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Volumn 12, Issue 8, 2012, Pages 1050-1067

In Vitro regulatory effect of epididymal serpin CRES on protease activity of proprotein convertase PC4/PCSK4

Author keywords

Cystatin related epididymal spermatogenic; Epididymal fluid; Inhibitor; Proprotein convertase 4; Proprotein convertase subtilisin kexin 4; Proprotein processing; Protein aggregation; Serpin

Indexed keywords

CYSTATIN RELATED EPIDIDYMAL SPERMATOGENIC RECOMBINANT PROTEIN; DIMER; KEXIN; MONOMER; PROPROTEIN CONVERTASE 4; RECOMBINANT PROTEIN; SERINE PROTEINASE; SERINE PROTEINASE INHIBITOR; SUBTILISIN; UNCLASSIFIED DRUG;

EID: 84866531888     PISSN: 15665240     EISSN: 18755666     Source Type: Journal    
DOI: 10.2174/156652412802480961     Document Type: Article
Times cited : (5)

References (161)
  • 1
    • 33750946999 scopus 로고    scopus 로고
    • Narrative review: Protein degradation and human diseases: The ubiquitin connection
    • Reinstein E, Ciechanover A. Narrative review: protein degradation and human diseases: the ubiquitin connection. Ann Intern Med 2006; 145(9): 676-84.
    • (2006) Ann Intern Med , vol.145 , Issue.9 , pp. 676-684
    • Reinstein, E.1    Ciechanover, A.2
  • 2
    • 34249336767 scopus 로고    scopus 로고
    • Changing venues for tumour suppression: Balancing destruction and localization by monoubiquitylation
    • Salmena L, Pandolfi PP. Changing venues for tumour suppression: balancing destruction and localization by monoubiquitylation. Nat Rev Cancer 2007; 7(6): 409-13.
    • (2007) Nat Rev Cancer , vol.7 , Issue.6 , pp. 409-413
    • Salmena, L.1    Pandolfi, P.P.2
  • 3
    • 19344362846 scopus 로고    scopus 로고
    • The proteasome and the delicate balance between destruction and rescue
    • Glickman MH, Adir N. The proteasome and the delicate balance between destruction and rescue. PLoS Biol 2004; 2: E13.
    • (2004) PLoS Biol , vol.2
    • Glickman, M.H.1    Adir, N.2
  • 4
    • 67449086054 scopus 로고    scopus 로고
    • Alveolar extracellular 20S proteasome in patients with acute respiratory distress syndrome
    • Sixt SU, Adamzik M, Spyrka D, et al. Alveolar extracellular 20S proteasome in patients with acute respiratory distress syndrome. Am J Respir Crit Care Med 2009; 179: 1098-1106.
    • (2009) Am J Respir Crit Care Med , vol.179 , pp. 1098-1106
    • Sixt, S.U.1    Adamzik, M.2    Spyrka, D.3
  • 5
    • 0034864799 scopus 로고    scopus 로고
    • Proteasome inhibitors: From research tools to drug candidates
    • Kisselev AF, Goldberg A. Proteasome inhibitors: from research tools to drug candidates. Chem Biol 2001; 8: 739-58.
    • (2001) Chem Biol , vol.8 , pp. 739-758
    • Kisselev, A.F.1    Goldberg, A.2
  • 6
    • 77449103325 scopus 로고    scopus 로고
    • Therapeutic strategies within the ubiquitin proteasome system
    • Eldridge AG, O'Brien T. Therapeutic strategies within the ubiquitin proteasome system. Cell Death Differ 2010; 17: 4-13.
    • (2010) Cell Death Differ , vol.17 , pp. 4-13
    • Eldridge, A.G.1    O'Brien, T.2
  • 7
    • 0037973279 scopus 로고    scopus 로고
    • A phase 2 study of bortezomib in relapsed, refractory myeloma
    • Richardson PG, Barlogie B, Berenson J, et al. A phase 2 study of bortezomib in relapsed, refractory myeloma. N Engl J Med 2003; 348: 2609-17.
    • (2003) N Engl J Med , vol.348 , pp. 2609-2617
    • Richardson, P.G.1    Barlogie, B.2    Berenson, J.3
  • 9
    • 0035929585 scopus 로고    scopus 로고
    • The human estrogen receptor-alpha is a ubiquitinated protein whose stability is affected differentially by agonists, antagonists, and selective estrogen receptor modulators
    • Wijayaratne AL, McDonnell DP. The human estrogen receptor-alpha is a ubiquitinated protein whose stability is affected differentially by agonists, antagonists, and selective estrogen receptor modulators. J Biol Chem 2001; 276(38): 35684-92.
    • (2001) J Biol Chem , vol.276 , Issue.38 , pp. 35684-35692
    • Wijayaratne, A.L.1    McDonnell, D.P.2
  • 10
    • 0142056952 scopus 로고    scopus 로고
    • Various phosphorylation pathways, depending on agonist and antagonist binding to endogenous estrogen receptor alpha (ERalpha), differentially affect ERalpha extractability, proteasome-mediated stability, and transcriptional activity in human breast cancer cells
    • Marsaud V, Gougelet A, Maillard S, Renoir JM. Various phosphorylation pathways, depending on agonist and antagonist binding to endogenous estrogen receptor alpha (ERalpha), differentially affect ERalpha extractability, proteasome-mediated stability, and transcriptional activity in human breast cancer cells. Mol Endocrinol 2003; 17(10): 2013-27.
    • (2003) Mol Endocrinol , vol.17 , Issue.10 , pp. 2013-2027
    • Marsaud, V.1    Gougelet, A.2    Maillard, S.3    Renoir, J.M.4
  • 11
    • 0037351881 scopus 로고    scopus 로고
    • Cyclic, proteasomemediated turnover of unliganded and liganded ERalpha on responsive promoters is an integral feature of estrogen signaling
    • Reid G, Hubner MR, Metivier R, et al. Cyclic, proteasomemediated turnover of unliganded and liganded ERalpha on responsive promoters is an integral feature of estrogen signaling. Mol Cell 2003; 11(3): 695-707.
    • (2003) Mol Cell , vol.11 , Issue.3 , pp. 695-707
    • Reid, G.1    Hubner, M.R.2    Metivier, R.3
  • 12
    • 54249154593 scopus 로고    scopus 로고
    • The UPS: A promising target for breast cancer treatment
    • doi: 10.1186/1471-2091-9-S1-S2
    • Sato K, Rajendra E, Ohta T. The UPS: a promising target for breast cancer treatment. BMC Biochemistry 2008; 9 (Suppl 1), S2: doi: 10.1186/1471-2091-9-S1-S2.
    • (2008) BMC Biochemistry , vol.9 , Issue.SUPPL. 1
    • Sato, K.1    Rajendra, E.2    Ohta, T.3
  • 13
    • 33748075461 scopus 로고    scopus 로고
    • Proteasome Inhibitor Drugs on the Rise
    • Joazeiro CAP, Anderson KC, Hunter T. Proteasome Inhibitor Drugs on the Rise. Cancer Res 2006; 66(16): 7840-2.
    • (2006) Cancer Res , vol.66 , Issue.16 , pp. 7840-7842
    • Joazeiro, C.A.P.1    Anderson, K.C.2    Hunter, T.3
  • 14
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunitspecific amino-terminal threonine modification by lactacystin
    • Fenteany G, Standaert RF, Lane WS, Choi S, Corey EJ, Schreiber SL. Inhibition of proteasome activities and subunitspecific amino-terminal threonine modification by lactacystin. Science 1995; 268: 726-731.
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 15
    • 27644562277 scopus 로고    scopus 로고
    • A novel orally active proteasome inhibitor induces apoptosis in multiple myeloma cells with mechanisms distinct from bortezomib
    • Chauhan D, Catley L, Li G, et al. A novel orally active proteasome inhibitor induces apoptosis in multiple myeloma cells with mechanisms distinct from bortezomib. Cancer Cell 2005; 8: 407-19.
    • (2005) Cancer Cell , vol.8 , pp. 407-419
    • Chauhan, D.1    Catley, L.2    Li, G.3
  • 16
    • 33847410207 scopus 로고    scopus 로고
    • The proteasome inhibitors bortezomib and PR-171 have antiproliferative and proapoptotic effects on primary human acute myeloid leukaemia cells
    • Stapnes C, Doskeland AP, Hatfield K, et al. The proteasome inhibitors bortezomib and PR-171 have antiproliferative and proapoptotic effects on primary human acute myeloid leukaemia cells. Br J Haematol 2007; 136(6): 814-28.
    • (2007) Br J Haematol , vol.136 , Issue.6 , pp. 814-828
    • Stapnes, C.1    Doskeland, A.P.2    Hatfield, K.3
  • 17
    • 0031657808 scopus 로고    scopus 로고
    • Matrix proteoglycans: From molecular design to cellular function
    • Iozzo RV. Matrix proteoglycans: from molecular design to cellular function. Annu Rev Biochem 1998; 67: 609-52.
    • (1998) Annu Rev Biochem , vol.67 , pp. 609-652
    • Iozzo, R.V.1
  • 18
    • 72449147268 scopus 로고    scopus 로고
    • Proteoglycans: From structural compounds to signaling molecules
    • Schaefer L, Schaefer RM. Proteoglycans: from structural compounds to signaling molecules. Cell Tissue Res 2010; 339(1): 237-46.
    • (2010) Cell Tissue Res , vol.339 , Issue.1 , pp. 237-246
    • Schaefer, L.1    Schaefer, R.M.2
  • 19
    • 84859102378 scopus 로고    scopus 로고
    • Glycosaminoglycans: From "cellular glue" to novel therapeutical agents
    • doi:10.1016/j.coph.2011.12.003
    • Karamanos NK, Tzanakakis GN. Glycosaminoglycans: from "cellular glue" to novel therapeutical agents. Curr Opin Pharmacol 2012; doi:10.1016/j.coph.2011.12.003
    • (2012) Curr Opin Pharmacol
    • Karamanos, N.K.1    Tzanakakis, G.N.2
  • 20
    • 77956637386 scopus 로고    scopus 로고
    • Proteoglycans in health and disease: Emerging concepts and future directions
    • Iozzo RV, Karamanos N. Proteoglycans in health and disease: emerging concepts and future directions. FEBS J 2010; 277(19): 3863.
    • (2010) FEBS J , vol.277 , Issue.19 , pp. 3863
    • Iozzo, R.V.1    Karamanos, N.2
  • 21
    • 77956641177 scopus 로고    scopus 로고
    • Proteoglycans in health and disease: Novel roles for proteoglycans in malignancy and their pharmacological targeting
    • Theocharis AD, Skandalis SS, Tzanakakis GN, Karamanos NK. Proteoglycans in health and disease: novel roles for proteoglycans in malignancy and their pharmacological targeting. FEBS J 2010; 277(19): 3904-23.
