메뉴 건너뛰기




Volumn 64, Issue 9, 2012, Pages 775-782

Pyruvate kinase type M2 is upregulated in colorectal cancer and promotes proliferation and migration of colon cancer cells

Author keywords

cell proliferation; cellular glucose metabolism; colorectal cancer; migration; protein expression; protein function; pyruvate kinase

Indexed keywords

PYRUVATE KINASE; PYRUVATE KINASE ISOENZYME M 2; UNCLASSIFIED DRUG;

EID: 84865321569     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.1066     Document Type: Article
Times cited : (92)

References (46)
  • 2
    • 78349269485 scopus 로고    scopus 로고
    • Human pyruvate kinase M2: A multifunctional protein
    • Gupta, V., and, Bamezai, R. N., (2010) Human pyruvate kinase M2: a multifunctional protein. Protein Sci. 11, 2031-2044.
    • (2010) Protein Sci. , vol.11 , pp. 2031-2044
    • Gupta, V.1    Bamezai, R.N.2
  • 3
    • 35448940364 scopus 로고    scopus 로고
    • Adaptive landscapes and emergent phenotypes: Why do cancers have high glycolysis?
    • DOI 10.1007/s10863-007-9085-y, Special Topic: The Warburg Effect: Its Continued Impact on Cancer Research into the 21st Century
    • Gillies, R. J., and, Gatenby, R. A., (2007) Adaptive landscapes and emergent phenotypes: why do cancers have high glycolysis? Bioenerg. Biomembr. 39, 251-257. (Pubitemid 47619378)
    • (2007) Journal of Bioenergetics and Biomembranes , vol.39 , Issue.3 , pp. 251-257
    • Gillies, R.J.1    Gatenby, R.A.2
  • 4
    • 79960029992 scopus 로고    scopus 로고
    • Lactate enhances motility of tumor cells and inhibits monocyte migration and cytokine release
    • Goetze, K., Walenta, S., Ksiazkiewicz, M., Kunz-Schughart, L. A., and, Mueller-Klieser, W., (2011) Lactate enhances motility of tumor cells and inhibits monocyte migration and cytokine release. Int. J. Oncol. 39, 453-463.
    • (2011) Int. J. Oncol. , vol.39 , pp. 453-463
    • Goetze, K.1    Walenta, S.2    Ksiazkiewicz, M.3    Kunz-Schughart, L.A.4    Mueller-Klieser, W.5
  • 6
    • 83055180206 scopus 로고    scopus 로고
    • Cancer: Sacrifice for survival
    • Grüning, N. M., and, Ralser, M., (2011) Cancer: sacrifice for survival. Nature 7, 190-191.
    • (2011) Nature , vol.7 , pp. 190-191
    • Grüning, N.M.1    Ralser, M.2
  • 7
    • 12444279265 scopus 로고
    • On the origin of cancer cells
    • Warburg, O., (1956) On the origin of cancer cells. Science 123, 309-314.
