RISS 학술연구정보서비스

검색
다국어 입력

http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.

변환된 중국어를 복사하여 사용하시면 됩니다.

예시)
  • 中文 을 입력하시려면 zhongwen을 입력하시고 space를누르시면됩니다.
  • 北京 을 입력하시려면 beijing을 입력하시고 space를 누르시면 됩니다.
닫기
    인기검색어 순위 펼치기

    RISS 인기검색어

      KCI등재

      기아상태에서 Ldh-C가 발현된 어류 조직의 젖산탈수소효소의 대사

      한글로보기

      https://www.riss.kr/link?id=A101779958

      • 0

        상세조회
      • 0

        다운로드
      서지정보 열기
      • 내보내기
      • 내책장담기
      • 공유하기
      • 오류접수

      부가정보

      국문 초록 (Abstract)

      젖산탈수소효소(Lactate dehydrogenase, EC 1.1.1.27, LDH) LDH-C의 기능을 확인하기 위해 liver-specific Ldh-C가 발현된 붕어(Carassius auratus)와 eye-specific Ldh-C가 발현된 파랑볼우럭(Lepomis macrochirus)을 기아 상태로 유지시킨 후(S) 조직들의 LDH 대사를 연구하였다. 기아 후 붕어 간조직의 LDH 활성이 크게 증가되었으며 LDH 비활성(units/mg)과 LDH/CS는 조직들에서 증가되어 혐기적 대사가 이루어짐을 확인하였다. 기아 후 LDH B4 동위효소가 골격근조직에서 감소되었고 심장조직에서 증가되었다. 눈과 뇌조직에 나타났던 LDH C4 동위효소는 liver-specific C4로 확인되었으며 기아 후에 없어지고, 눈조직은 C hybrid, 뇌조직은 A4, 간조직은 C hybrid와 C4 동위효소가 각각 증가되었다. 그러나 파랑볼우럭 조직에서 LDH 활성의 변화는 작았으나 눈조직에서 가장 크게 증가되었으며, 뇌조직은 LDH A4와 AC hybrid가 증가되었다. 피루브산 10 mM에 의해 기아 후 붕어 조직의 LDH 활성은 30.30-18.64%, 파랑볼우럭 조직의 LDH는 25-18.75% 남았으며, 붕어는 Km<SUP>PYR</SUP> 값이 증가되었다. 실험결과 LDH liver-specific C 동위효소가 기아 중에 간, 뇌 및 눈조직에서 발현되었고, 기아 후 뇌조직에서 젖산의 대사가 우세하고, 붕어 LDH liver-specific C가 파랑볼우럭 LDH eye-specific C보다 영향을 더 받는 것으로 사료된다.
      번역하기

      젖산탈수소효소(Lactate dehydrogenase, EC 1.1.1.27, LDH) LDH-C의 기능을 확인하기 위해 liver-specific Ldh-C가 발현된 붕어(Carassius auratus)와 eye-specific Ldh-C가 발현된 파랑볼우럭(Lepomis macrochirus)을 기아 상태...

      젖산탈수소효소(Lactate dehydrogenase, EC 1.1.1.27, LDH) LDH-C의 기능을 확인하기 위해 liver-specific Ldh-C가 발현된 붕어(Carassius auratus)와 eye-specific Ldh-C가 발현된 파랑볼우럭(Lepomis macrochirus)을 기아 상태로 유지시킨 후(S) 조직들의 LDH 대사를 연구하였다. 기아 후 붕어 간조직의 LDH 활성이 크게 증가되었으며 LDH 비활성(units/mg)과 LDH/CS는 조직들에서 증가되어 혐기적 대사가 이루어짐을 확인하였다. 기아 후 LDH B4 동위효소가 골격근조직에서 감소되었고 심장조직에서 증가되었다. 눈과 뇌조직에 나타났던 LDH C4 동위효소는 liver-specific C4로 확인되었으며 기아 후에 없어지고, 눈조직은 C hybrid, 뇌조직은 A4, 간조직은 C hybrid와 C4 동위효소가 각각 증가되었다. 그러나 파랑볼우럭 조직에서 LDH 활성의 변화는 작았으나 눈조직에서 가장 크게 증가되었으며, 뇌조직은 LDH A4와 AC hybrid가 증가되었다. 피루브산 10 mM에 의해 기아 후 붕어 조직의 LDH 활성은 30.30-18.64%, 파랑볼우럭 조직의 LDH는 25-18.75% 남았으며, 붕어는 Km<SUP>PYR</SUP> 값이 증가되었다. 실험결과 LDH liver-specific C 동위효소가 기아 중에 간, 뇌 및 눈조직에서 발현되었고, 기아 후 뇌조직에서 젖산의 대사가 우세하고, 붕어 LDH liver-specific C가 파랑볼우럭 LDH eye-specific C보다 영향을 더 받는 것으로 사료된다.