    • (2010) FEBS J , vol.277 , Issue.19 , pp. 3904-3923
    • Theocharis, A.D.1    Skandalis, S.S.2    Tzanakakis, G.N.3    Karamanos, N.K.4
  • 22
    • 78650484050 scopus 로고    scopus 로고
    • Metalloproteinases in health and disease: Challenges and the future prospects
    • Nagase H, Karamanos N. Metalloproteinases in health and disease: challenges and the future prospects. FEBS J 2011; 278(1): 1.
    • (2011) FEBS J , vol.278 , Issue.1 , pp. 1
    • Nagase, H.1    Karamanos, N.2
  • 23
    • 78650440475 scopus 로고    scopus 로고
    • Localizing matrix metalloproteinase activities in the pericellular environment
    • Murphy G, Nagase H. Localizing matrix metalloproteinase activities in the pericellular environment. FEBS J 2011; 278(1): 2-15.
    • (2011) FEBS J , vol.278 , Issue.1 , pp. 2-15
    • Murphy, G.1    Nagase, H.2
  • 24
    • 0026676859 scopus 로고
    • Natural inhibitor of transforming growth factor-beta protects against scarring in experimental kidney disease
    • Border WA, Noble NA, Yamamoto T, et al. Natural inhibitor of transforming growth factor-beta protects against scarring in experimental kidney disease. Nature 1992; 360: 361-4.
    • (1992) Nature , vol.360 , pp. 361-364
    • Border, W.A.1    Noble, N.A.2    Yamamoto, T.3
  • 25
    • 56949083199 scopus 로고    scopus 로고
    • Novel regulatory mechanisms for the proteoglycans decorin and biglycan during muscle formation and muscular dystrophy
    • Brandan E, Cabello-Verrugio C, Vial C. Novel regulatory mechanisms for the proteoglycans decorin and biglycan during muscle formation and muscular dystrophy. Matrix Biol 2008; 27: 700-8.
    • (2008) Matrix Biol , vol.27 , pp. 700-708
    • Brandan, E.1    Cabello-Verrugio, C.2    Vial, C.3
  • 26
    • 79960119978 scopus 로고    scopus 로고
    • Small leucine-rich proteoglycans in kidney disease
    • Schaefer L. Small leucine-rich proteoglycans in kidney disease. J Am Soc Nephrol 2011; 22: 1200-7.
    • (2011) J Am Soc Nephrol , vol.22 , pp. 1200-1207
    • Schaefer, L.1
  • 27
    • 0036118493 scopus 로고    scopus 로고
    • Absence of decorin adversely influences tubulointerstitial fibrosis of the obstructed kidney by enhanced apoptosis and increased inflammatory reaction
    • Schaefer L, Macakova K, Raslik I, et al. Absence of decorin adversely influences tubulointerstitial fibrosis of the obstructed kidney by enhanced apoptosis and increased inflammatory reaction. Am J Pathol 2002; 160: 1181-91.
    • (2002) Am J Pathol , vol.160 , pp. 1181-1191
    • Schaefer, L.1    McAkova, K.2    Raslik, I.3
  • 28
    • 0025353729 scopus 로고
    • Negative regulation of transforming growth factor-beta by the proteoglycan decorin
    • Yamaguchi Y, Mann DM, Ruoslahti E. Negative regulation of transforming growth factor-beta by the proteoglycan decorin. Nature 1990; 346: 281-4.
    • (1990) Nature , vol.346 , pp. 281-284
    • Yamaguchi, Y.1    Mann, D.M.2    Ruoslahti, E.3
  • 29
    • 0037145715 scopus 로고    scopus 로고
    • Human colon adenocarcinoma is associated with specific post-translational modifications of versican and decorin
    • Theocharis AD. Human colon adenocarcinoma is associated with specific post-translational modifications of versican and decorin. Biochim Biophys Acta 2002; 1588: 165-72.
    • (2002) Biochim Biophys Acta , vol.1588 , pp. 165-172
    • Theocharis, A.D.1
  • 30
    • 0036278883 scopus 로고    scopus 로고
    • The expression of decorin in human ovarian tumors
    • Nash MA, Deavers MT, Freedman RS. The expression of decorin in human ovarian tumors. Clin Cancer Res 2002; 8: 1754-60.
    • (2002) Clin Cancer Res , vol.8 , pp. 1754-1760
    • Nash, M.A.1    Deavers, M.T.2    Freedman, R.S.3
  • 31
    • 0037343750 scopus 로고    scopus 로고
    • The gastric carcinoma glycosaminoglycans and proteoglycans undergo marked alterations in their content, composition and chemical structure
    • Theocharis AD, Vynios DH, Papageorgakopoulou N, Skandalis SS, Theocharis DA. The gastric carcinoma glycosaminoglycans and proteoglycans undergo marked alterations in their content, composition and chemical structure. Int J Biochem Cell Biol 2003; 35: 376-90.
    • (2003) Int J Biochem Cell Biol , vol.35 , pp. 376-390
    • Theocharis, A.D.1    Vynios, D.H.2    Papageorgakopoulou, N.3    Skandalis, S.S.4    Theocharis, D.A.5
  • 32
    • 33745454902 scopus 로고    scopus 로고
    • The greatly increased amounts of accumulated versican and decorin with specific posttranslational modifications may be closely associated with the malignant phenotype of pancreatic cancer
    • Skandalis SS, Kletsas D, Kyriakopoulou D, Stavropoulos M, Theocharis DA. The greatly increased amounts of accumulated versican and decorin with specific posttranslational modifications may be closely associated with the malignant phenotype of pancreatic cancer. Biochim Biophys Acta 2006; 1760: 1217-25.
    • (2006) Biochim Biophys Acta , vol.1760 , pp. 1217-1225
    • Skandalis, S.S.1    Kletsas, D.2    Kyriakopoulou, D.3    Stavropoulos, M.4    Theocharis, D.A.5
  • 33
    • 48549098505 scopus 로고    scopus 로고
    • Decorin-induced growth inhibition is overcome through protracted expression and activation of epidermal growth factor receptors in osteosarcoma cells
    • Zafiropoulos A, Nikitovic D, Katonis P, Tsatsakis A, Karamanos NK, Tzanakakis GN. Decorin-induced growth inhibition is overcome through protracted expression and activation of epidermal growth factor receptors in osteosarcoma cells. Mol Cancer Res 2008; 6(5): 785-94.
    • (2008) Mol Cancer Res , vol.6 , Issue.5 , pp. 785-794
    • Zafiropoulos, A.1    Nikitovic, D.2    Katonis, P.3    Tsatsakis, A.4    Karamanos, N.K.5    Tzanakakis, G.N.6
  • 34
    • 0033046972 scopus 로고    scopus 로고
    • Cooperative action of germline mutations in decorin and p53 accelerates lymphoma tumorigenesis
    • Iozzo RV, Chakrani F, Perrotti D, et al. Cooperative action of germline mutations in decorin and p53 accelerates lymphoma tumorigenesis. Proc Natl Acad Sci USA 1999; 96: 3092-7.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3092-3097
    • Iozzo, R.V.1    Chakrani, F.2    Perrotti, D.3
  • 35
    • 77956621814 scopus 로고    scopus 로고
    • Proteoglycans in health and disease: Novel regulatory signaling mechanisms evoked by the small leucine-rich proteoglycans
    • Iozzo RV, Schaefer L. Proteoglycans in health and disease: novel regulatory signaling mechanisms evoked by the small leucine-rich proteoglycans. FEBS J 2010; 277(19): 3864-75.
    • (2010) FEBS J , vol.277 , Issue.19 , pp. 3864-3875
    • Iozzo, R.V.1    Schaefer, L.2
  • 36
    • 57349175862 scopus 로고    scopus 로고
    • Tumor microenvironment: Modulation by decorin and related molecules harboring leucine-rich tandem motifs
    • Goldoni S, Iozzo RV. Tumor microenvironment: Modulation by decorin and related molecules harboring leucine-rich tandem motifs. Int J Cancer 2008; 123: 2473-9.
    • (2008) Int J Cancer , vol.123 , pp. 2473-2479
    • Goldoni, S.1    Iozzo, R.V.2
  • 37
    • 79957605232 scopus 로고    scopus 로고
    • Proteoglycans in cancer biology, tumour microenvironment and angiogenesis
    • Iozzo RV, Sanderson RD. Proteoglycans in cancer biology, tumour microenvironment and angiogenesis. J Cell Mol Med 2011; 15: 1013-31.
    • (2011) J Cell Mol Med , vol.15 , pp. 1013-1031
    • Iozzo, R.V.1    Sanderson, R.D.2
  • 38
    • 0034693263 scopus 로고    scopus 로고
    • Sustained downregulation of the epidermal growth factor receptor by decorin. A mechanism for controlling tumor growth in vivo
    • Csordas G, Santra M, Reed CC, et al. Sustained downregulation of the epidermal growth factor receptor by decorin. A mechanism for controlling tumor growth in vivo. J Biol Chem 2000; 275: 32879-87.
    • (2000) J Biol Chem , vol.275 , pp. 32879-32887
    • Csordas, G.1    Santra, M.2    Reed, C.C.3
  • 39
    • 0029785662 scopus 로고    scopus 로고
    • Decorin-induced growth suppression is associated with upregulation of p21, an inhibitor of cyclin-dependent kinases
    • De Luca A, Santra M, Baldi A, Giordano A, Iozzo RV. Decorin-induced growth suppression is associated with upregulation of p21, an inhibitor of cyclin-dependent kinases. J Biol Chem 1996; 271: 18961-5.
    • (1996) J Biol Chem , vol.271 , pp. 18961-18965
    • de Luca, A.1    Santra, M.2    Baldi, A.3    Giordano, A.4    Iozzo, R.V.5
  • 41
    • 0037144523 scopus 로고    scopus 로고
    • Decorin binds to a narrow region of the epidermal growth factor (EGF) receptor, partially overlapping but distinct from the EGF-binding epitope
    • Santra M, Reed CC, Iozzo RV. Decorin binds to a narrow region of the epidermal growth factor (EGF) receptor, partially overlapping but distinct from the EGF-binding epitope. J Biol Chem 2002; 277: 35671-81.
    • (2002) J Biol Chem , vol.277 , pp. 35671-35681
    • Santra, M.1    Reed, C.C.2    Iozzo, R.V.3
  • 42
    • 25444503249 scopus 로고    scopus 로고
    • Decorin evokes protracted internalization and degradation of the epidermal growth factor receptor via caveolar endocytosis
    • Zhu JX, Goldoni S, Bix G, et al. Decorin evokes protracted internalization and degradation of the epidermal growth factor receptor via caveolar endocytosis. J Biol Chem 2005; 280: 32468-79.
