Skip to main content Accessibility help
×
Home

Review of: Opposing roles for specific TIMPs in breast cancer prognosis

  • E. W. Thompson (a1) (a2) and A. R. Mackay (a3)
  • View HTML
    • Send article to Kindle

      To send this article to your Kindle, first ensure no-reply@cambridge.org is added to your Approved Personal Document E-mail List under your Personal Document Settings on the Manage Your Content and Devices page of your Amazon account. Then enter the ‘name’ part of your Kindle email address below. Find out more about sending to your Kindle. Find out more about sending to your Kindle.

      Note you can select to send to either the @free.kindle.com or @kindle.com variations. ‘@free.kindle.com’ emails are free but can only be sent to your device when it is connected to wi-fi. ‘@kindle.com’ emails can be delivered even when you are not connected to wi-fi, but note that service fees apply.

      Find out more about the Kindle Personal Document Service.

      Review of: Opposing roles for specific TIMPs in breast cancer prognosis
      Available formats
      ×

      Send article to Dropbox

      To send this article to your Dropbox account, please select one or more formats and confirm that you agree to abide by our usage policies. If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your <service> account. Find out more about sending content to Dropbox.

      Review of: Opposing roles for specific TIMPs in breast cancer prognosis
      Available formats
      ×

      Send article to Google Drive

      To send this article to your Google Drive account, please select one or more formats and confirm that you agree to abide by our usage policies. If this is the first time you use this feature, you will be asked to authorise Cambridge Core to connect with your <service> account. Find out more about sending content to Google Drive.

      Review of: Opposing roles for specific TIMPs in breast cancer prognosis
      Available formats
      ×

Abstract

  • An abstract is not available for this content so a preview has been provided below. To view the full text please use the links above to select your preferred format.

Copyright

Corresponding author

Correspondence to: Erik W. Thompson, St Vincent's Institute of Medical Research, Fitzroy, Victoria, 3065, Australia. E-mail: rik@medstv.unimelb.edu.au; Tel: +61 3 9288 2569; Fax: +61 3 9416 0926