      더보기

      다국어 초록 (Multilingual Abstract)

      Metabolism of lactate dehydrogenase (EC 1.1.1.27, LDH) was studied to identify the function of LDH-C. Tissues of LDH liver-specific Ldh-C expressed Carassius auratus and eye-specific Ldh-C expressed Lepomis macrochirus after starvation were studied. LDH activity in liver tissue from C. auratus was increased after starvation. And LDH specific activity (units/mg) and LDH/CS were increased in tissues. It means the anaerobic metabolism was taking place in C. auratus after starvation. LDH B4 isozyme was decreased in skeletal muscle and increased in heart tissue. LDH C4 isozymes those showed in eye and brain tissues were identified as liver-specific C4 isozymes and disappeared after starvation. And C hybrid in eye, A4 isozyme in brain, and both C hybrid and C4 isozyme in liver tissue were increased, respectively. In L. macrochirus, the level of variation of LDH activities was low but greatly increased especially in eye tissue and LDH A4 and AC hybrid were increased in brain tissue. The LDH activities in tissues from C. auratus and L. macrochirus remained 30.30-18.64% and 25-18.75%, respectively, as a result of the inhibition by 10 mM of pyruvate. The Km<SUP>PYR</SUP> values of LDH in C. auratus were increased. As a result, LDH liver-specific C4 isozyme was expressed in liver, brain and eye tissues during starvation. It seems metabolism of lactate was predominant in brain tissue. After starvation, the liver-specific LDH-C was affected more than eye-specific LDH-C.
      번역하기

      Metabolism of lactate dehydrogenase (EC 1.1.1.27, LDH) was studied to identify the function of LDH-C. Tissues of LDH liver-specific Ldh-C expressed Carassius auratus and eye-specific Ldh-C expressed Lepomis macrochirus after starvation were studied. L...

      Metabolism of lactate dehydrogenase (EC 1.1.1.27, LDH) was studied to identify the function of LDH-C. Tissues of LDH liver-specific Ldh-C expressed Carassius auratus and eye-specific Ldh-C expressed Lepomis macrochirus after starvation were studied. LDH activity in liver tissue from C. auratus was increased after starvation. And LDH specific activity (units/mg) and LDH/CS were increased in tissues. It means the anaerobic metabolism was taking place in C. auratus after starvation. LDH B4 isozyme was decreased in skeletal muscle and increased in heart tissue. LDH C4 isozymes those showed in eye and brain tissues were identified as liver-specific C4 isozymes and disappeared after starvation. And C hybrid in eye, A4 isozyme in brain, and both C hybrid and C4 isozyme in liver tissue were increased, respectively. In L. macrochirus, the level of variation of LDH activities was low but greatly increased especially in eye tissue and LDH A4 and AC hybrid were increased in brain tissue. The LDH activities in tissues from C. auratus and L. macrochirus remained 30.30-18.64% and 25-18.75%, respectively, as a result of the inhibition by 10 mM of pyruvate. The Km<SUP>PYR</SUP> values of LDH in C. auratus were increased. As a result, LDH liver-specific C4 isozyme was expressed in liver, brain and eye tissues during starvation. It seems metabolism of lactate was predominant in brain tissue. After starvation, the liver-specific LDH-C was affected more than eye-specific LDH-C.