    • (2005) J Biol Chem , vol.280 , pp. 32468-32479
    • Zhu, J.X.1    Goldoni, S.2    Bix, G.3
  • 43
    • 66149095761 scopus 로고    scopus 로고
    • Decorin is a novel antagonistic ligand of the Met receptor
    • Goldoni S, Humphries A, Nystrom A, et al. Decorin is a novel antagonistic ligand of the Met receptor. J Cell Biol 2009; 185: 743-54.
    • (2009) J Cell Biol , vol.185 , pp. 743-754
    • Goldoni, S.1    Humphries, A.2    Nystrom, A.3
  • 44
    • 78650674666 scopus 로고    scopus 로고
    • Decorin antagonizes Met receptor activity and down-regulates {beta}-catenin and Myc levels
    • Buraschi S, Pal N, Tyler-Rubinstein N, Owens RT, Neill T, Iozzo RV. Decorin antagonizes Met receptor activity and down-regulates {beta}-catenin and Myc levels. J Biol Chem 2010; 285: 42075-85.
    • (2010) J Biol Chem , vol.285 , pp. 42075-42085
    • Buraschi, S.1    Pal, N.2    Tyler-Rubinstein, N.3    Owens, R.T.4    Neill, T.5    Iozzo, R.V.6
  • 45
    • 70149091269 scopus 로고    scopus 로고
    • Decorin suppresses prostate tumor growth through inhibition of epidermal growth factor and androgen receptor pathways
    • Hu Y, Sun H, Owens RT, et al. Decorin suppresses prostate tumor growth through inhibition of epidermal growth factor and androgen receptor pathways. Neoplasia 2009; 11: 1042-53.
    • (2009) Neoplasia , vol.11 , pp. 1042-1053
    • Hu, Y.1    Sun, H.2    Owens, R.T.3
  • 46
    • 13944249920 scopus 로고    scopus 로고
    • Decorin prevents metastatic spreading of breast cancer
    • Reed CC, Waterhouse A, Kirby S, et al. Decorin prevents metastatic spreading of breast cancer. Oncogene 2005; 24: 1104-10.
    • (2005) Oncogene , vol.24 , pp. 1104-1110
    • Reed, C.C.1    Waterhouse, A.2    Kirby, S.3
  • 47
    • 33748755116 scopus 로고    scopus 로고
    • Decorin protein core inhibits in vivo cancer growth and metabolism by hindering epidermal growth factor receptor function and triggering apoptosis via caspase-3 activation
    • Seidler DG, Goldoni S, Agnew C, et al. Decorin protein core inhibits in vivo cancer growth and metabolism by hindering epidermal growth factor receptor function and triggering apoptosis via caspase-3 activation. J Biol Chem 2006; 281: 26408-18.
    • (2006) J Biol Chem , vol.281 , pp. 26408-26418
    • Seidler, D.G.1    Goldoni, S.2    Agnew, C.3
  • 48
    • 0037364506 scopus 로고    scopus 로고
    • In vivo selective and distant killing of cancer cells using adenovirus-mediated decorin gene transfer
    • Tralhao JG, Schaefer L, Micegova M, et al. In vivo selective and distant killing of cancer cells using adenovirus-mediated decorin gene transfer. FASEB J 2003; 17: 464-6.
    • (2003) FASEB J , vol.17 , pp. 464-466
    • Tralhao, J.G.1    Schaefer, L.2    Micegova, M.3
  • 49
    • 79955054709 scopus 로고    scopus 로고
    • Regulatory roles of hyaluronan in health and disease
    • Hascall V, Karamanos N. Regulatory roles of hyaluronan in health and disease. FEBS J 2011; 278(9): 1411.
    • (2011) FEBS J , vol.278 , Issue.9 , pp. 1411
    • Hascall, V.1    Karamanos, N.2
  • 50
    • 44749083057 scopus 로고    scopus 로고
    • Hyaluronan in human tumors: Pathobiological and prognostic messages from cell-associated and stromal hyaluronan
    • Tammi RH, Kultti A, Kosma VM, Pirinen R, Auvinen P, Tammi MI. Hyaluronan in human tumors: pathobiological and prognostic messages from cell-associated and stromal hyaluronan. Semin Cancer Biol 2008; 18: 288-295.
    • (2008) Semin Cancer Biol , vol.18 , pp. 288-295
    • Tammi, R.H.1    Kultti, A.2    Kosma, V.M.3    Pirinen, R.4    Auvinen, P.5    Tammi, M.I.6
  • 51
    • 50149105712 scopus 로고    scopus 로고
    • Impact of the hyaluronan-rich tumor microenvironment on cancer initiation and progression
    • Itano N, Zhuo L, Kimata K. Impact of the hyaluronan-rich tumor microenvironment on cancer initiation and progression. Cancer Sci 2008; 99: 1720-25.
    • (2008) Cancer Sci , vol.99 , pp. 1720-1725
    • Itano, N.1    Zhuo, L.2    Kimata, K.3
  • 53
    • 79955063673 scopus 로고    scopus 로고
    • Hyaluronan-CD44 interactions as potential targets for cancer therapy
    • Misra S, Heldin P, Hascall VC, et al. Hyaluronan-CD44 interactions as potential targets for cancer therapy. FEBS J 2011; 278(9): 1429-43.
    • (2011) FEBS J , vol.278 , Issue.9 , pp. 1429-1443
    • Misra, S.1    Heldin, P.2    Hascall, V.C.3
  • 54
    • 0033889231 scopus 로고    scopus 로고
    • Hyaluronan in peritumoral stroma and malignant cells associates with breast cancer spreading and predicts survival
    • Auvinen P, Tammi R, Parkkinen J, et al. Hyaluronan in peritumoral stroma and malignant cells associates with breast cancer spreading and predicts survival. Am J Pathol 2000; 156: 529-36.
    • (2000) Am J Pathol , vol.156 , pp. 529-536
    • Auvinen, P.1    Tammi, R.2    Parkkinen, J.3
  • 55
    • 0031973883 scopus 로고    scopus 로고
    • Tumor cellassociated hyaluronan as an unfavorable prognostic factor in colorectal cancer
    • Ropponen K, Tammi M, Parkkinen J, et al. Tumor cellassociated hyaluronan as an unfavorable prognostic factor in colorectal cancer. Cancer Res 1998; 58: 342-7.
    • (1998) Cancer Res , vol.58 , pp. 342-347
    • Ropponen, K.1    Tammi, M.2    Parkkinen, J.3
  • 56
    • 0035783042 scopus 로고    scopus 로고
    • Hyaluronan in morphogenesis
    • Toole BP. Hyaluronan in morphogenesis. Semin Cell Dev Biol 2001; 12: 79-87.
    • (2001) Semin Cell Dev Biol , vol.12 , pp. 79-87
    • Toole, B.P.1
  • 57
    • 0027731762 scopus 로고
    • Localization of hyaluronan in normal breast tissue, radial scar, and tubular breast carcinoma
    • de la Torre M, Wells AF, Bergh J, Lindgren A. Localization of hyaluronan in normal breast tissue, radial scar, and tubular breast carcinoma. Hum Pathol 1993; 24: 1294-7.
    • (1993) Hum Pathol , vol.24 , pp. 1294-1297
    • de la Torre, M.1    Wells, A.F.2    Bergh, J.3    Lindgren, A.4
  • 58
    • 30844447925 scopus 로고    scopus 로고
    • Expression of hyaluronan in human tumor progression
    • Boregowda RK, Appaiah HN, Siddaiah M, et al. Expression of hyaluronan in human tumor progression. J Carcinog 2006; 5: 2.
    • (2006) J Carcinog , vol.5 , pp. 2
    • Boregowda, R.K.1    Appaiah, H.N.2    Siddaiah, M.3
  • 59
    • 0033847008 scopus 로고    scopus 로고
    • Disruption of hyaluronan synthase-2 abrogates normal cardiac morphogenesis and hyaluronan-mediated transformation of epithelium to mesenchyme
    • Camenisch TD, Spicer AP, Brehm-Gibson T, et al. Disruption of hyaluronan synthase-2 abrogates normal cardiac morphogenesis and hyaluronan-mediated transformation of epithelium to mesenchyme. J Clin Invest 2000; 106: 349-60.
    • (2000) J Clin Invest , vol.106 , pp. 349-360
    • Camenisch, T.D.1    Spicer, A.P.2    Brehm-Gibson, T.3
  • 60
    • 0035902816 scopus 로고    scopus 로고
    • Hyaluronan production increases the malignant properties of mesothelioma cells
    • Li Y, Heldin P. Hyaluronan production increases the malignant properties of mesothelioma cells. Br J Cancer 2001; 85: 600-7.
    • (2001) Br J Cancer , vol.85 , pp. 600-607
    • Li, Y.1    Heldin, P.2
  • 61
    • 0242412978 scopus 로고    scopus 로고
    • Elevated hyaluronan production induces mesenchymal and transformed properties in epithelial cells
    • Zoltan-Jones A, Huang L, Ghatak S, Toole BP. Elevated hyaluronan production induces mesenchymal and transformed properties in epithelial cells. J Biol Chem 2003; 278: 45801-10.
    • (2003) J Biol Chem , vol.278 , pp. 45801-45810
    • Zoltan-Jones, A.1    Huang, L.2    Ghatak, S.3    Toole, B.P.4
  • 62
    • 0037145745 scopus 로고    scopus 로고
    • Expression of hyaluronan synthase 2 or hyaluronidase 1 differentially affect the growth rate of transplantable colon carcinoma cell tumors
    • Jacobson A, Rahmanian M, Rubin K, Heldin P. Expression of hyaluronan synthase 2 or hyaluronidase 1 differentially affect the growth rate of transplantable colon carcinoma cell tumors. Int J Cancer 2002; 102: 212-9.
    • (2002) Int J Cancer , vol.102 , pp. 212-219
    • Jacobson, A.1    Rahmanian, M.2    Rubin, K.3    Heldin, P.4
  • 63
    • 34247857741 scopus 로고    scopus 로고
    • Hyperproduction of hyaluronan in neu-induced mammary tumor accelerates angiogenesis through stromal cell recruitment: Possible involvement of versican/PG-M
    • Koyama H, Hibi T, Isogai Z, et al. Hyperproduction of hyaluronan in neu-induced mammary tumor accelerates angiogenesis through stromal cell recruitment: possible involvement of versican/PG-M. Am J Pathol 2007; 170: 1086-99.
