가상수(Virtual Water) 개념과 물 관리 정책

고재경 한국수자원공사 2009 저널 물 정책·경제 Vol.12 No.-

간세포암종 조직의 Ribonuclease Inhibitor에 관한 연구

김용석,이성록,고재경 한양대학교 의과대학 1994 한양의대 학술지 Vol.14 No.1

In order to understand the interaction between ribonuclease(RNase) and RNase inhibitor in hepatocellular carcinoma, activities of RNase and RNase inhibitor were determined in the cancer tissue and ascitic fluid of patients with the liver cancer. Fractionated were the RNases and RNase inhibitors of the cancer tissue and the ascitic fluid to find out the enyme and the enzyme inhibitor specific to the liver cancer. RNase and RNase inhibitor activities in the peripheral area of liver cancer tissue were increased by 72% each and the positive rates of the enzyme and the enzyme inhibitor activities as markers for the liver cancer were high. RNase activity in the central area of liver cancer tissue was decreased significantly, while RNase inhibitor activity was unchanged. RNase activity in the ascitic fluid from patients with hepatocellular carcinoma was increased by 52%, while RNase inhibitor activity was unchanged. RNases in both contral and peripheral area of hepatocellular carcinoma tissue were separated by a DEAE-cellulose column chromatography into 7 isozymes(RNase isozyme Ⅰ-Ⅶ) each. No RNase specific to the cancer was isolated, but RNase isozyme V isolated from peripheral area of the liver cancer tissue was activated. Activity of RNase inhibitor associated with the RNase isozyme Ⅴ was also increased greatly as compared with that of the control tissue. Of the RNase isozymes isolated from both control and liver cancer tissues, RNase isozyme I was nonsecretory type of RNase active against RNA as substrate and RNase isozymes Ⅳ,Ⅴ,Ⅵ and Ⅶ were secretory type of RNase active against poly C. RNases in ascitic fluid from patient with hepatocellular carcinoma were separated into 4 isozymes(RNases isozymes Ⅰ-Ⅳ). No RNase specific to the cancer was isolated, but RNase isozyme I was markedly activated. RNase isozyme Ⅴ activated greatly in the peripheral area of the liver cancer tissue was, however, not found in the ascitic fluid. All RNase isozymes isolated from the ascitic fluid of patients with hepatocellular carcinoma were detected to be complexed with RNase inhibitor, of which RNase isozyme Ⅳ exhibited greater inhibitor activity. Observations that RNase isozyme Ⅴ isolated from peripheral area of hepatocellular carcinoma tissue (1)was activated. (2)was not released into the ascitic fluid confining the isozyme inside the liver cancer tissue, (3)was secretory type of RNase active against poly C as substrate and (4)exhibited higher RNase inhibitor activity suggested that regulatory action of the RNase isozyme Ⅴ and the RNase inhibitor might play an important role in carcinogenesis and suppression processes of the liver cancer.

골육종조직에서 활성화된 Neutral RNase Isozyme의 정제와 작용기전에 관한 연구

최충혁,최일용,김성준,고재경 한양대학교 의과대학 1994 한양의대 학술지 Vol.14 No.2

Of the RNase isozymes isolated from osteosarcoma tissue of human, ribonuclease(RNase) isozyme I exhibited the highest activity and appeared to be activated. The present study was carried out to purify the RNase isozyme I and to determine the substrate specificity for the isozyme specfic to osteosarcoma. Activities of both RNase and RNase inhibitor in osteosarcoma tissue were markedly increased, indicating the possible use of the enzyme and the enzyme inhibitor as biochemical marker for osteosarcoma. RNases in osteosarcoma tissue were separated by a DEAE-cellulose column chromatography into five isozymes, of which two isozymes were activated and other two isozymes were specific to osteosarcoma. The activity of RNase inhibitor complexed with these RNase isozymes was observed to be high. Of the two RNase isozymes activated, RNase isozyme I exhibited higher activity and appeared to be specific to osteosarcoma. The RNase isozyme I was separated by a HPLC into 7 subpeaks, of which RNase isozyme I-3 with the highest RNase activity appeared to by specific to osteosarcoma. The RNase isozyme I-3 separated and purified from osteosarcoma tissue was not active against double stranded polynucleotides, but active against single stranded polyribonucleotide, being highly active against single stranded polyribonucleotide, being highly active on C-C, C-U and A-U linkages. A considerable activity was observed with RNA as substrate, being different from other RNase isozymes isolated from osteosarcoma tissue and its control bone tissue. The results obtained in the present study indicated that the RNase isozyme I-3 results obtained in the present study indicated that the RNase isozyme I-3 purified from osteosarcoma tissue was activated, specific to osteosarcoma and exhibited a considerable acitivty on RNA, suggesting that the isozyme play an important role in RNA mediated tumorigenesis in osteosarcoma.

