Biology and potential clinical implications of tissue inhibitor of metalloproteinases-1 in colorectal cancer treatment

References

• Kronborg O, Jørgensen OD, Fenger C, Rasmussen M. Randomized study of biennial screening with a faecal occult blood test: results after nine screening rounds. Scand J Gastroenterol 2004; 39: 846–51
   PubMed Web of Science ®Google Scholar
• Ouyang DL, Chen JJ, Getzenberg R H, Schoen RE. Noninvasive testing for colorectal cancer: a review. Am J Gastroenterol 2005; 100: 1393–403
   PubMed Web of Science ®Google Scholar
• Ransohoff DF. Colon cancer screening in 2005: status and challenges. Gastroenterology 2005; 128: 1685–95
   PubMed Web of Science ®Google Scholar
• Young GP, St John JB, Winawer SJ, Rozen P. Choice of fecal occult blood tests for colorectal cancer screening: recommendations based on performance characteristics in population studies – a WHO (World Health Organization) and OMED (World Organization for Digestive Endoscopy) report. Am J Gastroenterol 2002; 97: 2499–507
   PubMed Web of Science ®Google Scholar
• Collins JF, Lieberman DA, Durbin TE, Weiss DG. Accuracy of screening for fecal occult blood on a single stool sample obtained by digital rectal examination: a comparison with recommended sampling practice. Ann Intern Med 2005; 142: 81–5
   PubMed Web of Science ®Google Scholar
• Benson AB III, Schrag D, Somerfield MR, Cohen AM, Figueredo AT, Flynn PJ, et al. American Society of Clinical Oncology recommendations on Adjuvant chemotherapy for stage II colon cancer. J Clin Oncol 2004; 22: 3408–19
   PubMed Web of Science ®Google Scholar
• Dalgleish AG. Cancer vaccines. Br J Cancer 2000; 82: 1619–24
   PubMed Web of Science ®Google Scholar
• Harris JE, Ryan L, Hoover HC, Jr, Stuart RK, Oken MM, Benson AB III, et al. Adjuvant active specific immunotherapy for stage II and III colon cancer with an autologous tumor cell vaccine: Eastern Cooperative Oncology Group Study E5283. J Clin Oncol 2000; 18: 148–57
   PubMed Web of Science ®Google Scholar
• Geutskens SB, van der Eb MM, Plomp AC, Jonges LE, Cramer SJ, Ensink NG, et al. Recombinant adenoviral vectors have adjuvant activity and stimulate t cell responses against tumor cells. Gene Ther 2000; 7: 1410–6
   PubMed Web of Science ®Google Scholar
• Jedinak A, Maliar T. Inhibitors of proteases as anticancer drugs. Neoplasma 2005; 52: 185–92
   PubMed Web of Science ®Google Scholar
• Folkman J. Fighting cancer by attacking its blood supply. Sci Am 1996; 275: 150–4
   PubMed Web of Science ®Google Scholar
• Grothey A. Antiangiogenic therapy in cancer: a new era has begun. Oncology (Williston Park) 2005; 19(Suppl 3)5–6
   PubMed Web of Science ®Google Scholar
• Lykke J, Nielsen HJ. Haemostatic alterations in colorectal cancer: perspectives for future treatment. J Surg Oncol 2004; 88: 269–75
   PubMed Web of Science ®Google Scholar
• Vermorken JB. Adjuvant immunotherapy in colorectal cancer. Semin Oncol 2000; 27(Suppl 10)66–71
   PubMed Web of Science ®Google Scholar
• Nielsen H J, Christensen IJ, Moesgaard F, Kehlet H. Ranitidine as adjuvant treatment in colorectal cancer. Br J Surg 2002; 89: 1416–22
   PubMed Web of Science ®Google Scholar
• Ngan SYK, Fisher R, Burmeister BH, Mackay J, Goldstein D, Kneebone A, et al. Promising results of a cooperative group phase II trial of preoperative chemoradiation for locally advanced rectal cancer (TROG 9801). Dis Colon Rectum 2005; 48: 1389–96
   PubMed Web of Science ®Google Scholar
• Holten-Andersen MN, Murphy G, Nielsen HJ, Pedersen AN, Christensen IJ, Hoyer-Hansen G, et al. Quantitation of TIMP-1 in plasma of healthy blood donors and patients with advanced cancer. Br J Cancer 1999; 80: 495–503