References

Hide All

References

Woessner JrJF. Matrix metalloproteinases and their inhibitors in connective tissue remodeling. FASEB 1991; 5: 21452154.
Baker AH, Edwards DR, Murphy G. Metalloproteinase inhibitors: biological actions and therapeutic opportunities. J Cell Sci 2002; 115: 37193727.
Stetler-Stevenson WG, Liotta LA, Kleiner DE. Extracellular matrix 6: role of matrix metalloproteinases in tumor invasion and metastasis. FASEB 1993; 7: 14341441.
Coussens LM, Fingleton B, Matrisian LM. Matrix metalloproteinase inhibitors and cancer: trials and tribulations. Science 2002; 295: 23872392.
Overall CM, Lopez-Otin C. Strategies for MMP inhibition in cancer: innovations for the post-trial era. Nat Rev Cancer 2002; 2: 657672.
Egeblad M, Werb Z. New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer 2002; 2: 161174.
Span PN, Lindberg RL, Manders Pet al. Tissue inhibitors of metalloproteinase expression in human breast cancer: TIMP-3 is associated with adjuvant endocrine therapy success. J Pathol 2004; 202: 395402.
Chambers AF, Matrisian LM. Changing views of the role of matrix metalloproteinases in metastasis. J Natl Cancer Inst 1997; 89: 12601270.
Ahonen M, Baker AH, Kahari VM. Adenovirus-mediated gene delivery of tissue inhibitor of metalloproteinases-3 inhibits invasion and induces apoptosis in melanoma cells. Cancer Res 1998; 58: 23102315.
Baker AH, George SJ, Zaltsman AB, et al. Inhibition of invasion and induction of apoptotic cell death of cancer cell lines by overexpression of TIMP-3. Br J Cancer 1999; 79: 13471355.
Spurbeck WW, Ng CY, Strom TS, et al. Enforced expression of tissue inhibitor of matrix metalloproteinase-3 affects functional capillary morphogenesis and inhibits tumor growth in a murine tumor model. Blood 2002; 100: 33613368.
Collen A, Hanemaaijer R, Lupu F, et al. Membrane-type matrix metalloproteinase-mediated angiogenesis in a fibrin–collagen matrix. Blood 2003; 101: 18101817.
Qi JH, Ebrahem Q, Moore N, et al. A novel function for tissue inhibitor of metalloproteinases-3 (TIMP3): inhibition of angiogenesis by blockage of VEGF binding to VEGF receptor-2. Nat Med 2003; 9: 407415.
Baker AH, Zaltsman AB, George SJ, Newby AC. Divergent effects of tissue inhibitor of metalloproteinase-1, -2, or -3 overexpression on rat vascular smooth muscle cell invasion, proliferation, and death in vitro. TIMP-3 promotes apoptosis. J Clin Invest 1998; 101: 14781487.
Smith MR, Kung H, Durum SK, et al. TIMP-3 induces cell death by stabilizing TNF-alpha receptors on the surface of human colon carcinoma cells. Cytokine 1997; 9: 770780.
Bond M, Murphy G, Bennett MR, et al. Tissue inhibitor of metalloproteinase-3 induces a Fas-associated death domain-dependent type II apoptotic pathway. J Biol Chem 2002; 277: 1378713795.
Fata JE, Leco KJ, Voura EB, et al. Accelerated apoptosis in the TIMP-3-deficient mammary gland. J Clin Invest 2001; 108: 831841.
Mohammed FF, Smookler DS, Taylor SE, et al. Abnormal TNF activity in TIMP3 – / – mice leads to chronic hepatic inflammation and failure of liver regeneration. Nat Genet 2004; 36: 969977.
Edwards DR. TIMP-3 and endocrine therapy of breast cancer: an apoptosis connection emerges. J Pathol 2004; 202: 391394.
Bisgaard HC, AR MacKayet al. “Spontaneous metastasis of rat liver epithelial cells transformed with v-raf and v-raf/v-myc: association with different phenotypic properties.” Invasion Metastasis 1997; 17(5): 24050.
Grana G. Shifting paradigms in hormonal therapy for breast cancer. Cancer Biol Ther 2004; 3(9): 797805.
Bachman KE, Herman JG, Corn PG, et al. Methylation-associated silencing of the tissue inhibitor of metalloproteinase-3 gene suggest a suppressor role in kidney, brain, and other human cancers. Cancer Res 1999; 59: 798802.
Kang SH, Choi HH, Kim SG, et al. Transcriptional inactivation of the tissue inhibitor of metalloproteinase-3 gene by DNA hypermethylation of the 5′-CpG island in human gastric cancer cell lines. Int J Cancer 2000; 86: 632635.
Ueki T, Toyota M, Sohn T, et al. Hypermethylation of multiple genes in pancreatic adenocarcinoma. Cancer Res 2000; 60: 18351839.
Wild A, Ramaswamy A, Langer P, et al. Frequent methylation-associated silencing of the tissue inhibitor of metalloproteinase-3 gene in pancreatic endocrine tumors. J Clin Endocrinol Metab 2003; 88: 13671373.
Zhao YG, Xiao AZ, Park HI, et al. Endometase/matrilysin-2 in human breast ductal carcinoma in situ and its inhibition by tissue inhibitors of metalloproteinases-2 and -4: a putative role in the initiation of breast cancer invasion. Cancer Res 2004; 64: 590598.
Wang M, Liu YE, Greene J, et al. Inhibition of tumor growth and metastasis of human breast cancer cells transfected with tissue inhibitor of metalloproteinase 4. Oncogene 1997; 14: 27672774.
Jiang Y, Wang M, Celiker MY, et al. Stimulation of mammary tumorigenesis by systemic tissue inhibitor of matrix metalloproteinase 4 gene delivery. Cancer Res 2001; 61: 23652370.
Schrohl AS, Holten-Andersen MN, Peters HA, et al. Tumor tissue levels of tissue inhibitor of metalloproteinase-1 as a prognostic marker in primary breast cancer. Clin Cancer Res 2004; 10: 22892298.
Schrohl AS, Christensen IJ, Pedersen AN, et al. Tumor tissue concentrations of the proteinase inhibitors tissue inhibitor of metalloproteinases-1 (TIMP-1) and plasminogen activator inhibitor type 1 (PAI-1) are complementary in determining prognosis in primary breast cancer. Mol Cell Proteom 2003; 2: 164172.