    • (2007) Am J Pathol , vol.170 , pp. 1086-1099
    • Koyama, H.1    Hibi, T.2    Isogai, Z.3
  • 64
    • 38749113916 scopus 로고    scopus 로고
    • Significance of tumor-associated stroma in promotion of intratumoral lymphangiogenesis: Pivotal role of a hyaluronan-rich tumor microenvironment
    • Koyama H, Kobayashi N, Harada M, et al. Significance of tumor-associated stroma in promotion of intratumoral lymphangiogenesis: pivotal role of a hyaluronan-rich tumor microenvironment. Am J Pathol 2008; 172: 179-93.
    • (2008) Am J Pathol , vol.172 , pp. 179-193
    • Koyama, H.1    Kobayashi, N.2    Harada, M.3
  • 65
    • 22244442728 scopus 로고    scopus 로고
    • Antisensemediated suppression of hyaluronan synthase 2 inhibits the tumorigenesis and progression of breast cancer
    • Udabage L, Brownlee GR, Waltham M, et al. Antisensemediated suppression of hyaluronan synthase 2 inhibits the tumorigenesis and progression of breast cancer. Cancer Res 2005; 65: 6139-50.
    • (2005) Cancer Res , vol.65 , pp. 6139-6150
    • Udabage, L.1    Brownlee, G.R.2    Waltham, M.3
  • 66
    • 34247492506 scopus 로고    scopus 로고
    • Silencing of hyaluronan synthase 2 suppresses the malignant phenotype of invasive breast cancer cells
    • Li Y, Li L, Brown TJ, Heldin P. Silencing of hyaluronan synthase 2 suppresses the malignant phenotype of invasive breast cancer cells. Int J Cancer 2007; 120: 2557-67.
    • (2007) Int J Cancer , vol.120 , pp. 2557-2567
    • Li, Y.1    Li, L.2    Brown, T.J.3    Heldin, P.4
  • 67
    • 0032213027 scopus 로고    scopus 로고
    • The cell surface heparan sulfate proteoglycan glypican-1 regulates growth factor in pancreatic carcinoma cells and is overexpressed in human pancreatic cancer
    • Kleeff J, Ishiwata T, Kumbasar A, et al. The cell surface heparan sulfate proteoglycan glypican-1 regulates growth factor in pancreatic carcinoma cells and is overexpressed in human pancreatic cancer. J Clin Invest 1998; 102: 1662-73.
    • (1998) J Clin Invest , vol.102 , pp. 1662-1673
    • Kleeff, J.1    Ishiwata, T.2    Kumbasar, A.3
  • 68
    • 0035879011 scopus 로고    scopus 로고
    • Glypican-1 is overexpressed in human breast cancer and modulates the mitogenic effects of multiple heparin-binding growth factors in breast cancer cells
    • Matsuda K, Maruyama H, Guo F, et al. Glypican-1 is overexpressed in human breast cancer and modulates the mitogenic effects of multiple heparin-binding growth factors in breast cancer cells. Cancer Res 2001; 61(14): 5562-9.
    • (2001) Cancer Res , vol.61 , Issue.14 , pp. 5562-5569
    • Matsuda, K.1    Maruyama, H.2    Guo, F.3
  • 69
    • 38149063860 scopus 로고    scopus 로고
    • Glypican-1 modulates the angiogenic and metastatic potential of human and mouse cancer cells
    • Aikawa T, Whipple CA, Lopez ME, et al. Glypican-1 modulates the angiogenic and metastatic potential of human and mouse cancer cells. J Clin Invest 2008; 118: 89-99.
    • (2008) J Clin Invest , vol.118 , pp. 89-99
    • Aikawa, T.1    Whipple, C.A.2    Lopez, M.E.3
  • 70
    • 33744729372 scopus 로고    scopus 로고
    • Glypican-1 is frequently overexpressed in human gliomas and enhances FGF-2 signaling in glioma cells
    • Su G, Meyer K, Nandini CD, Qiao D, Salamat S, Friedl A. Glypican-1 is frequently overexpressed in human gliomas and enhances FGF-2 signaling in glioma cells. Am J Pathol 2006; 168: 2014-26.
    • (2006) Am J Pathol , vol.168 , pp. 2014-2026
    • Su, G.1    Meyer, K.2    Nandini, C.D.3    Qiao, D.4    Salamat, S.5    Friedl, A.6
  • 71
    • 13344261391 scopus 로고    scopus 로고
    • Mutations in GPC3, a glypican gene, cause the Simpson-Golabi-Behmel overgrowth syndrome
    • Pilia G, Hughes-Benzie RM, MacKenzie A, et al. Mutations in GPC3, a glypican gene, cause the Simpson-Golabi-Behmel overgrowth syndrome. Nat Genet 1996; 12(3): 241-7.
    • (1996) Nat Genet , vol.12 , Issue.3 , pp. 241-247
    • Pilia, G.1    Hughes-Benzie, R.M.2    McKenzie, A.3
  • 72
    • 0031671855 scopus 로고    scopus 로고
    • Matrix metalloproteinase degradation of extracellular matrix: Biological consequences
    • Shapiro SD. Matrix metalloproteinase degradation of extracellular matrix: biological consequences. Curr Opin Cell Biol 1998; 10: 602-8.
    • (1998) Curr Opin Cell Biol , vol.10 , pp. 602-608
    • Shapiro, S.D.1
  • 73
    • 20444465773 scopus 로고    scopus 로고
    • Elevated formation of pyridinoline cross-links by profibrotic cytokines is associated with enhanced lysyl hydroxylase 2b levels
    • van der Slot AJ, van Dura EA, de Wit EC, et al. Elevated formation of pyridinoline cross-links by profibrotic cytokines is associated with enhanced lysyl hydroxylase 2b levels. Biochim Biophys Acta 2005; 1741: 95-102.
    • (2005) Biochim Biophys Acta , vol.1741 , pp. 95-102
    • van der Slot, A.J.1    van Dura, E.A.2    de Wit, E.C.3
  • 74
    • 0141751743 scopus 로고    scopus 로고
    • The presence of a fibrotic focus in invasive breast carcinoma correlates with the expression of carbonic anhydrase IX and is a marker of hypoxia and poor prognosis
    • Colpaert CG, Vermeulen PB, Fox SB, Harris AL, Dirix LY, Van Marck EA. The presence of a fibrotic focus in invasive breast carcinoma correlates with the expression of carbonic anhydrase IX and is a marker of hypoxia and poor prognosis. Breast Cancer Res Treat 2003; 81: 137-47.
    • (2003) Breast Cancer Res Treat , vol.81 , pp. 137-147
    • Colpaert, C.G.1    Vermeulen, P.B.2    Fox, S.B.3    Harris, A.L.4    Dirix, L.Y.5    van Marck, E.A.6
  • 75
    • 41749096366 scopus 로고    scopus 로고
    • Plasma MMP1 and MMP8 expression in breast cancer: Protective role of MMP8 against lymph node metastasis
    • Decock J, Hendrickx W, Vanleeuw U, et al. Plasma MMP1 and MMP8 expression in breast cancer: protective role of MMP8 against lymph node metastasis. BMC Cancer 2008; 8: 77.
    • (2008) BMC Cancer , vol.8 , pp. 77
    • Decock, J.1    Hendrickx, W.2    Vanleeuw, U.3
  • 76
    • 33646576169 scopus 로고    scopus 로고
    • Matrix metalloproteinases and tumor metastasis
    • Deryugina EI, Quigley JP. Matrix metalloproteinases and tumor metastasis. Cancer Metastasis Rev 2006; 25(1): 9-34.
    • (2006) Cancer Metastasis Rev , vol.25 , Issue.1 , pp. 9-34
    • Deryugina, E.I.1    Quigley, J.P.2
  • 77
    • 39449134211 scopus 로고    scopus 로고
    • Collagenase-2 (matrix metalloproteinase-8) plays a protective role in tongue cancer
    • Korpi JT, Kervinen V, Mäklin H, et al. Collagenase-2 (matrix metalloproteinase-8) plays a protective role in tongue cancer. Br J Cancer 2008; 98(4): 766-75.
    • (2008) Br J Cancer , vol.98 , Issue.4 , pp. 766-775
    • Korpi, J.T.1    Kervinen, V.2    Mäklin, H.3
  • 78
    • 0032835380 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 activation in human hepatic fibrosis regulation by cell-matrix interactions
    • Préaux AM, Mallat A, Nhieu JT, D'Ortho MP, Hembry RM, Mavier P. Matrix metalloproteinase-2 activation in human hepatic fibrosis regulation by cell-matrix interactions. Hepatology 1999; 30(4): 944-50.
    • (1999) Hepatology , vol.30 , Issue.4 , pp. 944-950
    • Préaux, A.M.1    Mallat, A.2    Nhieu, J.T.3    D'Ortho, M.P.4    Hembry, R.M.5    Mavier, P.6
  • 79
    • 0035793037 scopus 로고    scopus 로고
    • Disruption of matrix metalloproteinase 2 binding to integrin alpha v beta 3 by an organic molecule inhibits angiogenesis and tumor growth in vivo
    • Silletti S, Kessler T, Goldberg J, Boger DL, Cheresh DA. Disruption of matrix metalloproteinase 2 binding to integrin alpha v beta 3 by an organic molecule inhibits angiogenesis and tumor growth in vivo. Proc Natl Acad Sci U S A 2001; 98(1): 119-24.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , Issue.1 , pp. 119-124
    • Silletti, S.1    Kessler, T.2    Goldberg, J.3    Boger, D.L.4    Cheresh, D.A.5
  • 80
    • 78650424066 scopus 로고    scopus 로고
    • Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting
    • Gialeli C, Theocharis AD, Karamanos NK. Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting. FEBS J 2011; 278(1): 16-27.
    • (2011) FEBS J , vol.278 , Issue.1 , pp. 16-27
    • Gialeli, C.1    Theocharis, A.D.2    Karamanos, N.K.3
  • 81
    • 33846024069 scopus 로고    scopus 로고
    • The low density lipoprotein receptor-related protein functions as an endocytic receptor for decorin
    • Brandan E, Retamal C, Cabello-Verrugio C, Marzolo MP. The low density lipoprotein receptor-related protein functions as an endocytic receptor for decorin. J Biol Chem 2006; 281: 31562-71.
    • (2006) J Biol Chem , vol.281 , pp. 31562-31571
    • Brandan, E.1    Retamal, C.2    Cabello-Verrugio, C.3    Marzolo, M.P.4
  • 82
    • 34247579085 scopus 로고    scopus 로고
    • Endocytosis of the dermatan sulfate proteoglycan decorin utilizes multiple pathways and is modulated by epidermal growth factor receptor signaling
    • Feugaing DD, Tammi R, Echtermeyer FG, et al. Endocytosis of the dermatan sulfate proteoglycan decorin utilizes multiple pathways and is modulated by epidermal growth factor receptor signaling. Biochimie 2007; 89: 637-57.