   PubMed Web of Science ®Google Scholar
• Holten-Andersen MN, Stephens RW, Nielsen HJ, Murphy G, Christensen IJ, Stetler-Stevenson W., et al. High preoperative plasma tissue inhibitor of metalloproteinase-1 levels are associated with short survival of patients with colorectal cancer. Clin Cancer Res 2000; 6: 4292–9
   PubMed Web of Science ®Google Scholar
• Yukawa N, Yoshikawa T, Akaike M, Sugimusa Y, Takemiya S, Yanoma S, et al. Plasma concentration of tissue inhibitor of matrix metalloproteinase 1 in patients with colorectal carcinoma. Br J Surg 2001; 88: 1596–601
   PubMed Web of Science ®Google Scholar
• Simpson RA, Hemingway DM, Thompson MM. Plasma TIMP-1: a marker of metastasis in colorectal cancer. Colorectal Dis 2000; 2: 100–5
   PubMedGoogle Scholar
• Holten-Andersen MN, Christensen IJ, Nielsen HJ, Stephens RW, Jensen V, Nielsen OH, 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: 156–64
   PubMed Web of Science ®Google Scholar
• Holten-Andersen M, Christensen IJ, Nilbert M, Bendahl PO, Nielsen HJ, Brunner N, 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: 64–72
   PubMed Web of Science ®Google Scholar
• Yukawa N, Yoshikawa T, Akaike M, Sugimasa Y, Takemiya S, Yanoma S, et al. Prognostic impact of tissue inhibitor of matrix metalloproteinase-1 in plasma of patients with colorectal cancer. Anticancer Res 2004; 24: 2101–5
   PubMed Web of Science ®Google Scholar
• Waas ET, Hendriks T, Lomme RM, Wobbes T. Plasma levels of matrix metalloproteinase-2 and tissue inhibitor of metalloproteinase-1 correlate with disease stage and survival in colorectal cancer patients. Dis Colon Rectum 2005; 48: 700–10
   PubMed Web of Science ®Google Scholar
• Stricklin GP, Welgus HG. Human-skin fibroblast collagenase inhibitor: purification and biochemical-characterization. J Biol Chem 1983; 258: 12252–8
   PubMed Web of Science ®Google Scholar
• Murphy G, Houbrechts A, Cockett MI, Williamson RA, O'Shea M, Docherty AJP. The N-terminal domain of tissue inhibitor of metalloproteinases retains metalloproteinase inhibitory activity. Biochemistry 1991; 30: 8097–101
   PubMed Web of Science ®Google Scholar
• Carmichael DF, Sommer A, Thompson RC, Anderson DC, Smith CG, Welgus HG, et al. Primary structure and CDNA cloning of human fibroblast collagenase inhibitor. Proc Natl Acad Sci USA 1986; 83: 2407–11
   PubMed Web of Science ®Google Scholar
• Huebner K, Isobe M, Gasson JC, Golde DW, Croce CM. Localization of the gene encoding human erythroid-potentiating activity to chromosome region Xp11.1--Xp11.4. Am J Hum Genet 1986; 38: 819–26
   PubMed Web of Science ®Google Scholar
• Willard HF, Durfy SJ, Mahtani MM, Dorkins H, Davies KE, Williams BR. Regional localization of the TIMP gene on the human X chromosome. extension of a conserved synteny and linkage group on proximal Xp. Hum Genet 1989; 81: 234–8
   PubMed Web of Science ®Google Scholar
• Welgus HG, Stricklin GP. Human-skin fibroblast collagenase inhibitor: comparative studies in human connective tissues, serum, and amniotic fluid. J Biol Chem 1983; 258: 2259–64
   Web of Science ®Google Scholar
• Carmichael DF, Sommer A, Thompson RC, Anderson DC, Smith CG, Welgus HG, et al. Primary structure and CDNA cloning of human fibroblast collagenase inhibitor. Proc Natl Acad Sci USA 1986; 83: 2407–11
   PubMed Web of Science ®Google Scholar
• Welgus HG, Stricklin GP, Eisen AZ, Bauer EA, Cooney RV, Jeffrey JJ. Specific inhibitor of vertebrate collagenase produced by human-skin fibroblasts. J Biol Chem 1979; 254: 1938–43
   PubMed Web of Science ®Google Scholar
