메뉴 건너뛰기




Volumn 227, Issue 6, 2012, Pages 2613-2621

Association of C-terminal region of phosphoglycerate mutase with glycolytic complex regulates energy production in cancer cells

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; FRUCTOSE BISPHOSPHATE ALDOLASE; GLUCOSE; LACTIC ACID; PHOSPHOGLYCERATE MUTASE; PYRUVATE KINASE;

EID: 84857466328     PISSN: 00219541     EISSN: 10974652     Source Type: Journal    
DOI: 10.1002/jcp.22998     Document Type: Article
Times cited : (16)

References (29)
  • 1
    • 0000717689 scopus 로고
    • Methods of enzymatic analysis.
    • Bergmeyer HU, editor. New York: Academic Press
    • Bergmeyer HU, Gawehn K, Grassl M. 1974. Methods of enzymatic analysis. In: Bergmeyer HU, editor. Berlag Chemie Weinhein, Vol. 1. New York: Academic Press. pp 425-522.
    • (1974) Berlag Chemie Weinhein , vol.1 , pp. 425-522
    • Bergmeyer, H.U.1    Gawehn, K.2    Grassl, M.3
  • 2
    • 36349004121 scopus 로고    scopus 로고
    • Lactate favours the dissociation of skeletal muscle 6-phosphofructo-1-kinase tetramers down-regulating the enzyme and muscle glycolysis
    • Costa Leite T, Da Silva D, Guimarães Coelho R, Zancan P, Sola-Penna M. 2007. Lactate favours the dissociation of skeletal muscle 6-phosphofructo-1-kinase tetramers down-regulating the enzyme and muscle glycolysis. Biochem J 408:123-130.
    • (2007) Biochem J , vol.408 , pp. 123-130
    • Costa Leite, T.1    Da Silva, D.2    Guimarães Coelho, R.3    Zancan, P.4    Sola-Penna, M.5
  • 3
    • 75149150660 scopus 로고    scopus 로고
    • HnRNP proteins controlled by c-Myc deregulate pyruvate kinase mRNA splicing in cancer
    • David CJ, Chen M, Assanah M, Canoll P, Manley JL. 2010. HnRNP proteins controlled by c-Myc deregulate pyruvate kinase mRNA splicing in cancer. Nature 463:364-368.
    • (2010) Nature , vol.463 , pp. 364-368
    • David, C.J.1    Chen, M.2    Assanah, M.3    Canoll, P.4    Manley, J.L.5
  • 4
    • 4143064982 scopus 로고    scopus 로고
    • Phosphoglycerate mutase-derived polypeptide inhibits glycolytic flux and induces cell growth arrest in tumor cell lines
    • Engel M, Mazurek S, Eigenbrodt E, Welter C. 2004. Phosphoglycerate mutase-derived polypeptide inhibits glycolytic flux and induces cell growth arrest in tumor cell lines. J Biol Chem 279:35803-35812.
    • (2004) J Biol Chem , vol.279 , pp. 35803-35812
    • Engel, M.1    Mazurek, S.2    Eigenbrodt, E.3    Welter, C.4
  • 5
    • 33744783432 scopus 로고    scopus 로고
    • Attenuation of LDH-A expression uncovers a link between glycolysis, mitochondrial physiology, and tumor maintenance
    • Fantin VR, St-Pierre J, Leder P. 2006. Attenuation of LDH-A expression uncovers a link between glycolysis, mitochondrial physiology, and tumor maintenance. Cancer Cell 9:425-434.
    • (2006) Cancer Cell , vol.9 , pp. 425-434
    • Fantin, V.R.1    St-Pierre, J.2    Leder, P.3
  • 6
    • 0034640272 scopus 로고    scopus 로고
    • Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium
    • Fillinger S, Boschi-Muller S, Azza S, Dervyn E, Branlant G, Aymerich S. 2000. Two glyceraldehyde-3-phosphate dehydrogenases with opposite physiological roles in a nonphotosynthetic bacterium. J Biol Chem 275:14031-14037.
    • (2000) J Biol Chem , vol.275 , pp. 14031-14037
    • Fillinger, S.1    Boschi-Muller, S.2    Azza, S.3    Dervyn, E.4    Branlant, G.5    Aymerich, S.6