    • (2007) Biochimie , vol.89 , pp. 637-657
    • Feugaing, D.D.1    Tammi, R.2    Echtermeyer, F.G.3
  • 83
    • 36248966246 scopus 로고    scopus 로고
    • RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins
    • Mailand N, Bekker-Jensen S, Faustrup H, et al. RNF8 ubiquitylates histones at DNA double-strand breaks and promotes assembly of repair proteins. Cell 2007; 131(5): 887-900.
    • (2007) Cell , vol.131 , Issue.5 , pp. 887-900
    • Mailand, N.1    Bekker-Jensen, S.2    Faustrup, H.3
  • 84
    • 78049238210 scopus 로고    scopus 로고
    • Regulation of intracellular decorin via proteasome degradation in rat mesangial cells
    • Wu H, Jiang W, Zhang Y, et al. Regulation of intracellular decorin via proteasome degradation in rat mesangial cells. J Cell Biochem 2010; 111(4): 1010-9.
    • (2010) J Cell Biochem , vol.111 , Issue.4 , pp. 1010-1019
    • Wu, H.1    Jiang, W.2    Zhang, Y.3
  • 85
    • 54049155073 scopus 로고    scopus 로고
    • Overexpression of decorin induces apoptosis and cell growth arrest in cultured rat mesangial cells in vitro
    • Wu H, Wang S, Xue A, et al. Overexpression of decorin induces apoptosis and cell growth arrest in cultured rat mesangial cells in vitro. Nephrology 2008; 13: 607-15.
    • (2008) Nephrology , vol.13 , pp. 607-615
    • Wu, H.1    Wang, S.2    Xue, A.3
  • 86
    • 33748938324 scopus 로고    scopus 로고
    • The increased accumulation of structurally modified versican and decorin is related with the progression of laryngeal cancer
    • Skandalis SS, Theocharis AD, Papageorgakopoulou N, Vynios DH, Theocharis DA. The increased accumulation of structurally modified versican and decorin is related with the progression of laryngeal cancer. Biochimie 2006; 88(9): 1135-43.
    • (2006) Biochimie , vol.88 , Issue.9 , pp. 1135-1143
    • Skandalis, S.S.1    Theocharis, A.D.2    Papageorgakopoulou, N.3    Vynios, D.H.4    Theocharis, D.A.5
  • 87
    • 0034657931 scopus 로고    scopus 로고
    • Expression of human hyaluronan synthases in response to external stimuli
    • Jacobson A, Brinck J, Briskin MJ, Spicer AP, Heldin P. Expression of human hyaluronan synthases in response to external stimuli. Biochem J 2000; 348 Pt 1: 29-35.
    • (2000) Biochem J , vol.348 , Issue.PART 1 , pp. 29-35
    • Jacobson, A.1    Brinck, J.2    Briskin, M.J.3    Spicer, A.P.4    Heldin, P.5
  • 88
    • 1842790803 scopus 로고    scopus 로고
    • Differential regulation by IL-1beta and EGF of expression of three different hyaluronan synthases in oral mucosal epithelial cells and fibroblasts and dermal fibroblasts: Quantitative analysis using real-time RT-PCR
    • Yamada Y, Itano N, Hata K, Ueda M, Kimata K. Differential regulation by IL-1beta and EGF of expression of three different hyaluronan synthases in oral mucosal epithelial cells and fibroblasts and dermal fibroblasts: quantitative analysis using real-time RT-PCR. J Invest Dermatol 2004; 122: 631-9.
    • (2004) J Invest Dermatol , vol.122 , pp. 631-639
    • Yamada, Y.1    Itano, N.2    Hata, K.3    Ueda, M.4    Kimata, K.5
  • 89
    • 64549099768 scopus 로고    scopus 로고
    • The effects of 4-methylumbelliferone on hyaluronan synthesis, MMP2 activity, proliferation, and motility of human aortic smooth muscle cells
    • Vigetti D, Rizzi M, Viola M, et al. The effects of 4-methylumbelliferone on hyaluronan synthesis, MMP2 activity, proliferation, and motility of human aortic smooth muscle cells. Glycobiology 2009; 19: 537-46.
    • (2009) Glycobiology , vol.19 , pp. 537-546
    • Vigetti, D.1    Rizzi, M.2    Viola, M.3
  • 90
    • 65949106573 scopus 로고    scopus 로고
    • Targeted suppression of Has2 mRNA in mouse cumulus cell-oocyte complexes by adenovirus-mediated short-hairpin RNA expression
    • Sugiura K, Su YQ, Eppig JJ. Targeted suppression of Has2 mRNA in mouse cumulus cell-oocyte complexes by adenovirus-mediated short-hairpin RNA expression. Mol Reprod Dev 2009; 76: 537-47.
    • (2009) Mol Reprod Dev , vol.76 , pp. 537-547
    • Sugiura, K.1    Su, Y.Q.2    Eppig, J.J.3
  • 91
    • 79955052019 scopus 로고    scopus 로고
    • Transcriptional and posttranslational regulation of hyaluronan synthesis
    • Tammi RH, Passi AG, Rilla K, et al. Transcriptional and posttranslational regulation of hyaluronan synthesis. FEBS J 2011; 278(9): 1419-28.
    • (2011) FEBS J , vol.278 , Issue.9 , pp. 1419-1428
    • Tammi, R.H.1    Passi, A.G.2    Rilla, K.3
  • 92
    • 67349260101 scopus 로고    scopus 로고
    • 4-Methylumbelliferone inhibits hyaluronan synthesis by depletion of cellular UDP-glucuronic acid and downregulation of hyaluronan synthase 2 and 3
    • Kultti A, Pasonen-Seppanen S, Jauhiainen M, et al. 4-Methylumbelliferone inhibits hyaluronan synthesis by depletion of cellular UDP-glucuronic acid and downregulation of hyaluronan synthase 2 and 3. Exp Cell Res 2009; 315: 1914-23.
    • (2009) Exp Cell Res , vol.315 , pp. 1914-1923
    • Kultti, A.1    Pasonen-Seppanen, S.2    Jauhiainen, M.3
  • 93
    • 43149119998 scopus 로고    scopus 로고
    • Mannose inhibits hyaluronan synthesis by down-regulation of the cellular pool of UDP-N-acetylhexosamines
    • Jokela TA, Jauhiainen M, Auriola S, et al. Mannose inhibits hyaluronan synthesis by down-regulation of the cellular pool of UDP-N-acetylhexosamines. J Biol Chem 2008; 283: 7666-73.
    • (2008) J Biol Chem , vol.283 , pp. 7666-7673
    • Jokela, T.A.1    Jauhiainen, M.2    Auriola, S.3
  • 94
    • 33646336898 scopus 로고    scopus 로고
    • Molecular cloning and characterization of UDP-glucose dehydrogenase from the amphibian Xenopus laevis and its involvement in hyaluronan synthesis
    • Vigetti D, Ori M, Viola M, et al. Molecular cloning and characterization of UDP-glucose dehydrogenase from the amphibian Xenopus laevis and its involvement in hyaluronan synthesis. J Biol Chem 2006; 281: 8254-63.
    • (2006) J Biol Chem , vol.281 , pp. 8254-8263
    • Vigetti, D.1    Ori, M.2    Viola, M.3
  • 95
    • 0035046380 scopus 로고    scopus 로고
    • Regulation of renal proximal tubular epithelial cell hyaluronan generation: Implications for diabetic nephropathy
    • Jones S, Phillips AO. Regulation of renal proximal tubular epithelial cell hyaluronan generation: implications for diabetic nephropathy. Kidney Int 2001; 59: 1739-49.
    • (2001) Kidney Int , vol.59 , pp. 1739-1749
    • Jones, S.1    Phillips, A.O.2
  • 96
    • 1642414046 scopus 로고    scopus 로고
    • Hyaluronan structures synthesized by rat mesangial cells in response to hyperglycemia induce monocyte adhesion
    • Wang A, Hascall VC. Hyaluronan structures synthesized by rat mesangial cells in response to hyperglycemia induce monocyte adhesion. J Biol Chem 2004; 279: 10279-85.
    • (2004) J Biol Chem , vol.279 , pp. 10279-10285
    • Wang, A.1    Hascall, V.C.2
  • 97
    • 79955063269 scopus 로고    scopus 로고
    • Hyaluronan matrices in pathobiological processes
    • Wang A, de la Motte C, Lauer M, Hascall V. Hyaluronan matrices in pathobiological processes. FEBS J 2011; 278(9): 1412-8.
    • (2011) FEBS J , vol.278 , Issue.9 , pp. 1412-1418
    • Wang, A.1    de la Motte, C.2    Lauer, M.3    Hascall, V.4
  • 98
    • 0033852661 scopus 로고    scopus 로고
    • Role of the hexosamine biosynthetic pathway in diabetic nephropathy
    • Schleicher ED, Weigert C. Role of the hexosamine biosynthetic pathway in diabetic nephropathy. Kidney Int Suppl 2000; 77: S13-S18.
    • (2000) Kidney Int Suppl , vol.77
    • Schleicher, E.D.1    Weigert, C.2
  • 99
    • 2042540707 scopus 로고    scopus 로고
    • Activation of the hexosamine signaling pathway in adipose tissue results in decreased serum adiponectin and skeletal muscle insulin resistance
    • Hazel M, Cooksey RC, Jones D, et al. Activation of the hexosamine signaling pathway in adipose tissue results in decreased serum adiponectin and skeletal muscle insulin resistance. Endocrinology 2004; 145: 2118-28.
    • (2004) Endocrinology , vol.145 , pp. 2118-2128
    • Hazel, M.1    Cooksey, R.C.2    Jones, D.3
  • 100
    • 0034703095 scopus 로고    scopus 로고
    • O-Glycosylation of nuclear and cytosolic proteins. Dynamic interplay between O-GlcNAc and Ophosphate
    • Comer FI, Hart GW. O-Glycosylation of nuclear and cytosolic proteins. Dynamic interplay between O-GlcNAc and Ophosphate. J Biol Chem 2000; 275: 29179-82.
    • (2000) J Biol Chem , vol.275 , pp. 29179-29182
    • Comer, F.I.1    Hart, G.W.2
  • 101
    • 80052068559 scopus 로고    scopus 로고
    • O-GlcNAc signalling: Implications for cancer cell biology
    • Slawson C, Hart GW. O-GlcNAc signalling: implications for cancer cell biology. Nat Rev Cancer 2011; 11(9): 678-84.
