α-enolase, a multifunctional protein: Its role on pathophysiological situations

Journal of Biomedicine and Biotechnology

Volumn 2012, Issue , 2012, Pages

  Díaz Ramos, Àngels ^a   Roig Borrellas, Anna ^a   García Melero, Ana ^a   López Alemany, Roser ^a  

^a BELLVITGE BIOMEDICAL RESEARCH INSTITUTE IDIBELL   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA ENOLASE; DESMIN; INTERLEUKIN 8; PLASMINOGEN; ENOLASE;

ALZHEIMER DISEASE; APOPTOSIS; CARCINOGENESIS; CELL SURFACE; CELL TYPE; COLON CANCER; EXTRACELLULAR MATRIX; HUMAN; INTRACELLULAR SIGNALING; MUSCLE DEVELOPMENT; MUSCLE REGENERATION; NONHUMAN; PANCREAS ADENOCARCINOMA; PATHOPHYSIOLOGY; PLASMINOGEN ACTIVATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROCESSING; REVIEW; RHEUMATOID ARTHRITIS; ANIMAL; DISEASES; METABOLISM; SIGNAL TRANSDUCTION;

EUKARYOTA; MUS; PROKARYOTA;

ANIMALS; APOPTOSIS; DISEASE; HUMANS; MUSCLE DEVELOPMENT; PHOSPHOPYRUVATE HYDRATASE; PLASMINOGEN; SIGNAL TRANSDUCTION;

EID: 84869025512     PISSN: 11107243     EISSN: 11107251     Source Type: Journal    
DOI: 10.1155/2012/156795     Document Type: Review

References (142)

1. Pancholi V., Multifunctional α -enolase: its role in diseases. Cellular and Molecular Life Sciences 2001 58 7 902 920 2-s2.0-0034947535 (Pubitemid 32652817)
2. Piast M., Kustrzeba-Wójcicka I., Matusiewicz M., Banaś T., Molecular evolution of enolase. Acta Biochimica Polonica 2005 52 2 507 513 2-s2.0-23644438393 (Pubitemid 41133788)
3. Marangos P. J., Parma A. M., Goodwin F. K., Functional properties of neuronal and glial isoenzymes of brain enolase. Journal of Neurochemistry 1978 31 3 727 732 2-s2.0-0018103888 (Pubitemid 8401303)
4. Feo S., Oliva D., Barbieri G., Xu W., Fried M., Giallongo A., The gene for the muscle-specific enolase is on the short arm of human chromosome 17. Genomics 1990 6 1 192 194 2-s2.0-0025372882 10.1016/0888-7543(90)90467-9 (Pubitemid 20172373)
5. Giallongo A., Feo S., Moore R., Croce C. M., Showe L. C., Molecular cloning and nucleotide sequence of a full-length cDNA for human α enolase. Proceedings of the National Academy of Sciences of the United States of America 1986 83 18 6741 6745 2-s2.0-0038464170 (Pubitemid 16002309)
6. Fletcher L., Rider C. C., Taylor C. B., Enolase isoenzymes. III. Chromatographic and immunological characteristics of rat brain enolase. Biochimica et Biophysica Acta 1976 452 1 245 252 2-s2.0-0017104529
7. Kato K., Okagawa Y., Suzuki F., Shimizu A., Mokuno K., Takahashi Y., Immunoassay of human muscle enolase subunit in serum: a novel marker antigen for muscle diseases. Clinica Chimica Acta 1983 131 1-2 75 85 2-s2.0-0020629120 (Pubitemid 13105536)
8. Lebioda L., Stec B., Crystal structure of enolase indicates that enolase and pyruvate kinase evolved from a common ancestor. Nature 1988 333 6174 683 686 2-s2.0-0024289934
9. Zhang E., Brewer J. M., Minor W., Carreira L. A., Lebioda L., Mechanism of enolase: the crystal structure of asymmetric dimer enolase- 2-phospho-D-glycerate/enolase-phosphoenolpyruvate at 2.0 A resolution. Biochemistry 1997 36 41 12526 12534 2-s2.0-0030827288 10.1021/bi9712450 (Pubitemid 27446676)
10. Kang H. J., Jung S. K., Kim S. J., Chung S. J., Structure of human α -enolase (hENO1), a multifunctional glycolytic enzyme. Acta Crystallographica D 2008 64 6 651 657 2-s2.0-45749150355 10.1107/ S0907444908008561 (Pubitemid 351872066)
11. McAlister L., Holland M. J., Targeted deletion of a yeast enolase structural gene. Identification and isolation of yeast enolase isozymes. Journal of Biological Chemistry 1982 257 12 7181 7188 2-s2.0-0020490759
12. Holland J. P., Labieniec L., Swimmer C., Holland M. J., Homologous nucleotide sequences at the 5' termini of messenger RNAs synthesized from the yeast enolase and glyceraldehyde-3-phosphate dehydrogenase gene families. The primary structure of a third yeast glyceraldehyde-3-phosphate dehydrogenase gene. Journal of Biological Chemistry 1983 258 8 5291 5299 2-s2.0-0020575745 (Pubitemid 13096423)
13. Giallongo A., Oliva D., Calì L., Barba G., Barbieri G., Feo S., Structure of the human gene for alpha-enolase. European Journal of Biochemistry 1990 190 3 567 573 2-s2.0-0025700710
14. Feo S., Arcuri D., Piddini E., Passantino R., Giallongo A., ENO1 gene product binds to the c-myc promoter and acts as a transcriptional repressor: relationship with Myc promoter-binding protein 1 (MBP-1). FEBS Letters 2000 473 1 47 52 2-s2.0-0034604055 10.1016/S0014-5793(00)01494-0 (Pubitemid 30235183)
15. Miles L. A., Dahlberg C. M., Plescia J., Felez J., Kato K., Plow E. F., Role of cell-surface lysines in plasminogen binding to cells: identification of α -enolase as a candidate plasminogen receptor. Biochemistry 1991 30 6 1682 1691 2-s2.0-0025819231
16. Nakajima K., Hamanoue M., Takemoto N., Hattori T., Kato K., Kohsaka S., Plasminogen binds specifically to α -enolase on rat neuronal plasma membrane. Journal of Neurochemistry 1994 63 6 2048 2057 2-s2.0-0027948296 (Pubitemid 24369977)