      더보기

      목차 (Table of Contents)

      • 서론
      • 재료 및 방법
      • 결과 및 고찰
      • References
      • 초록
      • 서론
      • 재료 및 방법
      • 결과 및 고찰
      • References
      • 초록
      더보기

      참고문헌 (Reference)

      1 염정주, "풀망둑(Acanthogobius hasta) 젖산탈수소효소의 특성" 한국생명과학회 18 (18): 264-272, 2008

      2 박선영, "칠성장어(Lampetra japnica) 간조직 젖산탈수소효소와 대구(Gadus macrocephalus) liver-specific C4 동위효소의 특성 및 진화적 관계" 한국생명과학회 14 (14): 708-715, 2004

      3 염정주, "젖산탈수소효소 eye-specific C₄ 동위효소의 생화학적 특성 : 파랑볼우럭(Lepomis macrochirus)과 큰입우럭(Micropterus salmoides)" 한국생명과학회 22 (22): 209-219, 2012

      4 조성규, "급격한 용존산소량 증가에 순응한 꺽지(Coreoperca herzi)와 모래무지(Pseudogobio esocinus) 젖산탈수소효소 활성과 동위효소의 변화" 한국생명과학회 15 (15): 71-79, 2005

      5 박은미, "가물치(Channa argus) 젖산탈수소효소 동위효소들의 정제 및 특성" 한국생명과학회 20 (20): 260-268, 2010

      6 Black, D., "The sequential mobilisation and restoration of energy reserves in tissues of Atlantic cod during starvation and refeeding" 156 : 469-479, 1986

      7 Furné, M., "The metabolic effects of prolonged starvation and refeeding in sturgeon and rainbow trout" 182 : 63-76, 2012

      8 Van Roermund, C. W., "The membrane of peroxisomes in Saccharomyces cerevisiae is impermeable to NAD(H) and acetyl-CoA under in vivo conditions" 14 : 3480-, 1995

      9 Gillis, T. E., "The effects of starvation on plasma free amino acid and glucose concentrations in lake sturgeon" 49 : 1306-1316, 1996

      10 Wang, T., "The comparative physiology of food deprivation: from feast to famine" 68 : 223-251, 2006

      1 염정주, "풀망둑(Acanthogobius hasta) 젖산탈수소효소의 특성" 한국생명과학회 18 (18): 264-272, 2008

      2 박선영, "칠성장어(Lampetra japnica) 간조직 젖산탈수소효소와 대구(Gadus macrocephalus) liver-specific C4 동위효소의 특성 및 진화적 관계" 한국생명과학회 14 (14): 708-715, 2004

      3 염정주, "젖산탈수소효소 eye-specific C₄ 동위효소의 생화학적 특성 : 파랑볼우럭(Lepomis macrochirus)과 큰입우럭(Micropterus salmoides)" 한국생명과학회 22 (22): 209-219, 2012

      4 조성규, "급격한 용존산소량 증가에 순응한 꺽지(Coreoperca herzi)와 모래무지(Pseudogobio esocinus) 젖산탈수소효소 활성과 동위효소의 변화" 한국생명과학회 15 (15): 71-79, 2005

      5 박은미, "가물치(Channa argus) 젖산탈수소효소 동위효소들의 정제 및 특성" 한국생명과학회 20 (20): 260-268, 2010

      6 Black, D., "The sequential mobilisation and restoration of energy reserves in tissues of Atlantic cod during starvation and refeeding" 156 : 469-479, 1986

      7 Furné, M., "The metabolic effects of prolonged starvation and refeeding in sturgeon and rainbow trout" 182 : 63-76, 2012

      8 Van Roermund, C. W., "The membrane of peroxisomes in Saccharomyces cerevisiae is impermeable to NAD(H) and acetyl-CoA under in vivo conditions" 14 : 3480-, 1995

      9 Gillis, T. E., "The effects of starvation on plasma free amino acid and glucose concentrations in lake sturgeon" 49 : 1306-1316, 1996