    • (2011) Nat Rev Cancer , vol.11 , Issue.9 , pp. 678-684
    • Slawson, C.1    Hart, G.W.2
  • 102
    • 80052999905 scopus 로고    scopus 로고
    • Cellular content of UDP-N-acetylhexosamines controls hyaluronan synthase 2 expression and correlates with O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1
    • Jokela TA, Makkonen KM, Oikari S, et al. Cellular content of UDP-N-acetylhexosamines controls hyaluronan synthase 2 expression and correlates with O-linked N-acetylglucosamine modification of transcription factors YY1 and SP1. J Biol Chem 2011; 286(38): 33632-40.
    • (2011) J Biol Chem , vol.286 , Issue.38 , pp. 33632-33640
    • Jokela, T.A.1    Makkonen, K.M.2    Oikari, S.3
  • 103
    • 0346965700 scopus 로고    scopus 로고
    • O-GlcNAc modification is an endogenous inhibitor of the proteasome
    • Zhang F, Su K, Yang X, Bowe DB, Paterson AJ, Kudlow JE. O-GlcNAc modification is an endogenous inhibitor of the proteasome. Cell 2003; 115(6): 715-25.
    • (2003) Cell , vol.115 , Issue.6 , pp. 715-725
    • Zhang, F.1    Su, K.2    Yang, X.3    Bowe, D.B.4    Paterson, A.J.5    Kudlow, J.E.6
  • 104
    • 0036104603 scopus 로고    scopus 로고
    • Not just research tools--proteasome inhibitors offer therapeutic promise
    • Goldberg AL, Rock K. Not just research tools--proteasome inhibitors offer therapeutic promise. Nat Med 2002; 8(4): 338-40.
    • (2002) Nat Med , vol.8 , Issue.4 , pp. 338-340
    • Goldberg, A.L.1    Rock, K.2
  • 105
    • 0034864799 scopus 로고    scopus 로고
    • Proteasome inhibitors: From research tools to drug candidates
    • Kisselev AF, Goldberg AL. Proteasome inhibitors: from research tools to drug candidates. Chem Biol 2001; 8(8): 739-58.
    • (2001) Chem Biol , vol.8 , Issue.8 , pp. 739-758
    • Kisselev, A.F.1    Goldberg, A.L.2
  • 106
    • 83355163253 scopus 로고    scopus 로고
    • Inhibition of proteasomal proteolysis affects expression of extracellular matrix components and steroidogenesis in porcine oocytecumulus complexes
    • Nagyova E, Scsukova S, Nemcova L, et al. Inhibition of proteasomal proteolysis affects expression of extracellular matrix components and steroidogenesis in porcine oocytecumulus complexes. Domest Anim Endocrinol 2012; 42(1): 50-62.
    • (2012) Domest Anim Endocrinol , vol.42 , Issue.1 , pp. 50-62
    • Nagyova, E.1    Scsukova, S.2    Nemcova, L.3
  • 107
    • 77954908007 scopus 로고    scopus 로고
    • The activity of hyaluronan synthase 2 is regulated by dimerization and ubiquitination
    • Karousou E, Kamiryo M, Skandalis SS, et al. The activity of hyaluronan synthase 2 is regulated by dimerization and ubiquitination. J Biol Chem 2010; 285(31): 23647-54.
    • (2010) J Biol Chem , vol.285 , Issue.31 , pp. 23647-23654
    • Karousou, E.1    Kamiryo, M.2    Skandalis, S.S.3
  • 108
    • 34547646665 scopus 로고    scopus 로고
    • Heparan sulfate degradation products can associate with oxidized proteins and proteasomes
    • Mani K, Cheng F, Fransson LA. Heparan sulfate degradation products can associate with oxidized proteins and proteasomes. J Biol Chem 2007; 282(30): 21934-44.
    • (2007) J Biol Chem , vol.282 , Issue.30 , pp. 21934-21944
    • Mani, K.1    Cheng, F.2    Fransson, L.A.3
  • 109
    • 0029907548 scopus 로고    scopus 로고
    • Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans
    • Goedert M, Jakes R, Spillantini MG, Hasegawa M, Smith MJ, Crowther RA. Assembly of microtubule-associated protein tau into Alzheimer-like filaments induced by sulphated glycosaminoglycans. Nature 1996; 383: 550-3.
    • (1996) Nature , vol.383 , pp. 550-553
    • Goedert, M.1    Jakes, R.2    Spillantini, M.G.3    Hasegawa, M.4    Smith, M.J.5    Crowther, R.A.6
  • 110
    • 0034810802 scopus 로고    scopus 로고
    • Molecular genetics of mucopolysaccharidosis type IIIA and IIIB: Diagnostic, clinical, and biological implications
    • Yogalingam G, Hopwood JJ. Molecular genetics of mucopolysaccharidosis type IIIA and IIIB: Diagnostic, clinical, and biological implications. Hum Mutat 2001; 18: 264-81.
    • (2001) Hum Mutat , vol.18 , pp. 264-281
    • Yogalingam, G.1    Hopwood, J.J.2
  • 111
    • 6944221779 scopus 로고    scopus 로고
    • Glypican-1 as an Abeta binding HSPG in the human brain: Its localization in DIG domains and possible roles in the pathogenesis of Alzheimer's disease
    • Watanabe N, Araki W, Chui D-H, Makifuchi T, Ihara Y, Tabira T. Glypican-1 as an Abeta binding HSPG in the human brain: its localization in DIG domains and possible roles in the pathogenesis of Alzheimer's disease. FASEB J 2004; 18: 1013-5.
    • (2004) FASEB J , vol.18 , pp. 1013-1015
    • Watanabe, N.1    Araki, W.2    Chui, D-H.3    Makifuchi, T.4    Ihara, Y.5    Tabira, T.6
  • 112
    • 0343729304 scopus 로고    scopus 로고
    • A novel role for nitric oxide in the endogenous degradation of heparan sulfate during recycling of glypican-1 in vascular endothelial cells
    • Mani K, Jonsson, M, Edgren G, Belting M, Fransson LA. A novel role for nitric oxide in the endogenous degradation of heparan sulfate during recycling of glypican-1 in vascular endothelial cells. Glycobiology 2000; 10: 577-86.
    • (2000) Glycobiology , vol.10 , pp. 577-586
    • Mani, K.1    Jonsson, M.2    Edgren, G.3    Belting, M.4    Fransson, L.A.5
  • 113
    • 0037031909 scopus 로고    scopus 로고
    • Copperdependent autocleavage of glypican-1 heparan sulfate by nitric oxide derived from intrinsic nitrosothiols
    • Ding K, Mani K, Cheng F, Belting M, Fransson LA. Copperdependent autocleavage of glypican-1 heparan sulfate by nitric oxide derived from intrinsic nitrosothiols. J Biol Chem 2002; 277: 33353-60.
    • (2002) J Biol Chem , vol.277 , pp. 33353-33360
    • Ding, K.1    Mani, K.2    Cheng, F.3    Belting, M.4    Fransson, L.A.5
  • 114
    • 0037113903 scopus 로고    scopus 로고
    • Nitric oxide-dependent processing of heparan sulfate in recycling S-nitrosylated glypican-1 takes place in caveolin-1-containing endosomes
    • Cheng F, Mani K, van den Born J, Ding K, Belting M, Fransson LA. Nitric oxide-dependent processing of heparan sulfate in recycling S-nitrosylated glypican-1 takes place in caveolin-1-containing endosomes. J Biol Chem 2002; 277: 44431-9.
    • (2002) J Biol Chem , vol.277 , pp. 44431-44439
    • Cheng, F.1    Mani, K.2    van den Born, J.3    Ding, K.4    Belting, M.5    Fransson, L.A.6
  • 115
    • 0030958277 scopus 로고    scopus 로고
    • Nitric oxide degradation of heparin and heparan sulphate
    • Vilar RE, Ghael D, Li M, et al. Nitric oxide degradation of heparin and heparan sulphate. Biochem J 1997; 324: 473-9.
    • (1997) Biochem J , vol.324 , pp. 473-479
    • Vilar, R.E.1    Ghael, D.2    Li, M.3
  • 117
    • 0023153759 scopus 로고
    • Synaptophysin. A new marker for pancreatic neuroendocrine tumors
    • Chejfec G, Falkmer S, Grimelius L, et al. Synaptophysin. A new marker for pancreatic neuroendocrine tumors. Am J Surg Pathol 1987; 11(4): 241-7.
    • (1987) Am J Surg Pathol , vol.11 , Issue.4 , pp. 241-247
    • Chejfec, G.1    Falkmer, S.2    Grimelius, L.3
  • 118
    • 33646593786 scopus 로고    scopus 로고
    • Modifying the soil to affect the seed: Role of stromal-derived matrix metalloproteinases in cancer progression
    • Jodele S, Blavier L, Yoon JM, DeClerck, YA. Modifying the soil to affect the seed: role of stromal-derived matrix metalloproteinases in cancer progression. Cancer Metastasis Rev 2006; 25: 35-43.
    • (2006) Cancer Metastasis Rev , vol.25 , pp. 35-43
    • Jodele, S.1    Blavier, L.2    Yoon, J.M.3    DeClerck, Y.A.4
  • 119
    • 33847195428 scopus 로고    scopus 로고
    • Matrix metalloproteinases and the regulation of tissue remodelling
    • Page-McCaw A, Ewald AJ, Werb Z. Matrix metalloproteinases and the regulation of tissue remodelling. Nat Rev Mol Cell Biol 2007; 8: 221-33.
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 221-233
    • Page-McCaw, A.1    Ewald, A.J.2    Werb, Z.3
  • 120
    • 0033597726 scopus 로고    scopus 로고
    • The stromal proteinase MMP3/stromelysin-1 promotes mammary carcinogenesis
    • Sternlicht MD, Lochter A, Sympson CJ, et al. The stromal proteinase MMP3/stromelysin-1 promotes mammary carcinogenesis. Cell 1999; 98: 137-46.
    • (1999) Cell , vol.98 , pp. 137-146
    • Sternlicht, M.D.1    Lochter, A.2    Sympson, C.J.3
  • 121
    • 51049100625 scopus 로고    scopus 로고
    • Effect of ablation or inhibition of stromal matrix metalloproteinase-9 on lung metastasis in a breast cancer model is dependent on genetic background
    • Martin MD, Carter KJ, Jean-Philippe SR, et al. Effect of ablation or inhibition of stromal matrix metalloproteinase-9 on lung metastasis in a breast cancer model is dependent on genetic background. Cancer Res 2008; 68: 6251-9.
    • (2008) Cancer Res , vol.68 , pp. 6251-6259
    • Martin, M.D.1    Carter, K.J.2    Jean-Philippe, S.R.3
  • 122
    • 0037192458 scopus 로고    scopus 로고
    • Matrix metalloproteinase inhibitors and cancer: Trials and tribulations
    • Coussens LM, Fingleton B, Matrisian LM. Matrix metalloproteinase inhibitors and cancer: trials and tribulations. Science 2002; 295: 2387-92.