    • (1956) Science , vol.123 , pp. 309-314
    • Warburg, O.1
  • 8
    • 7944226627 scopus 로고    scopus 로고
    • Genes of glycolysis are ubiquitously overexpressed in 24 cancer classes
    • DOI 10.1016/j.ygeno.2004.08.010, PII S0888754304002277
    • Altenberg, B., and, Greulich, K. O., (2004) Genes of glycolysis are ubiquitously overexpressed in 24 cancer classes. Genomics 84, 1014-1020. (Pubitemid 39469126)
    • (2004) Genomics , vol.84 , Issue.6 , pp. 1014-1020
    • Altenberg, B.1    Greulich, K.O.2
  • 11
    • 0032520197 scopus 로고    scopus 로고
    • The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate
    • Jurica, M. S., Mesecar, A., Heath, P. J., Shi, W., Nowak, T., and, Stoddard, B. L., (1998) The allosteric regulation of pyruvate kinase by fructose-1,6-bisphosphate. Structure 6, 195-210. (Pubitemid 28153883)
    • (1998) Structure , vol.6 , Issue.2 , pp. 195-210
    • Jurica, M.S.1    Mesecar, A.2    Heath, P.J.3    Shi, W.4    Nowak, T.5    Stoddard, B.L.6
  • 12
    • 23044500915 scopus 로고    scopus 로고
    • Pyruvate kinase type M2 and its role in tumor growth and spreading
    • DOI 10.1016/j.semcancer.2005.04.009, PII S1044579X0500026X, Tumor Metabolome
    • Mazurek, S., Boschek, C. B., Hugo, F., and, Eigenbrodt, E., (2005) Pyruvate kinase type M2 and its role in tumor growth and spreading. Semin Cancer Biol. 15, 300-308. (Pubitemid 41058775)
    • (2005) Seminars in Cancer Biology , vol.15 , Issue.4 , pp. 300-308
    • Mazurek, S.1    Boschek, C.B.2    Hugo, F.3    Eigenbrodt, E.4
  • 13
    • 0032753789 scopus 로고    scopus 로고
    • Cell transformation by the E7 oncoprotein of human papillomavirus type 16: Interactions with nuclear and cytoplasmic target proteins
    • Zwerschke, W., and, Jansen-Dürr, P., (2000) Cell transformation by the E7 oncoprotein of human papillomavirus type 16: interactions with nuclear and cytoplasmic target proteins. Adv. Cancer Res. 78, 1-29.
    • (2000) Adv. Cancer Res. , vol.78 , pp. 1-29
    • Zwerschke, W.1    Jansen-Dürr, P.2
  • 14
    • 40749099894 scopus 로고    scopus 로고
    • Pyruvate kinase M2 is a phosphotyrosine-binding protein
    • DOI 10.1038/nature06667, PII NATURE06667
    • Christofk, H. R., Vander Heiden, M. G., and, Wu, N., (2008) Pyruvate kinase M2 is a phosphotyrosine-binding protein. Nature 452, 181-186. (Pubitemid 351380242)
    • (2008) Nature , vol.452 , Issue.7184 , pp. 181-186
    • Christofk, H.R.1    Vander Heiden, M.G.2    Wu, N.3    Asara, J.M.4    Cantley, L.C.5
  • 17
    • 0035909527 scopus 로고    scopus 로고
    • Metabolic cooperation between different oncogenes during cell transformation: Interaction between activated ras and HPV-16 E7
    • DOI 10.1038/sj.onc.1204792
    • Mazurek, S., Zwerschke, W., Jansen-Dürr, P., and, Eigenbrodt, E., (2001) Metabolic cooperation between different oncogenes during cell transformation: interaction between activated ras and HPV-16 E7. Oncogene 20, 6891-6898. (Pubitemid 33052178)
    • (2001) Oncogene , vol.20 , Issue.47 , pp. 6891-6898
    • Mazurek, S.1    Zwerschke, W.2    Jansen-Durr, P.3    Eigenbrodt, E.4
  • 18
    • 82155192703 scopus 로고    scopus 로고
    • MUC1-C oncoprotein regulates glycolysis and pyruvate kinase M2 activity in cancer cells
    • Kosugi, M., Ahmad, R., Alam, M., Uchida, Y., and, Kufe, D., (2011) MUC1-C oncoprotein regulates glycolysis and pyruvate kinase M2 activity in cancer cells. PLoS One 6, e28234.
    • (2011) PLoS One , vol.6
    • Kosugi, M.1    Ahmad, R.2    Alam, M.3    Uchida, Y.4    Kufe, D.5
  • 22
    • 77957275712 scopus 로고    scopus 로고
    • Present status and perspectives of colorectal cancer in Asia: Colorectal Cancer Working Group Report in 30th Asia-Pacific Cancer Conference
    • Hyodo, I., Suzuki, H., Takahashi, K., Saito, Y., Tanaka, S., Chiu, H. M., Kim, N. K., Li, J., Lim, R., Villalon, A., and, Boku, N., (2010) Present status and perspectives of colorectal cancer in Asia: Colorectal Cancer Working Group Report in 30th Asia-Pacific Cancer Conference. Jpn. J. Clin. Oncol. 40 (Suppl 1), i38-i43.