17. Dudani A. K., Cummings C., Hashemi S., Ganz P. R., Isolation of a novel 45 kDa plasminogen receptor from human endothelial cells. Thrombosis Research 1993 69 2 185 196 2-s2.0-0027403372 10.1016/0049-3848(93)90044-O (Pubitemid 23068243)
18. Redlitz A., Fowler B. J., Plow E. F., Miles L. A., The role of an enolase-related molecule in plasminogen binding to cells. European Journal of Biochemistry 1995 227 1-2 407 415 2-s2.0-0028839088 10.1111/j.1432-1033.1995. tb20403.x
19. Fontan P. A., Pancholi V., Nociari M. M., Fischetti V. A., Antibodies to streptococcal surface enolase react with human α -enolase: implications in poststreptococcal sequelae. Journal of Infectious Diseases 2000 182 6 1712 1721 2-s2.0-0033680465 10.1086/317604
20. Takei N., Kondo J., Nagaike K., Ohsawa K., Kato K., Kohsaka S., Neuronal survival factor from bovine brain is identical to neuron-specific enolase. Journal of Neurochemistry 1991 57 4 1178 1184 2-s2.0-0025945872 (Pubitemid 21922739)
21. Iida H., Yahara I., Yeast heat-shock protein of M(r) 48,000 is an isoprotein of enolase. Nature 1985 315 6021 688 690 2-s2.0-0021984720 (Pubitemid 15232887)
22. Aaronson R. M., Graven K. K., Tucci M., McDonald R. J., Farber H. W., Non-neuronal enolase is an endothelial hypoxic stress protein. Journal of Biological Chemistry 1995 270 46 27752 27757 2-s2.0-0028856318 10.1074/jbc.270.46.27752
23. Mathur R. L., Reddy M. C., Yee S., Imbesi R., Groth-Vasselli B., Farnsworth P. N., Investigation of lens glycolytic enzymes: species distribution and interaction with supramolecular order. Experimental Eye Research 1992 54 2 253 260 2-s2.0-0026609068
24. Walsh J. L., Keith T. J., Knull H. R., Glycolytic enzyme interactions with tubulin and microtubules. Biochimica et Biophysica Acta 1989 999 1 64 70 2-s2.0-0024342987 (Pubitemid 19264349)
25. Johnstone S. A., Waisman D. M., Rattner J. B., Enolase is present at the centrosome of HeLa cells. Experimental Cell Research 1992 202 2 458 463 2-s2.0-0026693656 10.1016/0014-4827(92)90099-T
26. Merkulova T., Lucas M., Jabet C., Lamande N., Rouzeau J. D., Gros F., Lazar M., Keller A., Biochemical characterization of the mouse muscle-specific enolase: developmental changes in electrophoretic variants and selective binding to other proteins. Biochemical Journal 1997 323 3 791 800 2-s2.0-0030908790 (Pubitemid 27202351)
27. Subramanian A., Miller D. M., Structural analysis of α -enolase: mapping the functional domains involved in down-regulation of the c-myc protooncogene. Journal of Biological Chemistry 2000 275 8 5958 5965 2-s2.0-0034009502 10.1074/jbc.275.8.5958 (Pubitemid 30115245)
28. Eriksson B., Öberg K., Stridsberg M., Tumor markers in neuroendocrine tumors. Digestion 2000 62 supplement 1 33 38 2-s2.0-0033843657 (Pubitemid 30665937)
29. Niklinski J., Furman M., Clinical tumour markers in lung cancer. European Journal of Cancer Prevention 1995 4 2 129 138 2-s2.0-0028942282
30. Cooper E. H., Neuron-specific enolase. International Journal of Biological Markers 1994 9 4 205 210 2-s2.0-0027949337 (Pubitemid 24350340)
31. Ledermann J. A., Serum neurone-specific enolase and other neuroendocrine markers in lung cancer. European Journal of Cancer A 1994 30 5 574 576 2-s2.0-0028236442 10.1016/0959-8049(94)90519-3 (Pubitemid 24164234)
32. Takashima M., Kuramitsu Y., Yokoyama Y., Iizuka N., Fujimoto M., Nishisaka T., Okita K., Oka M., Nakamura K., Overexpression of alpha enolase in hepatitis C virus-related hepatocellular carcinoma: association with tumor progression as determined by proteomic analysis. Proteomics 2005 5 6 1686 1692 2-s2.0-17844380283 10.1002/pmic.200401022 (Pubitemid 40593274)
33. Jeffery C. J., Moonlighting proteins. Trends in Biochemical Sciences 1999 24 1 8 11 2-s2.0-0033048066 10.1016/S0968-0004(98)01335-8 (Pubitemid 29074455)
34. Piatigorsky J., Multifunctional lens crystallins and corneal enzymes: more than meets the eye. Annals of the New York Academy of Sciences 1998 842 7 15 2-s2.0-0031970686
35. Irigoyen J. P., Muñoz-Cánoves P., Montero L., Koziczak M., Nagamine Y., The plasminogen activator system: biology and regulation. Cellular and Molecular Life Sciences 1999 56 1-2 104 132 2-s2.0-0033213996 (Pubitemid 29471930)
36. Miles L. A., Plow E. F., Binding and activation of plasminogen on the platelet surface. Journal of Biological Chemistry 1985 260 7 4303 4311 2-s2.0-0022001189 (Pubitemid 15091978)
37. Hajjar K. A., Harpel P. C., Jaffe E. A., Nachman R. L., Binding of plasminogen to cultured human endothelial cells. Journal of Biological Chemistry 1986 261 25 11656 11662 2-s2.0-0022978141 (Pubitemid 17206086)
38. Plow E. F., Freaney D. E., Plescia J., Miles L. A., The plasminogen system and cell surfaces: evidence for plasminogen and urokinase receptors on the same cell type. Journal of Cell Biology 1986 103 6 2411 2420 2-s2.0-0023025270 (Pubitemid 17216665)
39. Miles L. A., Plow E. F., Receptor mediated binding of the fibrinolytic components, plasminogen and urokinase, to peripheral blood cells. Thrombosis and Haemostasis 1987 58 3 936 942 2-s2.0-0023624310 (Pubitemid 18020467)
40. Blasi F., Carmeliet P., uPAR: a versatile signalling orchestrator. Nature Reviews Molecular Cell Biology 2002 3 12 932 943 2-s2.0-0036906177 10.1038/nrm977 (Pubitemid 35477371)