    • (2002) Science , vol.295 , pp. 2387-2392
    • Coussens, L.M.1    Fingleton, B.2    Matrisian, L.M.3
  • 123
    • 57749098804 scopus 로고    scopus 로고
    • Lysyl oxidase binds transforming growth factor-beta and regulates its signaling via amine oxidase activity
    • Atsawasuwan P, Mochida Y, Katafuchi M, et al. Lysyl oxidase binds transforming growth factor-beta and regulates its signaling via amine oxidase activity. J Biol Chem 2008; 283: 34229-40.
    • (2008) J Biol Chem , vol.283 , pp. 34229-34240
    • Atsawasuwan, P.1    Mochida, Y.2    Katafuchi, M.3
  • 124
    • 0035232015 scopus 로고    scopus 로고
    • Lysyl oxidases: A novel multifunctional amine oxidase family
    • Csiszar K. Lysyl oxidases: a novel multifunctional amine oxidase family. Prog Nucleic Acid Res Mol Biol 2001; 70: 1-32.
    • (2001) Prog Nucleic Acid Res Mol Biol , vol.70 , pp. 1-32
    • Csiszar, K.1
  • 125
    • 23444439813 scopus 로고    scopus 로고
    • Lysyl oxidase in development, aging and pathologies of the skin
    • Szauter KM, Cao T, Boyd CD, Csiszar K. Lysyl oxidase in development, aging and pathologies of the skin. Pathol Biol (Paris) 2005; 53: 448-56.
    • (2005) Pathol Biol (Paris) , vol.53 , pp. 448-456
    • Szauter, K.M.1    Cao, T.2    Boyd, C.D.3    Csiszar, K.4
  • 126
  • 128
    • 0033917881 scopus 로고    scopus 로고
    • Cell movement is guided by the rigidity of the substrate
    • Lo CM, Wang HB, Dembo M, Wang YL. Cell movement is guided by the rigidity of the substrate. Biophys J 2000; 79: 144-52.
    • (2000) Biophys J , vol.79 , pp. 144-152
    • Lo, C.M.1    Wang, H.B.2    Dembo, M.3    Wang, Y.L.4
  • 129
    • 0033696170 scopus 로고    scopus 로고
    • Substrate flexibility regulates growth and apoptosis of normal but not transformed cells
    • Wang HB, Dembo M, Wang YL. Substrate flexibility regulates growth and apoptosis of normal but not transformed cells. Am J Physiol Cell Physiol 2000; 279: C1345-50.
    • (2000) Am J Physiol Cell Physiol , vol.279
    • Wang, H.B.1    Dembo, M.2    Wang, Y.L.3
  • 130
    • 0034238092 scopus 로고    scopus 로고
    • Mechanochemical manipulation of hepatocyte aggregation can selectively induce or repress liver-specific function
    • Semler EJ, Ranucci CS, Moghe PV. Mechanochemical manipulation of hepatocyte aggregation can selectively induce or repress liver-specific function. Biotechnol Bioeng 2000; 69: 359-69.
    • (2000) Biotechnol Bioeng , vol.69 , pp. 359-369
    • Semler, E.J.1    Ranucci, C.S.2    Moghe, P.V.3
  • 131
    • 57549105751 scopus 로고    scopus 로고
    • Substrate modulus directs neural stem cell behavior
    • Saha K, Keung AJ, Irwin EF, et al. Substrate modulus directs neural stem cell behavior. Biophys J 2008; 95: 4426-38.
    • (2008) Biophys J , vol.95 , pp. 4426-4438
    • Saha, K.1    Keung, A.J.2    Irwin, E.F.3
  • 132
    • 24944547482 scopus 로고    scopus 로고
    • Tensional homeostasis and the malignant phenotype
    • Paszek MJ, Zahir N, Johnson KR, et al. Tensional homeostasis and the malignant phenotype. Cancer Cell 2005; 8: 241-54.
    • (2005) Cancer Cell , vol.8 , pp. 241-254
    • Paszek, M.J.1    Zahir, N.2    Johnson, K.R.3
  • 133
    • 38549148896 scopus 로고    scopus 로고
    • Biochemical and biophysical aspects of collagen nanostructure in the extracellular matrix
    • Kolacna L, Bakesova J, Varga F, et al. Biochemical and biophysical aspects of collagen nanostructure in the extracellular matrix. Physiol Res 2007; 56: S51-60.
    • (2007) Physiol Res , vol.56
    • Kolacna, L.1    Bakesova, J.2    Varga, F.3
  • 134
    • 0037226593 scopus 로고    scopus 로고
    • A molecular signature of metastasis in primary solid tumors
    • Ramaswamy S, Ross KN, Lander ES, Golub TR. A molecular signature of metastasis in primary solid tumors. Nat Genet 2003; 33: 49-54.
    • (2003) Nat Genet , vol.33 , pp. 49-54
    • Ramaswamy, S.1    Ross, K.N.2    Lander, E.S.3    Golub, T.R.4
  • 135
    • 43149112727 scopus 로고    scopus 로고
    • Mammographic density. Potential mechanisms of breast cancer risk associated with mammographic density: Hypotheses based on epidemiological evidence
    • Martin LJ, Boyd NF. Mammographic density. Potential mechanisms of breast cancer risk associated with mammographic density: hypotheses based on epidemiological evidence. Breast Cancer Res 2008; 10: 201.
    • (2008) Breast Cancer Res , vol.10 , pp. 201
    • Martin, L.J.1    Boyd, N.F.2
  • 136
    • 0036097996 scopus 로고    scopus 로고
    • Prognostic significance of fibrotic focus in invasive ductal carcinoma of the breast: A prospective observational study
    • Hasebe T, Sasaki S, Imoto S, Mukai K, Yokose T, Ochiai A. Prognostic significance of fibrotic focus in invasive ductal carcinoma of the breast: a prospective observational study. Mod Pathol 2002; 15: 502-16.
    • (2002) Mod Pathol , vol.15 , pp. 502-516
    • Hasebe, T.1    Sasaki, S.2    Imoto, S.3    Mukai, K.4    Yokose, T.5    Ochiai, A.6
  • 137
    • 49649106050 scopus 로고    scopus 로고
    • Gene expression profiles associated with the presence of a fibrotic focus and the growth pattern in lymph node-negative breast cancer
    • Van den Eynden GG, Smid M, Van Laere SJ, et al. Gene expression profiles associated with the presence of a fibrotic focus and the growth pattern in lymph node-negative breast cancer. Clin Cancer Res 2008; 14: 2944-52.
    • (2008) Clin Cancer Res , vol.14 , pp. 2944-2952
    • van den Eynden, G.G.1    Smid, M.2    van Laere, S.J.3
  • 138
    • 0036533617 scopus 로고    scopus 로고
    • Extracellular matrix building marked by the N-terminal propeptide of procollagen type I reflect aggressiveness of recurrent breast cancer
    • Jensen BV, Johansen JS, Skovsgaard T, Brandt J, Teisner B. Extracellular matrix building marked by the N-terminal propeptide of procollagen type I reflect aggressiveness of recurrent breast cancer. Int J Cancer 2002; 98: 582-9.
    • (2002) Int J Cancer , vol.98 , pp. 582-589
    • Jensen, B.V.1    Johansen, J.S.2    Skovsgaard, T.3    Brandt, J.4    Teisner, B.5
  • 139
    • 70450222098 scopus 로고    scopus 로고
    • Matrix crosslinking forces tumor progression by enhancing integrin signaling
    • Levental KR, Yu H, Kass L, et al. Matrix crosslinking forces tumor progression by enhancing integrin signaling. Cell 2009; 139(5): 891-906.
    • (2009) Cell , vol.139 , Issue.5 , pp. 891-906
    • Levental, K.R.1    Yu, H.2    Kass, L.3
  • 140
    • 33645805628 scopus 로고    scopus 로고
    • Proteasome blockade exerts an antifibrotic activity by coordinately down-regulating type I collagen and tissue inhibitor of metalloproteinase-1 and up-regulating metalloproteinase-1 production in human dermal fibroblasts
    • Fineschi S, Reith W, Guerne PA, Dayer JM, Chizzolini C. Proteasome blockade exerts an antifibrotic activity by coordinately down-regulating type I collagen and tissue inhibitor of metalloproteinase-1 and up-regulating metalloproteinase-1 production in human dermal fibroblasts. FASEB J 2006; 20(3): 562-4.
    • (2006) FASEB J , vol.20 , Issue.3 , pp. 562-564
    • Fineschi, S.1    Reith, W.2    Guerne, P.A.3    Dayer, J.M.4    Chizzolini, C.5
  • 141
    • 77951554549 scopus 로고    scopus 로고
    • Transcriptional regulation of matrix metalloproteinase-1 and collagen 1A2 explains the anti-fibrotic effect exerted by proteasome inhibition in human dermal fibroblasts
    • Goffin L, Seguin-Estévez Q, Alvarez M, Reith W, Chizzolini C. Transcriptional regulation of matrix metalloproteinase-1 and collagen 1A2 explains the anti-fibrotic effect exerted by proteasome inhibition in human dermal fibroblasts. Arthritis Res Ther 2010; 12(2): R73.
    • (2010) Arthritis Res Ther , vol.12 , Issue.2
    • Goffin, L.1    Seguin-Estévez, Q.2    Alvarez, M.3    Reith, W.4    Chizzolini, C.5
  • 142
    • 0030932125 scopus 로고    scopus 로고
    • The AP-1 site and MMP gene regulation: What is all the fuss about?
    • Benbow U, Brinckerhoff CE. The AP-1 site and MMP gene regulation: what is all the fuss about? Matrix Biol 1997; 15: 519-26.
    • (1997) Matrix Biol , vol.15 , pp. 519-526
    • Benbow, U.1    Brinckerhoff, C.E.2
  • 143
    • 0037189946 scopus 로고    scopus 로고
    • Proteasome inhibitors stimulate activator protein-1 pathway via reactive oxygen species production
    • Wu HM, Chi KH, Lin WW. Proteasome inhibitors stimulate activator protein-1 pathway via reactive oxygen species production. FEBS Lett 2002; 526(1-3): 101-5.
    • (2002) FEBS Lett , vol.526 , Issue.1-3 , pp. 101-105
    • Wu, H.M.1    Chi, K.H.2    Lin, W.W.3
  • 144
    • 71049176929 scopus 로고    scopus 로고
    • The proteasome is an integral part of solar ultraviolet a radiation-induced gene expression
    • Catalgol B, Ziaja I, Breusing N, et al. The proteasome is an integral part of solar ultraviolet a radiation-induced gene expression. J Biol Chem 2009; 284(44): 30076-86.