    • (2010) Jpn. J. Clin. Oncol. , vol.40 , Issue.SUPPL. 1
    • Hyodo, I.1    Suzuki, H.2    Takahashi, K.3    Saito, Y.4    Tanaka, S.5    Chiu, H.M.6    Kim, N.K.7    Li, J.8    Lim, R.9    Villalon, A.10    Boku, N.11
  • 23
    • 77955254992 scopus 로고    scopus 로고
    • Toward optimized front-line therapeutic strategies in patients with metastatic colorectal cancer-an expert review from the International Congress on Anti-Cancer Treatment (ICACT) 2009
    • Adam, R., Haller, D. G., Poston, G., Raoul, J. L., Spano, J. P., Tabernero, J., and, Van Cutsem, E., (2010) Toward optimized front-line therapeutic strategies in patients with metastatic colorectal cancer-an expert review from the International Congress on Anti-Cancer Treatment (ICACT) 2009. Ann. Oncol. 21, 1579-1584.
    • (2010) Ann. Oncol. , vol.21 , pp. 1579-1584
    • Adam, R.1    Haller, D.G.2    Poston, G.3    Raoul, J.L.4    Spano, J.P.5    Tabernero, J.6    Van Cutsem, E.7
  • 24
    • 75149150805 scopus 로고    scopus 로고
    • Prolyl hydroxylase-3 is down-regulated in colorectal cancer cells and inhibits IKKβ independent of hydroxylase activity
    • Xue, J., Li, X. B., Jiao, S., Wei, Y., Wu, G. H., and, Fang, J., (2010) Prolyl hydroxylase-3 is down-regulated in colorectal cancer cells and inhibits IKKβ independent of hydroxylase activity. Gastroenterology 138, 606-615.
    • (2010) Gastroenterology , vol.138 , pp. 606-615
    • Xue, J.1    Li, X.B.2    Jiao, S.3    Wei, Y.4    Wu, G.H.5    Fang, J.6
  • 25
    • 57349181198 scopus 로고    scopus 로고
    • Apigenin inhibited migration and invasion of human ovarian cancer A2780 cells through focal adhesion kinase
    • Hu, X. W., Meng, D., and, Fang, J., (2008) Apigenin inhibited migration and invasion of human ovarian cancer A2780 cells through focal adhesion kinase. Carcinogenesis 29, 2369-2376.
    • (2008) Carcinogenesis , vol.29 , pp. 2369-2376
    • Hu, X.W.1    Meng, D.2    Fang, J.3
  • 27
    • 8444233261 scopus 로고    scopus 로고
    • The metabolic marker tumour pyruvate kinase type M2 (tumour M2-PK) shows increased expression along the metaplasia-dysplasia-adenocarcinoma sequence in Barrett's oesophagus
    • DOI 10.1136/jcp.2004.018150
    • Koss, K., Harrison, R. F., Gregory, J., Darnton, S. J., Anderson, M. R., and, Jankowski, J. A., (2004) The metabolic marker tumour pyruvate kinase type M2 (tumour M2-PK) shows increased expression along the metaplasia-dysplasia- adenocarcinoma sequence in Barrett's oesophagus. J. Clin. Pathol. 57, 1156-1159. (Pubitemid 39486520)
    • (2004) Journal of Clinical Pathology , vol.57 , Issue.11 , pp. 1156-1159
    • Koss, K.1    Harrison, R.F.2    Gregory, J.3    Darnton, S.J.4    Anderson, M.R.5    Jankowski, J.A.Z.6
  • 28
    • 80052731244 scopus 로고    scopus 로고
    • No evidence for a shift in pyruvate kinase PKM1 to PKM2 expression during tumorigenesis
    • Bluemlein, K., Grüning, N. M., Feichtinger, R. G., Lehrach, H., Kofler, B., and, Ralser, M., (2011) No evidence for a shift in pyruvate kinase PKM1 to PKM2 expression during tumorigenesis. Oncotarget 2, 393-400.