41. Ossowski L., Aguirre-Ghiso J. A., Urokinase receptor and integrin partnership: coordination of signaling for cell adhesion, migration and growth. Current Opinion in Cell Biology 2000 12 5 613 620 2-s2.0-0033824172 10.1016/S0955-0674(00)00140-X
42. Lopez-Alemany R., Correc P., Camoin L., Burtin P., Purification of the plasmin receptor from human carcinoma cells and comparison to α -enolase. Thrombosis Research 1994 75 4 371 381 2-s2.0-0028133563 10.1016/0049-3848(94) 90252-6 (Pubitemid 24265070)
43. Hajjar K. A., Jacovina A. T., Chacko J., An endothelial cell receptor for plasminogen/tissue plasminogen activator. I. Identity with annexin II. Journal of Biological Chemistry 1994 269 33 21191 21197 2-s2.0-0028023538
44. Kassam G., Le B. H., Choi K. S., Kang H. M., Fitzpatrick S. L., Louie P., Waisman D. M., The p11 subunit of the annexin II tetramer plays a key role in the stimulation of t-PA-dependent plasminogen activation. Biochemistry 1998 37 48 16958 16966 2-s2.0-0032374094 10.1021/bi981713l (Pubitemid 28566773)
45. Herren T., Burke T. A., Das R., Plow E. F., Identification of histone H2B as a regulated plasminogen receptor. Biochemistry 2006 45 31 9463 9474 2-s2.0-33747093008 10.1021/bi060756w (Pubitemid 44223250)
46. Das R., Burke T., Plow E. F., Histone H2B as a functionally important plasminogen receptor on macrophages. Blood 2007 110 10 3763 3772 2-s2.0-36348985036 10.1182/blood-2007-03-079392 (Pubitemid 350159647)
47. Dudani A. K., Ganz P. R., Endothelial cell surface actin serves as a binding site for plasminogen, tissue plasminogen activator and lipoprotein(a). British Journal of Haematology 1996 95 1 168 178 2-s2.0-0029817448 (Pubitemid 26340247)
48. Kanalas J. J., Makker S. P., Identification of the rat Heymann nephritis autoantigen (GP330) as a receptor site for plasminogen. Journal of Biological Chemistry 1991 266 17 10825 10829 2-s2.0-0025833080 (Pubitemid 21906879)
49. Hembrough T. A., Li L., Gonias S. L., Cell-surface cytokeratin 8 is the major plasminogen receptor on breast cancer cells and is required for the accelerated activation of cell- associated plasminogen by tissue-type plasminogen activator. Journal of Biological Chemistry 1996 271 41 25684 25691 2-s2.0-0029795405 10.1074/jbc.271.41.25684 (Pubitemid 26337950)
50. Borza D. B., Morgan W. T., Acceleration of plasminogen activation by tissue plasminogen activator on surface-bound histidine-proline-rich glycoprotein. Journal of Biological Chemistry 1997 272 9 5718 5726 2-s2.0-0031041077 10.1074/jbc.272.9.5718 (Pubitemid 27102400)
51. Winram S. B., Lottenberg R., The plasmin-binding protein Plr of group A streptococci is identified as glyceraldehyde-3-phosphate dehydrogenase. Microbiology 1996 142 8 2311 2320 2-s2.0-0029799009 (Pubitemid 26288107)
52. Andronicos N. M., Chen E. I., Baik N., Bai H., Parmer C. M., Kiosses W. B., Kamps M. P., Yates J. R., Parmer R. J., Miles L. A., Proteomics-based discovery of a novel, structurally unique, and developmentally regulated plasminogen receptor, Plg-RKT, a major regulator of cell surface plasminogen activation. Blood 2010 115 7 1319 1330 2-s2.0-77949897126 10.1182/blood-2008-11- 188938
53. Felez J., Plasminogen binding to cell surfaces. Fibrinolysis and Proteolysis 1998 12 4 183 189 2-s2.0-0031735770 (Pubitemid 28539225)
54. López-Alemany R., Longstaff C., Hawley S., Mirshahi M., Fábregas P., Jardí M., Merton E., Miles L. A., Félez J., Inhibition of cell surface mediated plasminogen activation by a monoclonal antibody against α -enolase. American Journal of Hematology 2003 72 4 234 242 2-s2.0-0037381992 10.1002/ajh.10299 (Pubitemid 36383973)
55. Longstaff C., Merton R. E., Fabregas P., Felez J., Characterization of cell-associated plasminogen activation catalyzed by urokinase-type plasminogen activator, but independent of urokinase receptor (uPAR, CD87). Blood 1999 93 11 3839 3846 2-s2.0-0033153103 (Pubitemid 29249831)
56. Sinniger V., Mertont R. E., Fabregas P., Felez J., Longstaff C., Regulation of tissue plasminogen activator activity by cells: domains responsible for binding and mechanism of stimulation. Journal of Biological Chemistry 1999 274 18 12414 12422 2-s2.0-0033617285 10.1074/jbc.274.18.12414 (Pubitemid 29215472)
57. Félez J., Miles L. A., Fábregas P., Jardí M., Plow E. F., Lijnen R. H., Characterization of cellular binding sites and interactive regions within reactants required for enhancement of plasminogen activation by tPA on the surface of leukocytic cells. Thrombosis and Haemostasis 1996 76 4 577 584 2-s2.0-0029805471 (Pubitemid 26372014)
58. Miles L. A., Fless G. M., Scanu A. M., Baynham P., Sebald M. T., Skocir P., Curtiss L. K., Levin E. G., Hoover-Plow J. L., Plow E. F., Interaction of Lp(a) with plasminogen binding sites on cells. Thrombosis and Haemostasis 1995 73 3 458 465 2-s2.0-0028927338
59. Wygrecka M., Marsh L. M., Morty R. E., Henneke I., Guenther A., Lohmeyer J., Markart P., Preissner K. T., Enolase-1 promotes plasminogen-mediated recruitment of monocytes to the acutely inflamed lung. Blood 2009 113 22 5588 5598 2-s2.0-67049088421 10.1182/blood-2008-08-170837