암의 생화학적 지표로서의 Ribonuclease에 관한 연구

김정미,이용성,고재경 한양대학교 의과대학 1995 한양의대 학술지 Vol.15 No.1

The pattern of changes in activities and positive rates of ribonuclease (RNase) were determined in the cancer tissues, serum, ascitic fluid and cystic fluid in patients with 15 different cancers to evaluate the possibility of using RNase as a marker for human cancer. The activity of RNase in tumor tissues was increased in hepatocollular carcinoma(peripheral area), mucinous cystadenocarcinoma and endodermal sinus tumor of ovary, and osteosarcoma, metastatic squamous cell carcinoma and giant cell tumor of bone, decreased in hepatocellular carcinoma(central area), stomach cancer, renal cell carcinoma and serous cystadenocarcinoma of ovary and unchanged in bladder cancer, prostate cancer and lung cancers(epidermoid, adeno, large cell and small cell carcinomas). The positive rate of the tissue enzyme activity as a marker for cancer was observed to be over 50% in the liver, stomach, ovary and bone tumors suggesting that the RNase activity in the cancer tissues can be used for biochemical marker for these cancers. Serum RNase activity was singificantly increased in all cancers studied except for renal cell carcinoma. The enzyme activity in serum of renal cell carcinoma was unchanged. The positive rate of the serum RNase activity as a marker for cancer was found to be over 50% in 6 types of cancers(hepatocellular cancer, bladder cancer, serous cystadenocarcinoma and mucinous cystadenocarcinoma of ovary, acute lymphocytic and myelogenous leukemia) out of 15 types of cancers studied, indicating the possiblity of using the RNase activity as a diagnostic and biochemical markers for 6 types of cancers. In patients with hepatocellular carcinoma, the RNase activity was decreased in central area of the cancer tissue and increased in peripheral area of the cancer tissue, serum and ascitic fluid. In patients with serous cystadenocarcinoma of ovary, the RNase activity was decreased in the cancer tissue and increased in serum, ascitic fluid and cystic fluid of ovary. These results indicated that the RNase was released from the cancer tissue of the liver and overy into blood stream and that the RNase activity in the ascitic fluid and cystic fluid could be used as a marker for the liver and ovary cancer.

골에서 발생한 거대세포종에 특이한 Neutral Ribonuclease의 작용기전에 관한 연구

김성준,김세현,최일용,고재경 한양대학교 의과대학 1995 한양의대 학술지 Vol.15 No.2

To clarify a role of ribonuclease (RNase) in tumorigenesis for giant cell tumor of bone, a RNase isozyme activated in the tumor tissue was separated, and substrate specificity and mode of action of the isozyme were investigated. Activities of RNase and RNase inhibitor in giant cell tumor tissue of bone showed the highest value with poly C as substrate and lower value with RNA or poly A as substrate. Irrespective of substrate used, RNase and RNase inhibitor activities were markedly increased in the giant cell tumor tissue of bone as compared with those in the control bone tissue, and the positive rate of RNase and RNase inhibitor activities as marker for giant cell tumor were higher, suggesting the possible use of RNase and RNase inhibitor as a biochemical marker for giant cell tumor of bone. RNases in giant cell tumor tissue of bone were separated by a DEAE-cellulose column chromtography into 6 isozymes, of which the RNase isozyme V was greatly increased to be activated. The activated RNase isozyme V exhibited higher activity toward poly C than RNA as substrate, indicating the secretory type of enzyme. The RNase isozyme V hydrolyzed linkages of C-C, A-C and A-U with higher activity and the inhibitor activity complexed with the RNase isozme V was increased markedly. These results indicated that the RNase isozyme V was activated and exhibited to be secretory type of enzyme. Majority of hydrolytic products of poly C by the RNase isozyme V appeared to be oligoribonucleotides, suggesting the isozyme V as an endoribonclease. The present study revealed that the RNase isozyme V was activated and was secretory type of enzyme. The activity of the RNase inhibitor associated with the RNase isozyme V was increased and the isozyme was an endoribonuclease in nature, highly active toward the linkages of C-C, A-C and A-U of ss-polyribonucleotide, suggesting a possible action of the isozyme for suppression of the giant cell tumor of bone.