  • 8
    • 0037468610 scopus 로고    scopus 로고
    • FBPase is in the nuclei of cardiomyocytes
    • Gizak A, Dzugaj A. 2003. FBPase is in the nuclei of cardiomyocytes. FEBS Lett 539:51-55.
    • (2003) FEBS Lett , vol.539 , pp. 51-55
    • Gizak, A.1    Dzugaj, A.2
  • 9
    • 0017033341 scopus 로고
    • Conjugation of antibodies with fluorochromes: Modifications to the standard methods
    • Goding JW. 1976. Conjugation of antibodies with fluorochromes: Modifications to the standard methods. J Immunol Methods 13:215-226.
    • (1976) J Immunol Methods , vol.13 , pp. 215-226
    • Goding, J.W.1
  • 11
    • 0019321365 scopus 로고
    • Compartmentation of glycolytic enzymes in nerve endings as determined by glutaraldehyde fixation
    • Knull HR. 1980. Compartmentation of glycolytic enzymes in nerve endings as determined by glutaraldehyde fixation. J Biol Chem 255:6439-6444.
    • (1980) J Biol Chem , vol.255 , pp. 6439-6444
    • Knull, H.R.1
  • 13
    • 67349219399 scopus 로고    scopus 로고
    • Phosphoglycerate mutase in mammalian striated muscles: Subcellular localization and binding partners
    • Kowalski W, Gizak A, Rakus D. 2009. Phosphoglycerate mutase in mammalian striated muscles: Subcellular localization and binding partners. FEBS Lett 583:1841-1845.
    • (2009) FEBS Lett , vol.583 , pp. 1841-1845
    • Kowalski, W.1    Gizak, A.2    Rakus, D.3
  • 14
    • 0034494381 scopus 로고    scopus 로고
    • Coupling of creatine kinase to glycolytic enzymes at the sarcomeric I-band of skeletal muscle: A biochemical study in situ
    • Kraft T, Hornemann T, Stolz M, Nier V, Wallimann T. 2000. Coupling of creatine kinase to glycolytic enzymes at the sarcomeric I-band of skeletal muscle: A biochemical study in situ. J Muscle Res Cell Motil 21:691-703.
    • (2000) J Muscle Res Cell Motil , vol.21 , pp. 691-703
    • Kraft, T.1    Hornemann, T.2    Stolz, M.3    Nier, V.4    Wallimann, T.5
  • 15
    • 84856470082 scopus 로고    scopus 로고
    • Fretting about FRET in cell and structural biology.
    • Zuk D, editor. Cambridge, MA: Cell Press
    • Mayor S, Bilgrami S. 2007. Fretting about FRET in cell and structural biology. In: Zuk D, editor. Evaluating techniques in biochemical research. Cambridge, MA: Cell Press. pp 43-49.
    • (2007) Evaluating techniques in biochemical research , pp. 43-49
    • Mayor, S.1    Bilgrami, S.2
  • 16
    • 0029864851 scopus 로고    scopus 로고
    • Studies on associations of glycolytic and glutaminolytic enzymes in MCF-7 cells: Role of P36
    • Mazurek S, Hugo F, Failing K, Eigenbrodt E. 1996. Studies on associations of glycolytic and glutaminolytic enzymes in MCF-7 cells: Role of P36. J Cell Physiol 167:238-250.
    • (1996) J Cell Physiol , vol.167 , pp. 238-250
    • Mazurek, S.1    Hugo, F.2    Failing, K.3    Eigenbrodt, E.4
  • 17
    • 0031730047 scopus 로고    scopus 로고
    • Metabolic characteristics of different malignant cancer cell lines
    • Mazurek S, Grimm H, Wilker S, Leib S, Eigenbrodt E. 1998. Metabolic characteristics of different malignant cancer cell lines. Anticancer Res 18:3275-3282.
    • (1998) Anticancer Res , vol.18 , pp. 3275-3282
    • Mazurek, S.1    Grimm, H.2    Wilker, S.3    Leib, S.4    Eigenbrodt, E.5
  • 18
    • 0032797579 scopus 로고    scopus 로고
    • Alterations in the glycolytic and glutaminolytic pathways after malignant transformation of rat liver oval cells