• Egeblad M, Werb Z. New functions for the matrix metalloproteinases in cancer progression. Nat Rev Cancer 2002; 2: 161–74
   PubMed Web of Science ®Google Scholar
• Chesler L, Golde DW, Bersch N, Johnson MD. Metalloproteinase inhibition and erythroid potentiation are independent activities of tissue inhibitor of metalloproteinases-1. Blood 1995; 86: 4506–15
   PubMed Web of Science ®Google Scholar
• Gomis-Ruth FX, Maskos K, Betz M, Bergner A, Huber R, Suzuki K, et al. Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1. Nature 1997; 389: 77–81
   PubMed Web of Science ®Google Scholar
• Khokha R, Waterhouse P. The role of tissue inhibitor of metalloproteinase-1 in specific aspects of cancer progression and reproduction. J Neurooncol 1994; 18: 123–7
   PubMed Web of Science ®Google Scholar
• Thorgeirsson UP, Lindsay CK, Cottam DW, Gomez DE. Tumor invasion, proteolysis, and angiogenesis. J Neurooncol 1994; 18: 89–103
   PubMed Web of Science ®Google Scholar
• Gomez DE, Alonso DF, Yoshiji H, Thorgeirsson UP. Tissue inhibitors of metalloproteinases: structure, regulation and biological functions. Eur J Cell Biol 1997; 74: 111–22
   PubMed Web of Science ®Google Scholar
• Madlener M. Differential expression of matrix metalloproteinases and their physiological inhibitors in acute murine skin wounds. Arch Dermatol Res 1998; 290: S24–9
   PubMed Web of Science ®Google Scholar
• Saarialho-Kere UK. Patterns of matrix metalloproteinase and TIMP expression in chronic ulcers. Arch Dermatol Res 1998; 290: S47–54
   PubMed Web of Science ®Google Scholar
• Hewitt RE, Brown KE, Corcoran M, Stetler-Stevenson WG. Increased expression of tissue inhibitor of metalloproteinases type I (TIMP-I) in a more tumorigenic colon cancer cell line. J Pathology 2000; 192: 455–9
   PubMed Web of Science ®Google Scholar
• Louis E, Ribbens C, Godon A, Franchimont D, De Groote D, Hardy N, et al. Increased production of matrix metalloproteinase-3 and tissue inhibitor of metalloproteinase-1 by inflamed mucosa in inflammatory bowel disease. Clin Exp Immunol 2000; 120: 241–6
   PubMed Web of Science ®Google Scholar
• Chromek M, Tullus K, Lundahl J, Brauner A. Tissue inhibitor of metalloproteinase 1 activates normal human granulocytes, protects them from apoptosis, and blocks their transmigration during inflammation. Infect Immun 2004; 72: 82–8
   PubMed Web of Science ®Google Scholar
• Avalos BR, Kaufman SE, Tomonaga M, Williams RE, Golde DW, Gasson JC. K562 cells produce and respond to human erythroid-potentiating activity. Blood 1988; 71: 1720–5
   PubMed Web of Science ®Google Scholar
• Bertaux B, Hornebeck W, Eisen AZ, Dubertret L. Growth-stimulation of human keratinocytes by tissue inhibitor of metalloproteinases. J Invest Dermatol 1991; 97: 679–85
   PubMed Web of Science ®Google Scholar
• Guedez L, Stetler-Stevenson WG, Wolff L, Wang J, Fukushima P, Mansoor A, et al. In vitro suppression of programmed cell death of B cells by tissue inhibitor of metalloproteinases-1. J Clin Invest 1998; 102: 2002–10
   PubMed Web of Science ®Google Scholar
• 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: 494–9
   PubMed Web of Science ®Google Scholar
• Chirco R, Liu XW, Jung KK, Kim HR. Novel functions of TIMPs in cell signaling. Cancer Metastasis Rev 2006; 25: 99–113
   PubMed Web of Science ®Google Scholar
• 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: 235–44
   PubMed Web of Science ®Google Scholar
• Hayakawa T, Yamashita K, Tanzawa K, Uchijima E, Iwata K. Growth-promoting activity of tissue inhibitor of metalloproteinases-1 (TIMP-1) for a wide range of cells. A possible new growth factor in serum. FEBS Lett;298:29–32.
