied $55\%$ of total amino acid and also taurine, lysine, glycine, arginine and proline were occupied $65\%$ of total free amino acid. Fatty acid compositions of krill paste consist of $32.4\%$ of saturated fatty acid, $29.6\%$ of monoenoic acid and $38.0\%$ of polyenoic acid, and major fatty acids of product were eicosapentaenoic acid ($17.8\%$), oleic acid ($16.9\%$), palmitic acid ($15.3\%$), myristic acid ($8.7\%$) and docosahexaenoic acid ($8.4\%$). In case of procssing of fish sausage as one of experiment for krill paste use, Alaska pollack fish meat paste could be substituted with the krill paste up to $30\%$ without any significant defect in taste and texture of fish sausage, and the color of fish sausage could be maintained by the color of krill paste. Judging from the results of chemical and microbial experiments during frozen storage, the quality of krill paste could be preserved in good condition for 100 days at $-39^{\circ}C$.

• Tuberculosis and Respiratory Diseases
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• v.49 no.3
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• pp.310-322
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• 2000

Background : Phospholipase C(PLC) plays an important role in cellular signal transduction and is thought to be critical in cellular growth, differentiation and transformation of certain malignancies. Two second messengers produced from the enzymatic action of PLC are diacylglycerol (DAG) and inositol 1, 4, 5-trisphosphate (IP3). These two second messengers are important in down stream signal activation of protein kinase C and intracellular calcium elevation. In addition, functional domains of the PLC isozymes, such as Src homology 2 (SH2) domain, Src homology 3 (SH3) domain, and pleckstrin homology (PH) domain play crucial roles in protein translocation, lipid membrane modificailon and intracellular memrane trafficking which occur during various mitogenic processes. We have previously reported the presence of PLC-${\gamma}1$, ${\gamma}2$, ${\beta}1$, ${\beta}3$, and ${\delta}1$ isozymes in normal human lung tissue and tyrosine-kinase-independent activation of phospholipase C-${\gamma}$ isozymes by tau protein and AHNAK. We had also found that the expression of AHNAK protein was markedly increased in various mstologic types of lung can∞r tissues as compared to the normallungs. However, the report concerning expression of various PLC isozymes in lung canærs and other lung diseases is lacking. Therefore, in this study we examined the expression of PLC isozymes in the paired surgical specimens taken from lung cancer patients. Methods : Surgically resected lung cancer tissue samples taken from thirty seven patients and their paired normal control lungs from the same patients, The expression of various PLC isozymes were studied. Western blot analysis of the tissue extracts for the PLC isozymes and immunohistochemistry was performed on typical samples for localization of the isozyme. Results : In 16 of 18 squamous cell carcinomas, the expression of PLC-${\gamma}1$ was increased. PLC-${\gamma}1$ was also found to be increased in all of 15 adenocarcinoma patients. In most of the non-small cell lung cancer tissues we had examined, expression of PLC-${\delta}1$ was decreased. However, the expression of PLC-${\delta}1$ was markedly increased in 3 adenocarcinomas and 3 squamous carcinomas. Although the numbers were small, in all 4 cases of small cell lung cancer tissues, the expression of PLC-${\delta}1$ was nearly absent. Conclusion : We found increased expression of PLC-${\gamma}1$ isozyme in lung cancer tissues. Results of this study, taken together with our earlier findings of AHNAK protein-a putative PLD-${\gamma}$, activator-over-expression, and the changes observed in PLC-${\delta}1$ in primary human lung cancers may provide a possible insight into the derranged calcium-inositol signaling pathways leading to the lung malignancies.