60. von Heijne G., Liljestrom P., Mikus P., Andersson H., Ny T., The efficiency of the uncleaved secretion signal in the plasminogen activator inhibitor type 2 protein can be enhanced by point mutations that increase its hydrophobicity. Journal of Biological Chemistry 1991 266 23 15240 15243 2-s2.0-0025868410 (Pubitemid 21907640)
61. Bottalico L. A., Kendrick N. C., Keller A., Li Y., Tabas I., Cholesteryl ester loading of mouse peritoneal macrophages is associated with changes in the expression or modification of specific cellular proteins, including increase in an α -enolase isoform. Arteriosclerosis and Thrombosis 1993 13 2 264 275 2-s2.0-0027397616 (Pubitemid 23056800)
62. Cooper J. A., Esch F. S., Taylor S. S., Hunter T., Phosphorylation sites in enolase and lactate dehydrogenase utilized by tyrosine protein kinase in vivo and in vitro. Journal of Biological Chemistry 1984 259 12 7835 7841 2-s2.0-0021254544 (Pubitemid 14081202)
63. Lluís F., Roma J., Suelves M., Parra M., Aniorte G., Gallardo E., Illa I., Rodríguez L., Hughes S. M., Carmeliet P., Roig M., Muñoz-Cánoves P., Urokinase-dependent plasminogen activation is required for efficient skeletal muscle regeneration in vivo. Blood 2001 97 6 1703 1711 2-s2.0-0035869496 10.1182/blood.V97.6.1703 (Pubitemid 32217237)
64. Suelves M., López-Alemany R., Lluís F., Aniorte G., Serrano E., Parra M., Carmeliet P., Muñoz-Cánoves P., Plasmin activity is required for myogenesis in vitro and skeletal muscle regeneration in vivo. Blood 2002 99 8 2835 2844 2-s2.0-0037089235 10.1182/blood.V99.8.2835 (Pubitemid 34525372)
65. Suelves M., Vidal B., Ruiz V., Baeza-Raja B., Diaz-Ramos A., Cuartas I., Lluis F., Parra M., Jardi M., Lopez-Alemany R., Serrano A. L., Munoz-Canoves P., The plasminogen activation system in skeletal muscle regeneration: antagonistic roles of Urokinase-type Plasminogen Activator (UPA) and its inhibitor (PAI-1). Frontiers in Bioscience 2005 10 3 2978 2985 2-s2.0-21344452350 (Pubitemid 40910536)
66. Suelves M., Vidal B., Serrano A. L., Tjwa M., Roma J., López-Alemany R., Luttun A., De Lagrán M. M., Díaz M. À., Jardí M., Roig M., Dierssen M., Dewerchin M., Carmeliet P., Muñoz-Cánoves P., uPA deficiency exacerbates muscular dystrophy in MDX mice. Journal of Cell Biology 2007 178 6 1039 1051 2-s2.0-34548829943 10.1083/jcb.200705127 (Pubitemid 47443325)
67. Fibbi G., Barletta E., Dini G., Del Rosso A., Pucci M., Cerletti M., Del Rosso M., Cell invasion is affected by differential expression of urokinase plasminogen activator/urokinase plasminogen activator receptor system in muscle satellite cells from normal and dystrophic patients. Laboratory Investigation 2001 81 1 27 39 2-s2.0-0035137484 (Pubitemid 32108637)
68. Taylor J. M., Davies J. D., Peterson C. A., Regulation of the myoblast-specific expression of the human β -enolase gene. Journal of Biological Chemistry 1995 270 6 2535 2540 2-s2.0-0028842013 10.1074/jbc.270.6. 2535
69. Fougerousse F., Edom-Vovard F., Merkulova T., Ott M. O., Durand M., Butler-Browne G., Keller A., The muscle-specific enolase is an early marker of human myogenesis. Journal of Muscle Research and Cell Motility 2001 22 6 535 544 2-s2.0-0035736222 10.1023/A:1015008208007 (Pubitemid 34461797)
70. Keller A., Peltzer J., Carpentier G., Horváth I., Oláh J., Duchesnay A., Orosz F., Ovádi J., Interactions of enolase isoforms with tubulin and microtubules during myogenesis. Biochimica et Biophysica Acta 2007 1770 6 919 926 2-s2.0-34247260876 10.1016/j.bbagen.2007.01.015 (Pubitemid 46617030)
71. Merkulova T., Dehaupas M., Nevers M. C., Créminon C., Alameddine H., Keller A., Differential modulation of α β and γ enolase isoforms in regenerating mouse skeletal muscle. European Journal of Biochemistry 2000 267 12 3735 3743 2-s2.0-0033921682 10.1046/j.1432-1327.2000.01408.x (Pubitemid 30423036)
72. López-Alemany R., Suelves M., Muñoz-Cánoves P., Plasmin generation dependent on α -enolase-type plasminogen receptor is required for myogenesis. Thrombosis and Haemostasis 2003 90 4 724 733 2-s2.0-0142061003 (Pubitemid 37287642)
73. Bryer S. C., Koh T. J., The urokinase-type plasminogen activator receptor is not required for skeletal muscle inflammation or regeneration. American Journal of Physiology 2007 293 3 R1152 R1158 2-s2.0-34548396678 10.1152/ajpregu.00132.2007 (Pubitemid 47358936)
74. Yan L., Ge H., Li H., Lieber S. C., Natividad F., Resuello R. R. G., Kim S. J., Akeju S., Sun A., Loo K., Peppas A. P., Rossi F., Lewandowski E. D., Thomas A. P., Vatner S. F., Vatner D. E., Gender-specific proteomic alterations in glycolytic and mitochondrial pathways in aging monkey hearts. Journal of Molecular and Cellular Cardiology 2004 37 5 921 929 2-s2.0-7444251178 10.1016/j.yjmcc.2004.06.012 (Pubitemid 39446817)
75. Zhu L. A., Fang N. Y., Gao P. J., Jin X., Wang H. Y., Differential expression of α -enolase in the normal and pathological cardiac growth. Experimental and Molecular Pathology 2009 87 1 27 31 2-s2.0-67649422687 10.1016/j.yexmp.2009.05.002