   PubMed Web of Science ®Google Scholar
• Zhao WQ, Li H, Yamashita K, Guo XK, Hoshino T, Yoshida S, et al. Cell cycle-associated accumulation of tissue inhibitor of metalloproteinases-1 (TIMP-1) in the nuclei of human gingival fibroblasts. J Cell Sci 1998; 111: 1147–53
   PubMed Web of Science ®Google Scholar
• Wang T, Yamashita K, Iwata K, Hayakawa T. Both tissue inhibitors of metalloproteinases-1 (TIMP-1) and TIMP-2 activate ras but through different pathways. Biochem Biophys Res Commun 2002; 296: 201–5
   PubMed Web of Science ®Google Scholar
• Akahane T, Akahane M, Shah A, Thorgeirsson UP. TIMP-1 stimulates proliferation of human aortic smooth muscle cells and ras effector pathways. Biochem Biophys Res Commun 2004; 324: 440–5
   PubMed Web of Science ®Google Scholar
• Porter JF, Shen S, Denhardt DT. Tissue inhibitor of metalloproteinase-1 stimulates proliferation of human cancer cells by inhibiting a metalloproteinase. Br J Cancer 2004; 90: 463–70
   PubMed Web of Science ®Google Scholar
• Yamashita K, Suzuki M, Iwata H, Koike T, Hamaguchi M, Shinagawa A, et al. Tyrosine phosphorylation is crucial for growth signaling by tissue inhibitors of metalloproteinases (TIMP-1 and TIMP-2). FEBS Lett 1996; 396: 103–7
   PubMed Web of Science ®Google Scholar
• Soula-Rothhut M, Coissard C, Sartelet H, Boudot C, Bellon G, Martiny L, et al. The tumor suppressor PTEN inhibits EGF-induced TSP-1 and TIMP-1 expression in FTC-133 thyroid carcinoma cells. Exp Cell Res 2005; 304: 187–201
   PubMed Web of Science ®Google Scholar
• Hayakawa T, Yamashita K, Tanzawa K, Uchijima E, Iwata K. Growth-promoting activity of tissue inhibitor of metalloproteinases-1 (TIMP-1) for a wide range of cells. A possible new growth factor in serum. FEBS Lett 1992; 298: 29–32
   PubMed Web of Science ®Google Scholar
• O'Shea M, Willenbrock F, Williamson RA, Cockett MI, Freedman RB, Reynolds JJ, et al. Site-directed mutations that alter the inhibitory activity of the tissue inhibitor of metalloproteinases-1: importance of the N-terminal region between cysteine 3 and cysteine 13. Biochemistry 1992; 31: 10146–52
   PubMed Web of Science ®Google Scholar
• Fata JE, Leco KJ, Moorehead RA, Martin DC, Khokha R. Timp-1 is important for epithelial proliferation and branching morphogenesis during mouse mammary development. Dev Biol 1999; 211: 238–54
   PubMed Web of Science ®Google Scholar
• Fowlkes JL, Enghild JJ, Suzuki K, Nagase H. Matrix metalloproteinases degrade insulin-like growth factor-binding protein-3 in dermal fibroblast cultures. J Biol Chem 1994; 269: 25742–6
   PubMed Web of Science ®Google Scholar
• Gearing AJ, Beckett P, Christodoulou M, Churchill M, Clements JM, Crimmin M, et al. Matrix metalloproteinases and processing of pro-TNF-alpha. J Leukoc Biol 1995; 57: 774–7
   PubMed Web of Science ®Google Scholar
• Whitelock JM, Murdoch AD, Iozzo RV, Underwood PA. The degradation of human endothelial cell-derived perlecan and release of bound basic fibroblast growth factor by stromelysin, collagenase, plasmin, and heparanases. J Biol Chem 1996; 271: 10079–86
   PubMed Web of Science ®Google Scholar
• Fowlkes JL, Serra DM, Bunn RC, Thrailkill KM, Enghild JJ, Nagase H. Regulation of insulin-like growth factor (IGF)-I action by matrix metalloproteinase-3 involves selective disruption of IGF-I/IGF-binding protein-3 complexes. Endocrinology 2004; 145: 620–6