신세포암종 조직에서 암에 특이한 RNase Isozyme과 Inhibitor의 성상에 관한 연구

남경원,강진호,한중수,고재경 한양대학교 의과대학 1996 한양의대 학술지 Vol.16 No.1

Activities of ribonuclease (RNase) and RNAse inhibitor reported to be involved in carcinogenesis process were determined in the renal cell carcinoma tissue. RNase and RNAse inhibitor specific to the cancer were isolated from the renal cell carcinoma tissue. substrate specificity and other properties of th enzyme and enzyme inhibitor were studied and their interaction was investigated. RNase activity in the renal cell carcinoma tissue was significantly dicreased with the use of poly C as substrate and unchanged with the use of RNA as substrate. Ratio of RNA/poly C for RNase activity was higher in the cancer tissue than the control tissue. Activity of RNAse inhibitor was significantly increased and inhibitor/RNAse ratio was markedly higher in the cancer tissue. Proteins in the renal cell carcinoma tissue were separated by a DEAE-cellulose column chromatography into 6 peaks, of which five peak proteins exhibited RNASe and RNase inhibitor activities. Activities of RNase and RNAse inhibitor in for RNASE isozyme fractions except for RNAse isozyme I were lower in the cancer tissue than in the control tissue, but RNA/poly C ratio for RNase activity and inhibitor/RNase ratio were higher in th cancer tissue than the control tissue than the control, and RNA/poly C ratio for the RNase activity and inhibitor/RNA ratio were markedly higher in the isozyme I fraction of the cancer tissue. The RNase isozyme I isolated from the renal cell carcinoma tissue was highly active toward poly AC and AU, the activity being decreased toward poly C,AU, U, RNA, poly CIU, CU, CI in order. Noactivity was observed toward poly AGU, AG, GU, poly dA and dT. Substrate specificity of the RNAse isozyme I from the cancer tissue was similar to that of the isozyme I from the control tissue in pattern but differ in that relative activity toward poly CU, AC, ACU, U and RNA was higher in the isozyme I from the cancer tissue than from the control tissue. The present study were summerized that (1) RNAse acitivity was significantly decreased and RNAse inhibitor activity was increased in the renal cell carcinoma tissue, (2) ratio of RNA/poly C for RNAse activity and inhibitor/RNase ratio were higher in the RNAse isozyme I from the renal cell carcinoma tissue than that from the renal control tissue and (3) substrate specificity was different between the two tissues. These results indicatd that the RNase isozyme I isolated from the renal cell carcinoma tissue is specific to the cancer and that the isozyme appears to be regulated strongly by the RNase inhibitor, suggesting an important role of the isozyme in carcinogenesis of the renal cell carcinoma.

초등학생의 가정환경 및 학교생활 경험과 자아개념 간의 관계

고재경,송현종 한국지역사회교육상담학회 2002 지역사회교육상담연구 Vol.1 No.1

Postero-Anterior Cephalometry를 利用한 顔貌의 非對稱에 關한 硏究

金在德,高在炅 大韓口腔顎顔面 放射線學會 1987 Imaging Science in Dentistry Vol.17 No.1

The purpose of this article was to determine the amount of cranio-facial asymmetry in normal subject before the analysis of the cranio-facial asymmetry as the result of internal derangement in T.M.J. dysfunction. The author has conducted analysis using Cephalometric P-A reviews of 54 males and 51 females. Following the Grayson's method of measurement, the standard value of cranio-facial asymmetry in normal subject was obtained. The following results were obtained : 1. Compared with right and left width, asymmetry could be identified in normal subject, although the degree of the difference appears to be small. 2. In male, asymmetric value of contact point of the upper central incisors is 0.76 ±0.84㎜, that of the lower central incisors is 0.86 ±0.86㎜, and that of center of genial tubercle is 0.87 ±1.06㎜. In female, asymmetric value of contract point of the upper central incisors is 1.03 ±1.29㎜, that of the lower incisors is 1.11 ±1.18㎜, and that of center of genial tubercle is 1.45 ±2.15㎜. 3. Cranio-facial saymmetry in female is somewhat greater than that of male.