76. Mizukami Y., Iwamatsu A., Aki T., Kimura M., Nakamura K., Nao T., Okusa T., Matsuzaki M., Yoshida K. I., Kobayashi S., ERK1/2 regulates intracellular ATP levels through α -enolase expression in cardiomyocytes exposed to ischemic hypoxia and reoxygenation. Journal of Biological Chemistry 2004 279 48 50120 50131 2-s2.0-9644266707 10.1074/jbc.M402299200 (Pubitemid 39577824)
77. Mair J., Progress in myocardial damage detection: new biochemical markers for clinicians. Critical Reviews in Clinical Laboratory Sciences 1997 34 1 1 66 2-s2.0-0030936680 (Pubitemid 27129513)
78. Kim H. E., Dalal S. S., Young E., Legato M. J., Weisfeldt M. L., D'Armiento J., Disruption of the myocardial extracellular matrix leads to cardiac dysfunction. Journal of Clinical Investigation 2000 106 7 857 866 2-s2.0-0033802162
79. Heymans S., Luttun A., Nuyens D., Theilmeier G., Creemers E., Moons L., Dyspersin G. D., Cleutjens J. P. M., Shipley M., Angellilo A., Levi M., Nübe O., Baker A., Keshet E., Lupu F., Herbert J. M., Smits J. F. M., Shapiro S. D., Baes M., Borgers M., Collen D., Daemen M. J. A. P., Carmeliet P., Inhibition of plasminogen activators or matrix metalloproteinases prevents cardiac rupture but impairs therapeutic angiogenesis and causes cardiac failure. Nature Medicine 1999 5 10 1135 1142 2-s2.0-0032826035 10.1038/13459 (Pubitemid 29474417)
80. Creemers E., Cleutjens J., Smits J., Heymans S., Moons L., Collen D., Daemen M., Carmeliet P., Disruption of the plasminogen gene in mice abolishes wound healing after myocardial infarction. American Journal of Pathology 2000 156 6 1865 1873 2-s2.0-0033881033 (Pubitemid 30641756)
81. Macfelda K., Weiss T. W., Kaun C., Breuss J. M., Kapeller B., Zorn G., Oberndorfer U., Voegele-Kadletz M., Huber-Beckmann R., Ullrich R., Binder B. R., Losert U. M., Maurer G., Pacher R., Huber K., Wojta J., Plasminogen activator inhibitor 1 expression is regulated by the inflammatory mediators interleukin-1 α tumor necrosis factor- α transforming growth factor- β and oncostatin M in human cardiac myocytes. Journal of Molecular and Cellular Cardiology 2002 34 12 1681 1691 2-s2.0-18744386925 10.1006/jmcc.2002.2117 (Pubitemid 35454482)
82. Takeshita K., Hayashi M., Iino S., Kondo T., Inden Y., Iwase M., Kojima T., Hirai M., Ito M., Loskutoff D. J., Saito H., Murohara T., Yamamoto K., Increased expression of plasminogen activator inhibitor-1 in cardiomyocytes contributes to cardiac fibrosis after myocardial infarction. American Journal of Pathology 2004 164 2 449 456 2-s2.0-1542289735 (Pubitemid 38364661)
83. Carroll S. M., Nimmo L. E., Knoepfler P. S., White F. C., Bloor C. M., Gene expression in a swine model of right ventricular hypertrophy: intercellular adhesion molecule, vascular endothelial growth factor and plasminogen activators are upregulated during pressure overload. Journal of Molecular and Cellular Cardiology 1995 27 7 1427 1441 2-s2.0-0029120866 10.1006/jmcc.1995.0135
84. Pasumarthi K. B. S., Field L. J., Cardiomyocyte cell cycle regulation. Circulation Research 2002 90 10 1044 1054 2-s2.0-0037205320 10.1161/01.RES. 0000020201.44772.67 (Pubitemid 34627902)
85. Olivetti G., Abbi R., Quaini F., Kajstura J., Cheng W., Nitahara J. A., Quaini E., Di Loreto C., Beltrami C. A., Krajewski S., Reed J. C., Anversa P., Apoptosis in the failing human heart. The New England Journal of Medicine 1997 336 16 1131 1141 2-s2.0-0030766192 10.1056/NEJM199704173361603 (Pubitemid 27374695)
86. Guerra S., Leri A., Wang X., Finato N., Di Loreto C., Beltrami C. A., Kajstura J., Anversa P., Myocyte death in the failing human heart is gender dependent. Circulation Research 1999 85 9 856 866 2-s2.0-0032724201 (Pubitemid 29504161)
87. Ho-Tin-Noé B., Rojas G., Vranckx R., Lijnen H. R., Anglés-Cano E., Functional hierarchy of plasminogen kringles 1 and 4 in fibrinolysis and plasmin-induced cell detachment and apoptosis. FEBS Journal 2005 272 13 3387 3400 2-s2.0-22144488826 10.1111/j.1742-4658.2005.04754.x (Pubitemid 40979309)
88. Meilhac O., Ho-Tin-Noé B., Houard X., Philippe M., Michel J. B., Anglés-Cano E., Pericellular plasmin induces smooth muscle cell anoikis. The FASEB Journal 2003 17 10 1301 1303 2-s2.0-0037590158
89. Ho-Tin-Noé B., Enslen H., Doeuvre L., Corsi J. M., Lijnen H. R., Anglés-Cano E., Role of plasminogen activation in neuronal organization and survival. Molecular and Cellular Neuroscience 2009 42 4 288 295 2-s2.0-70449525143 10.1016/j.mcn.2009.08.001
90. Kochtebane N., Choqueux C., Passefort S., Nataf P., Messika-Zeitoun D., Bartagi A., Michel J. B., Anglés-Cano E., Jacob M. P., Plasmin induces apoptosis of aortic valvular myofibroblasts. Journal of Pathology 2010 221 1 37 48 2-s2.0-77951020329 10.1002/path.2681
91. Ucker D. S., Jain M. R., Pattabiraman G., Palasiewicz K., Birge R. B., Li H., Externalized glycolytic enzymes are novel, conserved, and early biomarkers of apoptosis. Journal of Biological Chemistry 2012 287 10625 10343