      10 Wang, T., "The comparative physiology of food deprivation: from feast to famine" 68 : 223-251, 2006

      11 Scanlan, M. J., "The cancer/testis genes: review, standardization, and commentary" 4 : 1-, 2004

      12 Wang, Y., "Testis-specific lactate dehydrogenase (LDH-C4) in skeletal muscle enhances apika’s sprint-running capacity in hypoxic environment" 12 : 9218-9236, 2015

      13 Coonrod, S., "Testis-Specific Lactate dehydrogenase (LDH-C4; Ldh3) in murine oocytes and preimplantation embryos" 27 : 502-509, 2006

      14 Shaklee, J. B., "Specialized lactate dehydrogenase isozymes: the molecular and genetic basis for the unique eye and liver LDHs of teleost fishes" 185 : 217-240, 1973

      15 Metón, I., "Short-and long-term effects of refeeding on key enzyme activities in glycolysis-gluconeogenesis in the liver of gilthead seabream (Sparus aurata)" 225 : 99-107, 2003

      16 Miller, K. M., "Salmon spawning migration: metabolic shifts and environmental triggers" 4 : 75-89, 2009

      17 Wang, X., "Pyruvate protects mitochondria from oxidative stress in human neuroblastoma SK-N-SH cells" 1132 : 1-9, 2007

      18 Cho, S. K., "Purification and immunochemistry of lactate dehydrogenase in Lampetra japonica" 36 : 505-513, 1993

      19 De Roos, R, "Plasma ketone, glucose, lactate, and alanine levels in the vascular supply to and from the brain of the spiny dogfish shark (Squalus acanthias)" 268 : 354-363, 1994

      20 Moyes, C. D., "Oxidative properties of carp red and white muscle" 143 : 321-331, 1989

      21 Koslowski, M., "Multiple splice variants of lactate dehydrogenase C selectively expressed in human cancer" 62 : 6750-6755, 2002

      22 Koehler-Stec, E. M., "Monocarboxylate transporter expression in mouse brain" 275 : 516-524, 1998

      23 Fantin, V. R., "Mitochondriotoxic compounds for cancer therapy" 25 : 4787-4797, 2006

      24 Furné, M., "Metabolic organization of the sturgeon acipenser naccarii:a comparative study with rainbow trout Oncorhynchus mykiss" 289 : 161-166, 2009

      25 Dunn, J. F., "Metabolic adjustments to diving and recovery in the African lungfish. Amer" 245 : 651-657, 1983

      26 Whitt, G. S., "Localization of lactate dehydrogenase activity in the cells of the fish (Xiphophorus helleri) eye" 174 : 215-224, 1970

      27 Quistorff, B., "Lactate fuels the human brain during exercise" 22 : 3443-3449, 2008

      28 Park, S. Y., "Lactate dehydrogenase isozymes of Cypriniform and Perciform fishes: Expression of the Ldh-C gene" 265-277, 1993

      29 Goldberg, E., "LDH C: The ultimate testis-specific gene" 31 : 86-94, 2010

      30 Baumgart, E., "L-lactate dehydrogenase A-and AB isoforms are bona fide peroxisomal enzymes in rat liver evidence for involvement in intraperoxisomal NADH reoxidation" 271 : 3846-3855, 1996

      31 O’Brien, J., "Kinetic parameters and lactate dehydrogenase isozyme activities support possible lactate utilization by neurons" 32 : 597-607, 2007

      32 Mukai, C., "Glycolysis plays a major role for adenosine triphosphate supplementation in mouse sperm flagellar movement" 71 : 540-547, 2004

      33 Soengas, J. L., "Food deprivation and refeeding in Atlantic salmon, Salmo salar: effects on brain and liver carbohydrate and ketone bodies metabolism" 15 : 491-511, 1996

      34 Val, A. L., "Fishes of the amazone and environment: physiological and biochemical aspect" Springer 224-, 1995

      35 de Almeida-Val, V. M. F., "Evolutionary trends of LDH isozymes in fishes" 105 : 21-28, 1993

      36 Markert, C. L., "Evolution of a gene. Multiple genes for LDH isozymes provide a model of the evolution of gene structure, function and regulation" 189 : 102-114, 1975