    • (2011) Oncotarget , vol.2 , pp. 393-400
    • Bluemlein, K.1    Grüning, N.M.2    Feichtinger, R.G.3    Lehrach, H.4    Kofler, B.5    Ralser, M.6
  • 29
    • 68949098403 scopus 로고    scopus 로고
    • Pyruvate kinase isoenzyme M2 is a glycolytic sensor differentially regulating cell proliferation, cell size and apoptotic cell death-dependent on glucose supply
    • Spoden, G. A., Rostek, U., Lechner, S., Mitterberger, M., Mazurek, S., and, Zwerschke, W., (2009) Pyruvate kinase isoenzyme M2 is a glycolytic sensor differentially regulating cell proliferation, cell size and apoptotic cell death-dependent on glucose supply. Exp. Cell Res. 315, 2765-2774.
    • (2009) Exp. Cell Res. , vol.315 , pp. 2765-2774
    • Spoden, G.A.1    Rostek, U.2    Lechner, S.3    Mitterberger, M.4    Mazurek, S.5    Zwerschke, W.6
  • 30
    • 0035717984 scopus 로고    scopus 로고
    • Metabolic mapping with bioluminescence: Basic and clinical relevance
    • DOI 10.1016/S1389-0344(01)00107-1, PII S1389034401001071
    • Walenta, S., Schroeder, T., and, Mueller-Klieser, W., (2002) Metabolic mapping with bioluminescence: basic and clinical relevance. Biomol. Eng. 18, 249-262. (Pubitemid 34158559)
    • (2002) Biomolecular Engineering , vol.18 , Issue.6 , pp. 249-262
    • Walenta, S.1    Schroeder, T.2    Mueller-Klieser, W.3
  • 31
    • 0037325180 scopus 로고    scopus 로고
    • Breast cancer stromal myxoid changes are associated with tumor invasion and metastasis: A central role for hyaluronan
    • DOI 10.1097/01.MP.0000051582.75890.2D
    • Wernicke, M., Pineiro, L. C., Caramutti, D., Dorn, V. G., Raffo, M. M., Guixa, H. G., Telenta, M., and, Morandi, A. A., (2003) Breast cancer stromal myxoid changes are associated with tumor invasion and metastasis: a central role for hyaluronan. Mod. Pathol. 16, 99-107. (Pubitemid 36245740)
    • (2003) Modern Pathology , vol.16 , Issue.2 , pp. 99-107
    • Wernicke, M.1    Pineiro, L.C.2    Caramutti, D.3    Dorn, V.G.4    Raffo, M.M.L.5    Guixa, H.G.6    Telenta, M.7    Morandi, A.A.8
  • 32
    • 0037207873 scopus 로고    scopus 로고
    • Laminin γ2-chain fragment in the circulation: A prognostic indicator of epithelial tumor invasion
    • Katayama, M., Sanzen, N., Funakoshi, A., and, Sekiguchi, K., (2003) Laminin gamma2-chain fragment in the circulation: a prognostic indicator of epithelial tumor invasion. Cancer Res. 63, 222-229. (Pubitemid 36070443)
    • (2003) Cancer Research , vol.63 , Issue.1 , pp. 222-229
    • Katayama, M.1    Sanzen, N.2    Funakoshi, A.3    Sekiguchi, K.4    Fukushima, Y.5
  • 33
    • 32044459728 scopus 로고    scopus 로고
    • Tumorigenesis suppressor Pdcd4 down-regulates mitogen-activated protein kinase kinase kinase kinase 1 expression to suppress colon carcinoma cell invasion
    • DOI 10.1128/MCB.26.4.1297-1306.2006
    • Yang, H. S., Matthews, C. P., Clair, T., Wang, Q., Baker, A. R., Li, C. C., Tan, T. H., and, Colburn, N. H., (2006) Tumorigenesis suppressor Pdcd4 down-regulates mitogen-activated protein kinase kinase kinase kinase 1 expression to suppress colon carcinoma cell invasion. Mol. Cell Biol. 26, 1297-1306. (Pubitemid 43202557)
    • (2006) Molecular and Cellular Biology , vol.26 , Issue.4 , pp. 1297-1306