92. Herrmann M., Voll R. E., Zoller O. M., Hagenhofer M., Ponner B. B., Kalden J. R., Impaired phagocytosis of apoptotic cell material by monocyte-derived macrophages from patients with systemic lupus erythematosus. Arthritis and Rheumatism 1998 41 1241 1250 (Pubitemid 28313427)
93. Cohen P. L., Caricchio R., Abraham V., Camenisch T. D., Charles Jennette J., Roubey R. A. S., Shelton Earp H., Matsushima G., Reap E. A., Delayed apoptotic cell clearance and lupus-like autoimmunity in mice lacking the c-mer membrane tyrosine kinase. Journal of Experimental Medicine 2002 196 1 135 140 2-s2.0-0036645294 10.1084/jem.20012094 (Pubitemid 34747319)
94. Rothlin C. V., Ghosh S., Zuniga E. I., Oldstone M. B. A., Lemke G., TAM receptors are pleiotropic inhibitors of the innate immune response. Cell 2007 131 6 1124 1136 2-s2.0-36849033963 10.1016/j.cell.2007.10.034 (Pubitemid 350235020)
95. Thorp E. B., Mechanisms of failed apoptotic cell clearance by phagocyte subsets in cardiovascular disease. Apoptosis 2010 15 9 1124 1136 2-s2.0-77956904529 10.1007/s10495-010-0516-6
96. O'Mullane M. J., Baker M. S., Loss of cell viability dramatically elevates cell surface plasminogen binding and activation. Experimental Cell Research 1998 242 1 153 164 2-s2.0-0031814996 10.1006/excr.1998.4067 (Pubitemid 28366531)
97. Cesarman G. M., Guevara C. A., Hajjar K. A., An endothelial cell receptor for plasminogen/tissue plasminogen activator (t-PA). II. Annexin II-mediated enhancement of t-PA-dependent plasminogen activation. Journal of Biological Chemistry 1994 269 33 21198 21203 2-s2.0-0028129557
98. Chang G. C., Liu K. J., Hsieh C. L., Hu T. S., Charoenfuprasert S., Liu H. K., Luh K. T., Hsu L. H., Wu C. W., Ting C. C., Chen C. Y., Chen K. C., Yang T. Y., Chou T. Y., Wang W. H., Whang-Peng J., Shih N. Y., Identification of α -enolase as an autoantigen in lung cancer: its overexpression is associated with clinical outcomes. Clinical Cancer Research 2006 12 19 5746 5754 2-s2.0-33750285970 10.1158/1078-0432.CCR-06-0324 (Pubitemid 44629605)
99. López-Pedrera C., Villalba J. M., Siendones E., Barbarroja N., Gómez-Díaz C., Rodríguez-Ariza A., Buendía P., Torres A., Velasco F., Proteomic analysis of acute myeloid leukemia: identification of potential early biomarkers and therapeutic targets. Proteomics 2006 6 supplement 1 S293 S299 2-s2.0-33746150544
100. Katayama M., Nakano H., Ishiuchi A., Wu W., Oshima R., Sakurai J., Nishikawa H., Yamaguchi S., Otsubo T., Protein pattern difference in the colon cancer cell lines examined by two-dimensional differential in-gel electrophoresis and mass spectrometry. Surgery Today 2006 36 12 1085 1093 2-s2.0-33751402104 10.1007/s00595-006-3301-y (Pubitemid 44819452)
101. Capello M., Ferri-Borgogno S., Cappello P., Novelli F., α -enolase: a promising therapeutic and diagnostic tumor target. FEBS Journal 2011 278 7 1064 1074 2-s2.0-79952830765 10.1111/j.1742-4658.2011.08025.x
102. Jiang W., Li X., Rao S., Wang L., Du L., Li C., Wu C., Wang H., Wang Y., Yang B., Constructing disease-specific gene networks using pair-wise relevance metric: application to colon cancer identifies interleukin 8, desmin and enolase 1 as the central elements. BMC Systems Biology 2008 2, article 72 2-s2.0-52249100151 10.1186/1752-0509-2-72
103. Georges E., Bonneau A. M., Prinos P., RNAi-mediated knockdown of alpha-enolase increases the sensitivity of tumor cells to antitubulin chemotherapeutics. International Journal of Biochemistry and Molecular Biology 2011 2 303 308
104. Trojanowicz B., Winkler A., Hammje K., Chen Z., Sekulla C., Glanz D., Schmutzler C., Mentrup B., Hombach-Klonisch S., Klonisch T., Finke R., Köhrle J., Dralle H., Hoang-Vu C., Retinoic acid-mediated down-regulation of ENO1/MBP-1 gene products caused decreased invasiveness of the follicular thyroid carcinoma cell lines. Journal of Molecular Endocrinology 2009 42 3 249 260 2-s2.0-64549112704 10.1677/JME-08-0118
105. Tsai S. T., Chien I. H., Shen W. H., Kuo Y. Z., Jin Y. T., Wong T. Y., Hsiao J. R., Wang H. P., Shih N. Y., Wu L. W., ENO1, a potential prognostic head and neck cancer marker, promotes transformation partly via chemokine CCL20 induction. European Journal of Cancer 2010 46 9 1712 1723 2-s2.0-77952584341 10.1016/j.ejca.2010.03.018
106. Jin S., DiPaola R. S., Mathew R., White E., Metabolic catastrophe as a means to cancer cell death. Journal of Cell Science 2007 120 3 379 383 2-s2.0-33847400593 10.1242/jcs.03349 (Pubitemid 46332501)
107. Abiko Y., Nishimura M., Kusano K., Nakashima K., Okumura K., Arakawa T., Takuma T., Mizoguchi I., Kaku T., Expression of MIP-3 α /CCL20, a macrophage inflammatory protein in oral squamous cell carcinoma. Archives of Oral Biology 2003 48 2 171 175 2-s2.0-0037309763 10.1016/S0003-9969(02)00167-X (Pubitemid 36453669)
108. Zhou W., Capello M., Fredolini C., Piemonti L., Liotta L. A., Novelli F., Petricoin E. F., Mass spectrometry analysis of the post-translational modifications of r-enolase from pancreatic ductal adenocarcinoma cells. Journal of Proteome Research 2010 9 6 2929 2936 2-s2.0-77954565511 10.1021/pr901109w