      37 Zakhartsev, M., "Effects of temperature acclimation on lactate dehydrogenase of cod (Gadus morhua): genetic, kinetic and thermodynamic aspects" 207 : 95-112, 2004

      38 Chatzifotis, S., "Effect of starvation and re-feeding on reproductive indices, body weight, plasma metabolites and oxidative enzymes of sea bass (Dicentrarchus labrax)" 316 : 53-59, 2011

      39 Davis, B. J, "Disc electrophoresis. II. Method and application to human serum proteins" 121 : 404-427, 1964

      40 Tylicki, A., "Differences in some properties of lactate dehydrogenase from muscles of the carp Cyprinus carpio and trout Salmo gairdneri" 42 : 143-147, 2006

      41 Whitt, G. S, "Developmental genetics of the lactate dehydrogenase isozymes of fish" 175 : 1-35, 1970

      42 Koukourakis, M. I., "Comparison of metabolic pathways between cancer cells and stromal cells in colorectal carcinomas:a metabolic survival role for tumor-associated stroma" 66 : 632-637, 2006

      43 Yeon, J. H., "Charaterization of lactate dehydrogenase and expression of monocarboxylate transporters (MCT) 1, 2, 4 in liver from Carassius auratus" Cheongju Univ. 2011

      44 Kim, J. B., "Changes of activities and isozymes of lactate dehydrogenase in Coreoperca herzi acclimated to acute increase of temperature for short-term period" 43-50, 2004

      45 Brooks, G. A, "Cell-cell and intracellular lactate shuttles" 587 : 5591-5600, 2009

      46 Brooks, G. A., "Cardiac and skeletal muscle mitochondria have a monocarboxylate transporter MCT1" 87 : 1713-1718, 1999

      47 Bond, C. E., "Biology of fishes" Saunders College Publishing 241-258, 1996

      48 Navarro, I., "Biochemistry and molecular biology of fishes metabolic biochem, vol 4" Elsevier 393-434, 1995

      49 Hinch, S. G., "Behavioural physiology of fish migrations: salmon as a model approach" 24 : 239-295, 2005

      50 Park, E. M., "Activities of lactate dehydrogenase and ratios of lactate dehydrogenase/citrate synthase in tissue of Odontobutis interrupta" 28 : 15-24, 2011

      51 Bradford, M. M, "A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding" 72 : 248-254, 1976

      52 Sensabaugh, G. F., "A lactate dehydrogenase specific to the liver of gadoid fish" 247 : 585-593, 1972

      더보기

      동일학술지(권/호) 다른 논문

      분석정보

      View

      상세정보조회

      0

      Usage

      원문다운로드

      0

      대출신청

      0

      복사신청

      0

      EDDS신청

      0

      동일 주제 내 활용도 TOP

      더보기

      주제

      연도별 연구동향

      연도별 활용동향

      연관논문

      연구자 네트워크맵

      공동연구자 (7)

      유사연구자 (20) 활용도상위20명

      인용정보 인용지수 설명보기

      학술지 이력

      학술지 이력
      연월일 이력구분 이력상세 등재구분
      2027 평가예정 재인증평가 신청대상 (재인증)
      2021-01-01 평가 등재학술지 유지 (재인증) KCI등재
      2018-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2015-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2011-08-03 학술지명변경 외국어명 : Korean Journal of Life Science -> Journal of Life Science KCI등재
      2011-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2009-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2007-01-01 평가 등재학술지 유지 (등재유지) KCI등재
      2004-01-01 평가 등재학술지 선정 (등재후보2차) KCI등재
      2003-01-01 평가 등재후보 1차 PASS (등재후보1차) KCI등재후보
      2001-07-01 평가 등재후보학술지 선정 (신규평가) KCI등재후보
      더보기

      학술지 인용정보

      학술지 인용정보
      기준연도 WOS-KCI 통합IF(2년) KCIF(2년) KCIF(3년)
      2016 0.37 0.37 0.42
      KCIF(4년) KCIF(5년) 중심성지수(3년) 즉시성지수
      0.43 0.43 0.774 0.09
      더보기

      이 자료와 함께 이용한 RISS 자료

      나만을 위한 추천자료

      해외이동버튼