McCarthy K, Maguire T, McGreal G, et al. High levels of tissue inhibitor of metalloproteinase-1 predict poor outcome in patients with breast cancer. Int J Cancer 1999; 84: 4448.
Visscher DW, Hoyhtya M, Ottosen SK, et al. Enhanced expression of tissue inhibitor of metalloproteinase-2 (TIMP-2) in the stroma of breast carcinomas correlates with tumor recurrence. Int J Cancer 1994; 59: 339344.
Ree AH, Florenes VA, Berg JP, et al. High levels of messenger RNAs for tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2) in primary breast carcinomas are associated with development of distant metastases. Clin Cancer Res 1997; 3: 16231628.
Nakopoulou L, Giannopoulou I, Stefanaki K, et al. Enhanced mRNA expression of tissue inhibitor of metalloproteinase-1 (TIMP-1) in breast carcinomas is correlated with adverse prognosis. J Pathol 2002; 197: 307313.
Nakopoulou L, Giannopoulou I, Lazaris A, et al. The favorable prognostic impact of tissue inhibitor of matrix metalloproteinases-1 protein overexpression in breast cancer cells. APMIS 2003; 111: 10271036.
Farina AR, Tacconelli A, Cappabianca L, et al. Thioredoxin alters the matrix metalloproteinase/tissue inhibitors of metalloproteinase balance and stimulates human SK–N–SH neuroblastoma cell invasion. Eur J Biochem 2001; 268: 405413.
Jiang Y, Goldberg ID, Shi YE. Complex roles of tissue inhibitors of metalloproteinases in cancer. Oncogene 2002; 21: 22452252.
Aljada IS, Ramnath N, Donohue K, et al. Upregulation of the tissue inhibitor of metalloproteinase-1 protein is associated with progression of human non-small-cell lung cancer. J Clin Oncol 2004; 22: 32183229.
Holten-Andersen MN, Christensen IJ, Nielsen HJ, et al. Total levels of tissue inhibitor of metalloproteinases 1 in plasma yield high diagnostic sensitivity and specificity in patients with colon cancer. Clin Cancer Res 2002; 8: 156164.
Holten-Andersen MN, Christensen IJ, Nilbert M, et al. Association between preoperative plasma levels of tissue inhibitor of metalloproteinases 1 and rectal cancer patient survival: a validation study. Eur J Cancer 2004; 40: 6472.
Lijnen HR. Matrix metalloproteinases and cellular fibrinolytic activity. Biochemistry (Mosc) 2002; 67: 9298.
Orgel D, Schroder W, Hecker-Kia A, et al. The cleavage of pro-urokinase type plasminogen activator by stromelysin-1. Clin Chem Lab Med 1998; 36: 697702.
Patterson BC, Sang QA. Angiostatin-converting enzyme activities of human matrilysin (MMP-7) and gelatinase B/type IV collagenase (MMP-9). J Biol Chem 1997; 272: 2882328825.
O'Reilly MS, Wiederschain D, Stetler-Stevenson WG, et al. Regulation of angiostatin production by matrix metalloproteinase-2 in a model of concomitant resistance. J Biol Chem 1999; 274: 2956829571.
Farina AR, Tacconelli A, Cappabianca L, et al. Inhibition of human MDA-MB-231 breast cancer cell invasion by matrix metalloproteinase 3 involves degradation of plasminogen. Eur J Biochem 2002; 269: 44764483.
Deryugina EI, Luo GX, Reisfeld RA, et al. Tumor cell invasion through matrigel is regulated by activated matrix metalloproteinase-2. Anticancer Res 1997; 17: 32013210.
Shabani F, McNeil J, Tippett L. The oxidative inactivation of tissue inhibitor of metalloproteinase-1 (TIMP-1) by hypochlorous acid (HOCI) is suppressed by antirheumatic drugs. Free Radic Res 1998; 28: 115123.
Haklar G, Sayin-Ozveri E, Yuksel M, et al. Different kinds of reactive oxygen and nitrogen species were detected in colon and breast tumors. Cancer Lett 2001; 165: 219224.
Lincoln DT, Ali Emadi EM. Tonissen F, Clarke FM. The thioredoxin–thioredoxin reductase system: over-expression in human cancer. Anticancer Res 2003; 23: 24252433.
Gasson JC, Golde DW, Kaufman SE, et al. Molecular characterization and expression of the gene encoding human erythroid-potentiating activity. Nature 1985; 315: 768771.
Luparello C, Avanzato G, Carella C, Pucci-Minafra I. Tissue inhibitor of metalloprotease (TIMP)-1 and proliferative behaviour of clonal breast cancer cells. Breast Cancer Res Treat 1999; 54: 235244.
Yamashita K, Suzuki M, Iwata H, et al. Tyrosine phosphorylation is crucial for growth signaling by tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2). FASEB 1996; 396: 103107.
Liu XW, Bernardo MM, Fridman R, Kim HR. Tissue inhibitor of metalloproteinase-1 protects human breast epithelial cells against intrinsic apoptotic cell death via the focal adhesion kinase/phosphatidylinositol 3-kinase and MAPK signaling pathway. J Biol Chem 2003; 278: 4036440372.
Ritter LM, Garfield SH, Thorgeirsson UP. Tissue inhibitor of metalloproteinases-1 (TIMP-1) binds to the cell surface and translocates to the nucleus of human MCF-7 breast carcinoma cells. Biochem Biophys Res Commun 1999; 257: 494499.
Yamazaki M, Akahane T, Buck Tet al. Long-term exposure to elevated levels of circulating TIMP-1 but not mammary TIMP-1 suppresses growth of mammary carcinomas in transgenic mice. Carcinogenesis 2004; 25: 17351746.

Review of: Opposing roles for specific TIMPs in breast cancer prognosis

  • E. W. Thompson (a1) (a2) and A. R. Mackay (a3)

Metrics

Full text views

Total number of HTML views: 0
Total number of PDF views: 0 *
Loading metrics...

Abstract views

Total abstract views: 0 *
Loading metrics...

* Views captured on Cambridge Core between <date>. This data will be updated every 24 hours.

Usage data cannot currently be displayed