    • (2009) J Biol Chem , vol.284 , Issue.44 , pp. 30076-30086
    • Catalgol, B.1    Ziaja, I.2    Breusing, N.3
  • 145
    • 0037200088 scopus 로고    scopus 로고
    • Activation of p38 alpha MAPK enhances collagenase-1 (matrix metalloproteinase (MMP)-1) and stromelysin-1 (MMP-3) expression by mRNA stabilization
    • Reunanen N, Li SP, Ahonen M, Foschi M, Han J, Kähäri VM. Activation of p38 alpha MAPK enhances collagenase-1 (matrix metalloproteinase (MMP)-1) and stromelysin-1 (MMP-3) expression by mRNA stabilization. J Biol Chem 2002; 277(35): 32360-8.
    • (2002) J Biol Chem , vol.277 , Issue.35 , pp. 32360-32368
    • Reunanen, N.1    Li, S.P.2    Ahonen, M.3    Foschi, M.4    Han, J.5    Kähäri, V.M.6
  • 146
    • 0035422658 scopus 로고    scopus 로고
    • Unexpected transcriptional induction of monocyte chemoattractant protein 1 by proteasome inhibition: Involvement of the c-Jun N-terminal kinase-activator protein 1 pathway
    • Nakayama K, Furusu A, Xu Q, Konta T, Kitamura M. Unexpected transcriptional induction of monocyte chemoattractant protein 1 by proteasome inhibition: involvement of the c-Jun N-terminal kinase-activator protein 1 pathway. J Immunol 2001; 167(3): 1145-50.
    • (2001) J Immunol , vol.167 , Issue.3 , pp. 1145-1150
    • Nakayama, K.1    Furusu, A.2    Xu, Q.3    Konta, T.4    Kitamura, M.5
  • 147
    • 0034972517 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha induces expression of genes for matrix degradation in human chondrocyte-like HCS-2/8 cells through activation of NF-kappaB: Abrogation of the tumor necrosis factor alpha effect by proteasome inhibitors
    • Sakai T, Kambe F, Mitsuyama H, et al. Tumor necrosis factor alpha induces expression of genes for matrix degradation in human chondrocyte-like HCS-2/8 cells through activation of NF-kappaB: abrogation of the tumor necrosis factor alpha effect by proteasome inhibitors. J Bone Miner Res 2001; 16(7): 1272-80.
    • (2001) J Bone Miner Res , vol.16 , Issue.7 , pp. 1272-1280
    • Sakai, T.1    Kambe, F.2    Mitsuyama, H.3
  • 148
    • 4644306893 scopus 로고    scopus 로고
    • Downregulation of matrix metalloproteinases and collagens and suppression of cardiac fibrosis by inhibition of the proteasome
    • Meiners S, Hocher B, Weller A, et al. Downregulation of matrix metalloproteinases and collagens and suppression of cardiac fibrosis by inhibition of the proteasome. Hypertension 2004; 44(4): 471-7.
    • (2004) Hypertension , vol.44 , Issue.4 , pp. 471-477
    • Meiners, S.1    Hocher, B.2    Weller, A.3
  • 149
    • 4444235841 scopus 로고    scopus 로고
    • The proteasome inhibitor bortezomib synergizes with gemcitabine to block the growth of human 253JB-V bladder tumors in vivo
    • Kamat AM, Karashima T, Davis DW, et al. The proteasome inhibitor bortezomib synergizes with gemcitabine to block the growth of human 253JB-V bladder tumors in vivo. Mol Cancer Ther 2004; 3(3): 279-90.
    • (2004) Mol Cancer Ther , vol.3 , Issue.3 , pp. 279-290
    • Kamat, A.M.1    Karashima, T.2    Davis, D.W.3
  • 150
    • 9444249941 scopus 로고    scopus 로고
    • Evidence that mitogen-activated protein kinase phosphatase-1 induction by proteasome inhibitors plays an antiapoptotic role
    • Small GW, Shi YY, Edmund NA, Somasundaram S, Moore DT, Orlowski RZ. Evidence that mitogen-activated protein kinase phosphatase-1 induction by proteasome inhibitors plays an antiapoptotic role. Mol Pharmacol 2004; 66(6): 1478-90.
    • (2004) Mol Pharmacol , vol.66 , Issue.6 , pp. 1478-1490
    • Small, G.W.1    Shi, Y.Y.2    Edmund, N.A.3    Somasundaram, S.4    Moore, D.T.5    Orlowski, R.Z.6
  • 151
    • 79953736762 scopus 로고    scopus 로고
    • Matrix stiffness modulates proliferation, chemotherapeutic response, and dormancy in hepatocellular carcinoma cells
    • Schrader J, Gordon-Walker TT, Aucott RL, et al. Matrix stiffness modulates proliferation, chemotherapeutic response, and dormancy in hepatocellular carcinoma cells. Hepatology 2011; 53(4): 1192-205.
    • (2011) Hepatology , vol.53 , Issue.4 , pp. 1192-1205
    • Schrader, J.1    Gordon-Walker, T.T.2    Aucott, R.L.3
  • 152
    • 77955021301 scopus 로고    scopus 로고
    • Metastatic growth from dormant cells induced by a col-I-enriched fibrotic environment
    • Barkan D, El Touny LH, Michalowski AM, et al. Metastatic growth from dormant cells induced by a col-I-enriched fibrotic environment. Cancer Res 2010; 70(14): 5706-16.
    • (2010) Cancer Res , vol.70 , Issue.14 , pp. 5706-5716
    • Barkan, D.1    El Touny, L.H.2    Michalowski, A.M.3
  • 153
    • 66249100268 scopus 로고    scopus 로고
    • The mechanical rigidity of the extracellular matrix regulates the structure, motility, and proliferation of glioma cells
    • Ulrich TA, de Juan Pardo EM, Kumar S. The mechanical rigidity of the extracellular matrix regulates the structure, motility, and proliferation of glioma cells. Cancer Res 2009; 69(10): 4167-74.
    • (2009) Cancer Res , vol.69 , Issue.10 , pp. 4167-4174
    • Ulrich, T.A.1    de Juan Pardo, E.M.2    Kumar, S.3
  • 154
  • 155
    • 0037821846 scopus 로고    scopus 로고
    • Inhibition of proteasome activity induces concerted expression of proteasome genes and de novo formation of Mammalian proteasomes
    • Meiners S, Heyken D, Weller A, et al. Inhibition of proteasome activity induces concerted expression of proteasome genes and de novo formation of Mammalian proteasomes. J Biol Chem 2003; 278(24): 21517-25.
    • (2003) J Biol Chem , vol.278 , Issue.24 , pp. 21517-21525
    • Meiners, S.1    Heyken, D.2    Weller, A.3
  • 156
    • 38149082008 scopus 로고    scopus 로고
    • Increased expression and altered subunit composition of proteasomes induced by continuous proteasome inhibition establish apoptosis resistance and hyperproliferation of Burkitt lymphoma cells
    • Fuchs D, Berges C, Opelz G, Daniel V, Naujokat C. Increased expression and altered subunit composition of proteasomes induced by continuous proteasome inhibition establish apoptosis resistance and hyperproliferation of Burkitt lymphoma cells. J Cell Biochem 2008; 103(1): 270-83.
    • (2008) J Cell Biochem , vol.103 , Issue.1 , pp. 270-283
    • Fuchs, D.1    Berges, C.2    Opelz, G.3    Daniel, V.4    Naujokat, C.5
  • 157
    • 33744477355 scopus 로고    scopus 로고
    • Preincubation with the proteasome inhibitor MG-132 enhances proteasome activity via the Nrf2 transcription factor in aging human skin fibroblasts
    • Kraft DC, Deocaris CC, Wadhwa R, Rattan SI. Preincubation with the proteasome inhibitor MG-132 enhances proteasome activity via the Nrf2 transcription factor in aging human skin fibroblasts. Ann N Y Acad Sci 2006; 1067: 420-4.
    • (2006) Ann N Y Acad Sci , vol.1067 , pp. 420-424
    • Kraft, D.C.1    Deocaris, C.C.2    Wadhwa, R.3    Rattan, S.I.4
  • 158
    • 33744899830 scopus 로고    scopus 로고
    • Induction of 26S proteasome subunit PSMB5 by the bifunctional inducer 3-methylcholanthrene through the Nrf2-ARE, but not the AhR/Arnt-XRE, pathway
    • Kwak MK, Kensler TW. Induction of 26S proteasome subunit PSMB5 by the bifunctional inducer 3-methylcholanthrene through the Nrf2-ARE, but not the AhR/Arnt-XRE, pathway. Biochem Biophys Res Commun 2006; 345(4): 1350-7.
    • (2006) Biochem Biophys Res Commun , vol.345 , Issue.4 , pp. 1350-1357
    • Kwak, M.K.1    Kensler, T.W.2
  • 159
    • 84858972249 scopus 로고    scopus 로고
    • Nrf2-dependent induction of proteasome and Pa28__ regulator are required for adaptation to oxidative stress
    • Pickering AM, Linder RA, Zhang H, Forman HJ, Davies KJ. Nrf2-dependent induction of proteasome and Pa28__ regulator are required for adaptation to oxidative stress. J Biol Chem 2012; 287(13): 10021-31.
    • (2012) J Biol Chem , vol.287 , Issue.13 , pp. 10021-10031
    • Pickering, A.M.1    Linder, R.A.2    Zhang, H.3    Forman, H.J.4    Davies, K.J.5
  • 160
    • 37649017714 scopus 로고    scopus 로고
    • Identification of retinoic acid as an inhibitor of transcription factor Nrf2 through activation of retinoic acid receptor alpha
    • Wang XJ, Hayes JD, Henderson CJ, Wolf CR. Identification of retinoic acid as an inhibitor of transcription factor Nrf2 through activation of retinoic acid receptor alpha. Proc Natl Acad Sci USA 2007; 104(49): 19589-94.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.49 , pp. 19589-19594
    • Wang, X.J.1    Hayes, J.D.2    Henderson, C.J.3    Wolf, C.R.4
  • 161
    • 79955612814 scopus 로고    scopus 로고
    • Luteolin inhibits Nrf2 leading to negative regulation of the Nrf2/ARE pathway and sensitization of human lung carcinoma A549 cells to therapeutic drugs
    • Tang X, Wang H, Fan L, et al. Luteolin inhibits Nrf2 leading to negative regulation of the Nrf2/ARE pathway and sensitization of human lung carcinoma A549 cells to therapeutic drugs. Free Radic Biol Med 2011; 50(11): 1599-609.
    • (2011) Free Radic Biol Med , vol.50 , Issue.11 , pp. 1599-1609
    • Tang, X.1    Wang, H.2    Fan, L.3


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