109. Tomaino B., Cappello P., Capello M., Fredolini C., Sperduti I., Migliorini P., Salacone P., Novarino A., Giacobino A., Ciuffreda L., Alessio M., Nisticò P., Scarpa A., Pederzoli P., Zhou W., Petricoin E. F., Liotta L. A., Giovarelli M., Milella M., Novelli F., Circulating autoantibodies to phosphorylated α -enolase are a hallmark of pancreatic cancer. Journal of Proteome Research 2011 10 1 105 112 2-s2.0-79951526292 10.1021/pr100213b
110. Iwabata H., Yoshida M., Komatsu Y., Proteomic analysis of organ-specific post-translational lysine-acetylation and -methylation in mice by use of anti-acetyllysine and -methyllysine mouse monoclonal antibodies. Proteomics 2005 5 18 4653 4664 2-s2.0-29544438797 10.1002/pmic.200500042 (Pubitemid 43016886)
111. Lu N., Zhang Y., Li H., Gao Z., Oxidative and nitrative modifications of α -enolase in cardiac proteins from diabetic rats. Free Radical Biology and Medicine 2010 48 7 873 881 2-s2.0-77249139132 10.1016/j.freeradbiomed.2010. 01.010
112. Gannon J., Staunton L., O'Connell K., Doran P., Ohlendieck K., Phosphoproteomic analysis of aged skeletal muscle. International Journal of Molecular Medicine 2008 22 1 33 42 2-s2.0-51249091494
113. Baraibar M. A., Hyzewicz J., Rogowska-Wrzesinska A., Oxidative stress-induced proteome alterations target different cellular pathways in human myoblasts. Free Radical Biology and Medicine 2011 51 1522 1532
114. Kinloch A., Tatzer V., Wait R., Peston D., Lundberg K., Donatien P., Moyes D., Taylor P. C., Venables P. J., Identification of citrullinated alpha-enolase as a candidate autoantigen in rheumatoid arthritis. Arthritis Research & Therapy 2005 7 6 R1421 1429 2-s2.0-33644667809
115. Pratesi F., Moscato S., Sabbatini A., Chimenti D., Bombardieri S., Migliorini P., Autoantibodies specific for α -enolase in systemic autoimmune disorders. Journal of Rheumatology 2000 27 1 109 115 2-s2.0-0033977341 (Pubitemid 30058637)
116. Wakui K., Tanemura M., Suzumori K., Hidaka E., Ishikawa M., Kubota T., Fukushima Y., Clinical applications of two-color telomeric fluorescence in situ hybridization for prenatal diagnosis: identification of chromosomal translocation in five families with recurrent miscarriages or a child with multiple congenital anomalies. Journal of Human Genetics 1999 44 2 85 90 2-s2.0-0033016168 10.1007/s100380050115 (Pubitemid 29146929)
117. Saulot V., Vittecoq O., Charlionet R., Fardellone P., Lange C., Marvin L., Machour N., Le Loët X., Gilbert D., Tron F., Presence of autoantibodies to the glycolytic enzyme α -enolase in sera from patients with early rheumatoid arthritis. Arthritis and Rheumatism 2002 46 5 1196 1201 2-s2.0-0036095626 10.1002/art.10252 (Pubitemid 34525825)
118. Wegner N., Lundberg K., Kinloch A., Fisher B., Malmström V., Feldmann M., Venables P. J., Autoimmunity to specific citrullinated proteins gives the first clues to the etiology of rheumatoid arthritis. Immunological Reviews 2010 233 1 34 54 2-s2.0-73249145617 10.1111/j.0105-2896.2009.00850.x
119. Chang X., Wei C., Glycolysis and rheumatoid arthritis. International Journal of Rheumatic Diseases 2011 14 3 217 222 2-s2.0-79961132978 10.1111/j.1756-185X.2011.01598.x
120. Jacovina A. T., Zhong F., Khazanova E., Lev E., Deora A. B., Hajjar K. A., Neuritogenesis and the nerve growth factor-induced differentiation of PC-12 cells requires annexin II-mediated plasmin generation. Journal of Biological Chemistry 2001 276 52 49350 49358 2-s2.0-0035966011 10.1074/jbc.M106289200
121. Obermajer N., Doljak B., Jamnik P., Fonović U. P., Kos J., Cathepsin X cleaves the C-terminal dipeptide of alpha- and gamma-enolase and impairs survival and neuritogenesis of neuronal cells. International Journal of Biochemistry and Cell Biology 2009 41 8-9 1685 1696 2-s2.0-67349238285 10.1016/j.biocel.2009.02.019
122. Butterfield D. A., Lange M. L. B., Multifunctional roles of enolase in Alzheimer's disease brain: beyond altered glucose metabolism. Journal of
123. Castegna A., Aksenov M., Thongboonkerd V., Klein J. B., Pierce W. M., Booze R., Markesbery W. R., Butterfield D. A., Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part II: dihydropyrimidinase-related protein 2, α -enolase and heat shock cognate 71. Journal of Neurochemistry 2002 82 6 1524 1532 2-s2.0-0036733145 10.1046/j.1471-4159.2002.01103.x
124. Owen J. B., Domenico F. D., Suitana R., Perluigi M., Cini C., Pierce W. M., Butterfield D. A., Proteomics-determined differences in the concanavalin-A-fractionated proteome of hippocampus and inferior parietal lobule in subjects with alzheimer's disease and mild cognitive impairment: implications for progression of AD. Journal of Proteome Research 2009 8 2 471 482 2-s2.0-61849168093 10.1021/pr800667a
125. Newman S. F., Sultana R., Perluigi M., Coccia R., Cai J., Pierce W. M., Klein J. B., Turner D. M., Butterfield D. A., An increase in S-glutathionylated proteins in the Alzheimer's disease inferior parietal lobule, a proteomics approach. Journal of Neuroscience Research 2007 85 7 1506 1514 2-s2.0-34248223082 10.1002/jnr.21275 (Pubitemid 46724394)