    • Yang, H.-S.1    Matthews, C.P.2    Clair, T.3    Wang, Q.4    Baker, A.R.5    Li, C.-C.H.6    Tan, T.-H.7    Colburn, N.H.8
  • 35
    • 0034652620 scopus 로고    scopus 로고
    • High lactate levels predict likelihood of metastases, tumor recurrence, and restricted patient survival in human cervical cancers
    • Walenta, S., Wetterling, M., Lehrke, M., Schwickert, G., Sundfør, K., Rofstad, E. K., and, Mueller-Klieser, W., (2000) High lactate levels predict likelihood of metastases, tumor recurrence, and restricted patient survival in human cervical cancers. Cancer Res. 60, 916-921. (Pubitemid 30129526)
    • (2000) Cancer Research , vol.60 , Issue.4 , pp. 916-921
    • Walenta, S.1    Wetterling, M.2    Lehrke, M.3    Schwickert, G.4    Sundfor, K.5    Rofstad, E.K.6    Mueller-Klieser, W.7
  • 39
    • 46749121459 scopus 로고    scopus 로고
    • Causes and consequences of increased glucose metabolism of cancers
    • DOI 10.2967/jnumed.107.047258
    • Gillies, R. J., Robey, I., and, Gatenby, R. A., (2008) Causes and consequences of increased glucose metabolism of cancers. J. Nucl. Med. 49 (Suppl 2), 24S-42S. (Pubitemid 351948035)
    • (2008) Journal of Nuclear Medicine , vol.49 , Issue.SUPPL.6
    • Gillies, R.J.1    Robey, I.2    Gatenby, R.A.3
  • 40
    • 8144228566 scopus 로고    scopus 로고
    • Why do cancers have high aerobic glycolysis?
    • DOI 10.1038/nrc1478
    • Gatenby, R. A., and, Gillies, R. J., (2004) Why do cancers have high aerobic glycolysis? Nat. Rev. 4, 891-899. (Pubitemid 39472955)
    • (2004) Nature Reviews Cancer , vol.4 , Issue.11 , pp. 891-899
    • Gatenby, R.A.1    Gillies, R.J.2
  • 41
    • 79960029992 scopus 로고    scopus 로고
    • Lactate enhances motility of tumor cells and inhibits monocyte migration and cytokine release
    • Goetze, K., Walenta, S., Ksiazkiewicz, M., Kunz-Schughart, L. A., and, Mueller-Klieser, W., (2011) Lactate enhances motility of tumor cells and inhibits monocyte migration and cytokine release. Int. J. Oncol. 39, 453-463.
    • (2011) Int. J. Oncol. , vol.39 , pp. 453-463
    • Goetze, K.1    Walenta, S.2    Ksiazkiewicz, M.3    Kunz-Schughart, L.A.4    Mueller-Klieser, W.5
  • 44
    • 79953329777 scopus 로고    scopus 로고
    • Lactate influx through the endothelial cell monocarboxylate transporter MCT1 supports an NF-κB/IL-8 pathway that drives tumor angiogenesis
    • Végran, F., Boidot, R., Michiels, C., Sonveaux, P., and, Feron, O., (2011) Lactate influx through the endothelial cell monocarboxylate transporter MCT1 supports an NF-κB/IL-8 pathway that drives tumor angiogenesis. Cancer Res. 71, 2550-2560.
    • (2011) Cancer Res. , vol.71 , pp. 2550-2560
    • Végran, F.1    Boidot, R.2    Michiels, C.3    Sonveaux, P.4    Feron, O.5
  • 45
    • 34447547148 scopus 로고    scopus 로고
    • Regulation of tumor pH and the role of carbonic anhydrase 9
    • DOI 10.1007/s10555-007-9064-0, Special issue on Hypoxia and Cancer, Guest Editor: Gregg L. Semenza
    • Swietach, P., Vaughan-Jones, R. D., and, Harris, A. L., (2007) Regulation of tumor pH and the role of carbonic anhydrase 9. Cancer Metastasis Rev. 26, 299-310. (Pubitemid 47101667)
    • (2007) Cancer and Metastasis Reviews , vol.26 , Issue.2 , pp. 299-310
    • Swietach, P.1    Vaughan-Jones, R.D.2    Harris, A.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.