   PubMed Web of Science ®Google Scholar
• Murphy FR, Issa R, Zhou XY, Ratnarajah S, Nagase H, Arthur MJP, et al. Inhibition of apoptosis of activated hepatic stellate cells by tissue inhibitor of metalloproteinase-1 is mediated via effects on matrix metalloproteinase inhibition: implications for reversibility of liver fibrosis. J Biol Chem 2002; 277: 11069–76
   PubMed Web of Science ®Google Scholar
• Boudreau N, Sympson CJ, Werb Z, Bissell MJ. Suppression of ice and apoptosis in mammary epithelial-cells by extracellular-matrix. Science 1995; 267: 891–3
   PubMed Web of Science ®Google Scholar
• Murphy F, Waung J, Collins J, Arthur MJ, Nagase H, Mann D, et al. N-cadherin cleavage during activated hepatic stellate cell apoptosis is inhibited by tissue inhibitor of metalloproteinase-1. Comp Hepatol 2004; 3(Suppl 1)S8
   PubMedGoogle Scholar
• Alexander CM, Howard EW, Bissell MJ, Werb Z. Rescue of mammary epithelial cell apoptosis and entactin degradation by a tissue inhibitor of metalloproteinases-1 transgene. J Cell Biol 1996; 135: 1669–77
   PubMed Web of Science ®Google Scholar
• Li G, Fridman R, Kim HR. Tissue inhibitor of metalloproteinase-1 inhibits apoptosis of human breast epithelial cells. Cancer Res 1999; 59: 6267–75
   PubMed Web of Science ®Google Scholar
• Lambert E, Boudot C, Kadri Z, Soula-Rothhut M, Sowa ML, Mayeux P, et al. Tissue inhibitor of metalloproteinases-1 signalling pathway leading to erythroid cell survival. Biochem J 2003; 372: 767–74
   PubMed Web of Science ®Google Scholar
• Lee SJ, Yoo HJ, Bae YS, Kim HJ, Lee ST. TIMP-1 inhibits apoptosis in breast carcinoma cells via a pathway involving pertussis toxin-sensitive g protein and C-Src. Biochem Biophys Res Commun 2003; 312: 1196–201
   PubMed Web of Science ®Google Scholar
• Liu XW, Bernardo MM, Fridman R, Kim HRC. 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: 40364–72
   PubMed Web of Science ®Google Scholar
• Cornelius LA, Nehring LC, Harding E, Bolanowski M, Welgus HG, Kobayashi DK, et al. Matrix metalloproteinases generate angiostatin: effects on neovascularization. J Immunol 1998; 161: 6845–52
   PubMed Web of Science ®Google Scholar
• Wen W, Moses MA, Wiederschain D, Arbiser JL, Folkman J. The Generation of endostatin is mediated by elastase. Cancer Res 1999; 59: 6052–6
   PubMed Web of Science ®Google Scholar
• Yoshiji H, Harris SR, Raso E, Gomez DE, Lindsay CK, Shibuya M, et al. Mammary carcinoma cells over-expressing tissue inhibitor of metalloproteinases-1 show enhanced vascular endothelial growth factor expression. Int J f Cancer 1998; 75: 81–7
   PubMed Web of Science ®Google Scholar
• Guedez L, McMarlin AJ, Kingma DW, Bennett TA, Stetler-Stevenson M, Stetler-Stevenson WG. Tissue inhibitor of metalloproteinase-1 alters the tumorigenicity of Burkitt's lymphoma via divergent effects on tumor growth and angiogenesis. Am J Pathol 2001; 158: 1207–15
   PubMed Web of Science ®Google Scholar
• Reed MJ, Koike T, Sadoun E, Sage EH, Puolakkainen P. Inhibition of TIMP1 enhances angiogenesis in vivo and cell migration in vitro. Microvasc Res 2003; 65: 9–17
   PubMed Web of Science ®Google Scholar