鼻Polyp組織에서 核酸分解酵素 活性度의 變動에 對한 硏究

김선곤,이형석,송기준,안경성,고재경 한양대학교 의과대학 1986 한양의대 학술지 Vol.6 No.1

In order to investigate whether activities of enzymes involved in nucleic acid metabolism were changed in nasal polyp tissues, enzyme levels of typical nucleases, ribonuclease (RNase) and deoxyribonuclease (DNase) were determined in nasal polyp tissues and were compared with those in normal control tissues. Also measured were concentrations of DNA, RNA and proteins in nasal polyp tissues, and results were as follows: 1) Activities of RNases were significantly higher in nasal polyp tissues than in normal control tissues; neutral RNase activity was increased by 92% and acid RNase by 62%. The positive rate of the enzyme activity as a marker for nasal polyp was observed to be high (46%) in neutral RNase and low (18%) in acid RNase. 2) While activities of RNases were significantly increased, activities of DNases (neutral, acid and alkaline DNases) remained unchanged, and the positive rate of DNase activities as a marker for nasal polyp was also found to be low. 3) Concentrations of DNA, RNA and proteins in nasal polyp tissues were increased by 62%, 46% and 89%, respectively, as compared with those in normal control tissues. The positive rates of nucleic acid and protein levels as a marker for nasal polyp were obtained to be high (46% each) in DNA and protein and low (18%) in RNA. 4) Neutral RNases in nasal polyp tissues were isolated in four peaks by DEAE-cellulose column chromatography. The neutral RNases isolated from nasal polyp tissues exhibited the highest activity against polycytidylate (poly C) and virtually no activity was observed against purine polyribonucleotides, polyadenylate (poly A) and polyguanylate (poly G). The RNase activity was observed to be higher with RNA as substrate than with polyuridylate (poly U). 5) The pattern of nasal polyp tissue proteins separated by polyacrylamide gel electrophoresis appeared to be different from that normal nasal tissue proteins. It was, however, unclear whether proteins specific to nasal polyp was present in the nasal polyp tissues. The results indicated that concentrations of nucleic acids and proteins and RNase activity used as a marker for tissue proliferation and tumor were significantly increased in nasal polyp tissues, but DNase activity known to be involved in development and maintenance of tumors remained unchanged. This may show the one aspect of difference between nasal polyp characterized by tissue proliferation and tumor tissues.

소아 급성 백혈병 환아의 혈청 Ribonuclease의 분리에 대한 연구

김정환,한중수,고재경 한양대학교 의과대학 1986 한양의대 학술지 Vol.6 No.1

In the present study activities of neutral RNase and positive rate of the enzyme as a marker for leukemia were determined in serum of patients (children) with acute lymphocytic and nonlymphocytic leukemia. The neutral RNase in the serum was isolated and fractionated by DEAE-cellulose column chromatography and polyacrylamide gel electrophoresis to investigate whether the enzyme proteins unique to acute leukemia were present in serum of the patients. 1. Activities of serum neutral RNase and positive rate of the serum enzyme as a marker for acute leukemia were significantly increased. 2. Of the protein peaks isolated by DEAE-cellulose column chromatography in normal and patient with acute lymphocytic leukemia, four protein peaks exhibited RNase activity. Activities and specific activities of neutral RNase of each of four DEAE-cellulose peaks from the leukiemc serum were greater than those from normal serum especially in DEAE-cellulose peaks Ⅲ and Ⅳ. 3. Patterns of protein bands fractionated by polyacrylamide gel electrophoresis in serum of patients with acute lymphocytic leukemia were similar to those of normal serum in DEAE-cellulose peaks, Ⅰ, Ⅱ and Ⅲ, but appeared to different from those of normal in DEAE-cellulose peak Ⅳ. The results indicated that determination of serum neutral RNase could be used as a marker for acute leukemia in children and suggested that RNase specific to leukemia might be present in serum of patients (children) with lymphocytic leukmia.