126. Zhang Y., Zhou Z. H., Bugge T. H., Wahl L. M., Urokinase-type plasminogen activator stimulation of monocyte matrix metalloproteinase-1 production is mediated by plasmin-dependent signaling through annexin A2 and inhibited by inactive plasmin. Journal of Immunology 2007 179 5 3297 3304 2-s2.0-38449100242
127. Syrovets T., Jendrach M., Rohwedder A., Schüle A., Simmet T., Plasmin-induced expression of cytokines and tissue factor in human monocytes involves AP-1 and IKK β -mediated NF- κ B activation. Blood 2001 97 12 3941 3950 2-s2.0-0035877968 10.1182/blood.V97.12.3941
128. Burysek L., Syrovets T., Simmet T., The serine protease plasmin triggers expression of MCP-1 and CD40 in human primary monocytes via activation of p38 MAPK and Janus kinase (JAK)/STAT signaling pathways. Journal of Biological Chemistry 2002 277 36 33509 33517 2-s2.0-0037031851 10.1074/jbc.M201941200 (Pubitemid 34987557)
129. Li Q., Laumonnier Y., Syrovets T., Simmet T., Plasmin triggers cytokine induction in human monocyte-derived macrophages. Arteriosclerosis, Thrombosis, and Vascular Biology 2007 27 6 1383 1389 2-s2.0-34249335018 10.1161/ATVBAHA.107. 142901 (Pubitemid 46809429)
130. Pendurthi U. R., Ngyuen M., Andrade-Gordon P., Petersen L. C., Rao L. V. M., Plasmin induces Cyr61 gene expression in fibroblasts via protease-activated receptor-1 and p44/42 mitogen-activated protein kinase-dependent signaling pathway. Arteriosclerosis, Thrombosis, and Vascular Biology 2002 22 9 1421 1426 2-s2.0-0036739950 10.1161/01.ATV.0000030200.59331.3F
131. Mandal S. K., Rao L. V. M., Tran T. T. T., Pendurthi U. R., A novel mechanism of plasmin-induced mitogenesis in fibroblasts. Journal of Thrombosis and Haemostasis 2005 3 1 163 169 2-s2.0-20444497340 10.1111/j.1538-7836.2004. 01054.x (Pubitemid 41647129)
132. Sousa L. P., Silva B. M., Brasil B. S. A. F., Nogueira S. V., Ferreira P. C. P., Kroon E. G., Kato K., Bonjardim C. A., Plasminogen/plasmin regulates α -enolase expression through the MEK/ERK pathway. Biochemical and Biophysical Research Communications 2005 337 4 1065 1071 2-s2.0-27144518785 10.1016/j.bbrc.2005.09.154 (Pubitemid 41505234)
133. De Sousa L. P., Brasil B. S. A. F., Silva B. M., Freitas M. H. A., Nogueira S. V., Ferreira P. C. P., Kroon E. G., Bonjardim C. A., Plasminogen/plasmin regulates c-fos and egr-1 expression via the MEK/ERK pathway. Biochemical and Biophysical Research Communications 2005 329 1 237 245 2-s2.0-13844272549 10.1016/j.bbrc.2005.01.123 (Pubitemid 40255446)
134. Majumdar M., Tarui T., Shi B., Akakura N., Ruf W., Takada Y., Plasmin-induced migration requires signaling through protease-activated receptor 1 and integrin α 9 β 1. Journal of Biological Chemistry 2004 279 36 37528 37534 2-s2.0-4444229880 10.1074/jbc.M401372200 (Pubitemid 39195465)
135. Tarui T., Majumdar M., Miles L. A., Ruf W., Takada Y., Plasmin-induced migration of endothelial cells: a potential target for the anti-angiogenic action of angiostatin. Journal of Biological Chemistry 2002 277 37 33564 33570 2-s2.0-0037072784 10.1074/jbc.M205514200
136. Roztocil E., Nicholl S. M., Galaria I. I., Davies M. G., Plasmin-induced smooth muscle cell proliferation requires epidermal growth factor activation through an extracellular pathway. Surgery 2005 138 2 180 186 2-s2.0-24344484078 10.1016/j.surg.2005.06.014 (Pubitemid 41253799)
137. Petrak J., Ivanek R., Toman O., Cmejla R., Cmejlova J., Vyoral D., Zivny J., Vulpe C. D., Déjà vu in proteomics. A hit parade of repeatedly identified differentially expressed proteins. Proteomics 2008 8 9 1744 1749 2-s2.0-43549094212 10.1002/pmic.200700919 (Pubitemid 351678270)
138. Roozendaal C., Zhao M. H., Horst G., Lockwood C. M., Kleibeuker J. H., Limburg P. C., Nelis G. F., Kallenberg C. G. M., Catalase and α -enolase: two novel granulocyte autoantigens in inflammatory bowel disease (IBD). Clinical and Experimental Immunology 1998 112 1 10 16 2-s2.0-0031972187 10.1046/j.1365-2249.1998.00528.x (Pubitemid 28157092)
139. Vermeulen N., Arijs I., Joossens S., Vermeire S., Clerens S., Van Den Bergh K., Michiels G., Arckens L., Schuit F., Van Lommel L., Rutgeerts P., Bossuyt X., Anti- α -enolase antibodies in patients with inflammatory bowel disease. Clinical Chemistry 2008 54 3 534 541 2-s2.0-40449087635 10.1373/clinchem.2007.098368 (Pubitemid 351348163)
140. Ballot E., Bruneel A., Labas V., Johanet C., Identification of rat targets of anti-soluble liver antigen autoantibodies by serologic proteome analysis. Clinical Chemistry 2003 49 4 634 643 2-s2.0-0037381176 10.1373/49.4.634 (Pubitemid 36379529)
141. Bruschi M., Carnevali M. L., Murtas C., Candiano G., Petretto A., Prunotto M., Gatti R., Argentiero L., Magistroni R., Garibotto G., Scolari F., Ravani P., Gesualdo L., Allegri L., Ghiggeri G. M., Direct characterization of target podocyte antigens and auto-antibodies in human membranous glomerulonephritis: alfa-enolase and borderline antigens. Journal of Proteomics 2011 74 10 2008 2017 2-s2.0-79958283238 10.1016/j.jprot.2011.05.021
142. Kim J. W., Dang C. V., Multifaceted roles of glycolytic enzymes. Trends in Biochemical Sciences 2005 30 3 142 150 2-s2.0-14744284637 10.1016/j.tibs.2005.01.005 (Pubitemid 40332530)