    • Mazurek S, Eigenbrodt E, Failing K, Steinberg P. 1999. Alterations in the glycolytic and glutaminolytic pathways after malignant transformation of rat liver oval cells. J Cell Physiol 181:136-146.
    • (1999) J Cell Physiol , vol.181 , pp. 136-146
    • Mazurek, S.1    Eigenbrodt, E.2    Failing, K.3    Steinberg, P.4
  • 19
    • 0035874480 scopus 로고    scopus 로고
    • Effects of the human papilloma virus HPV-16 E7 oncoprotein on glycolysis and glutaminolysis: Role of pyruvate kinase type M2 and the glycolytic-enzyme complex
    • Mazurek S, Zwerschke W, Jansen-Dürr P, Eigenbrodt E. 2001. Effects of the human papilloma virus HPV-16 E7 oncoprotein on glycolysis and glutaminolysis: Role of pyruvate kinase type M2 and the glycolytic-enzyme complex. Biochem J 356:247-256.
    • (2001) Biochem J , vol.356 , pp. 247-256
    • Mazurek, S.1    Zwerschke, W.2    Jansen-Dürr, P.3    Eigenbrodt, E.4
  • 21
    • 23044500915 scopus 로고    scopus 로고
    • Pyruvate kinase type M2 and its role in tumor growth and spreading
    • Mazurek S, Boschek CB, Hugo F, Eigenbrodt E. 2005. Pyruvate kinase type M2 and its role in tumor growth and spreading. Semin Cancer Biol 15:300-308.
    • (2005) Semin Cancer Biol , vol.15 , pp. 300-308
    • Mazurek, S.1    Boschek, C.B.2    Hugo, F.3    Eigenbrodt, E.4
  • 22
    • 79958103961 scopus 로고    scopus 로고
    • Pyruvate kinase type M2: A key regulator of the metabolic budget system in tumor cells
    • Mazurek S. 2011. Pyruvate kinase type M2: A key regulator of the metabolic budget system in tumor cells. Int J Biochem Cell Biol 43:969-980.
    • (2011) Int J Biochem Cell Biol , vol.43 , pp. 969-980
    • Mazurek, S.1
  • 23
    • 0024379013 scopus 로고
    • Characterization of triosephosphate isomerase mutants with reduced enzyme activity in Mus musculus
    • Merkle S, Pretsch W. 1989. Characterization of triosephosphate isomerase mutants with reduced enzyme activity in Mus musculus. Genetics 123:837-844.
    • (1989) Genetics , vol.123 , pp. 837-844
    • Merkle, S.1    Pretsch, W.2
  • 25
    • 0032486286 scopus 로고    scopus 로고
    • Alpha-enolase a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci
    • Pancholi V, Fischetti VA. 1998. Alpha-enolase a novel strong plasmin(ogen) binding protein on the surface of pathogenic streptococci. J Biol Chem 273:14503-14515.
    • (1998) J Biol Chem , vol.273 , pp. 14503-14515
    • Pancholi, V.1    Fischetti, V.A.2
  • 26
    • 0242299766 scopus 로고    scopus 로고
    • Colocalization of muscle FBPase and muscle aldolase on both sides of the Z-line
    • Rakus D, Mamczur P, Gizak A, Dus D, Dzugaj A. 2003. Colocalization of muscle FBPase and muscle aldolase on both sides of the Z-line. Biochem Biophys Res Commun 311:294-299.
    • (2003) Biochem Biophys Res Commun , vol.311 , pp. 294-299
    • Rakus, D.1    Mamczur, P.2    Gizak, A.3    Dus, D.4    Dzugaj, A.5
  • 27
    • 0021257326 scopus 로고
    • Catalytic activity of rabbit skeletal muscle aldolase in the crystalline state
    • Sygusch J, Beaudry D. 1984. Catalytic activity of rabbit skeletal muscle aldolase in the crystalline state. J Biol Chem 259:10222-10227.
    • (1984) J Biol Chem , vol.259 , pp. 10222-10227
    • Sygusch, J.1    Beaudry, D.2
  • 28


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.