• Zacchigna S, Zentilin L, Morini M, Dell'Eva R, Noonan DM, Albini A, et al. AAV-mediated gene transfer of tissue inhibitor of metalloproteinases-1 inhibits vascular tumor growth and angiogenesis in vivo. Cancer Gene Ther 2004; 11: 73–80
   PubMed Web of Science ®Google Scholar
• Fernandez HA, Kallenbach K, Seghezzi G, Grossi E, Colvin S, Schneider R, et al. Inhibition of endothelial cell migration by gene transfer of tissue inhibitor of metalloproteinases-1. J Surg Res 1999; 82: 156–62
   PubMed Web of Science ®Google Scholar
• Thorgeirsson UP, Yoshiji H, Sinha CC, Gomez DE. Breast cancer; tumor neovasculature and the effect of tissue inhibitor of metalloproteinases-1 (TIMP-1) on angiogenesis. In Vivo 1996; 10: 137–44
   PubMed Web of Science ®Google Scholar
• Akahane T, Akahane M, Shah A, Connor CM, Thorgeirsson UP. TIMP-1 inhibits microvascular endothelial cell migration by MMP-dependent and MMP-independent mechanisms. Exp Cell Res 2004; 301: 158–67
   PubMed Web of Science ®Google Scholar
• Ikenaka Y, Yoshiji H, Kuriyama S, Yoshii J, Noguchi R, Tsujinoue H, , et al. Tissue inhibitor of metalloproteinases-1 (TIMP-1) inhibits tumor growth and angiogenesis in the TIMP-1 transgenic mouse model. Int J Cancer;105:340–6.
   PubMed Web of Science ®Google Scholar
• Newell KJ, Witty JP, Rodgers WH, Matrisian LM. Expression and localization of matrix-degrading metalloproteinases during colorectal tumorigenesis. Mol Carcinog 1994; 10: 199–206
   PubMed Web of Science ®Google Scholar
• Zeng ZS, Guillem JG. Distinct pattern of matrix metalloproteinase 9 and tissue inhibitor of metalloproteinase 1 MRNA expression in human colorectal cancer and liver metastases. Br J Cancer 1995; 72: 575–82
   PubMed Web of Science ®Google Scholar
• Hewitt RE, Leach IH, Powe DG, Clark IM, Cawston TE, Turner DR. Distribution of collagenase and tissue inhibitor of metalloproteinases (TIMP) in colorectal tumours. Int J Cancer 1991; 49: 666–72
   PubMed Web of Science ®Google Scholar
• Tomita T, Iwata K. Matrix metalloproteinases and tissue inhibitors of metalloproteinases in colonic adenomas-adenocarcinomas. Dis Colon Rectum 1996; 39: 1255–64
   PubMed Web of Science ®Google Scholar
• Joo YE, Seo KS, Kim J, Kim HS, Rew JS, Park CS, et al. Role of tissue inhibitors of metalloproteinases (TIMPs) in colorectal carcinoma. J Korean Med Sci 1999; 14: 417–23
   PubMed Web of Science ®Google Scholar
• Holten-Andersen MN, Hansen U, Brunner N, Nielsen HJ, Illemann M, Nielsen BS. Localization of tissue inhibitor of metalloproteinases 1 (TIMP-1) in human colorectal adenoma and adenocarcinoma. Intl J Cancer 2005; 113: 198–206
   PubMed Web of Science ®Google Scholar
• Møller Sørensen N, Dowell BL, Stewart KD, Jensen V, Larsen L, Lademann U, et al. Establishment and characterization of 7 new monoclonal antibodies to tissue inhibitor of metalloproteinases-1. Tumour Biol 2005; 26: 71–80
   PubMedGoogle Scholar
• Holten-Andersen MN, Christensen IJ, Nielsen HJ, Lilja H, Murphy G, Jensen V, et al. Measurement of the Noncomplexed free fraction of tissue inhibitor of metalloproteinases I in plasma by immunoassay. Clin Chem 2002; 48: 1305–13
   PubMed Web of Science ®Google Scholar
• Tayebjee MH, Lip GYH, Blann AD, MacFadyen RJ. Effects of age, gender, ethnicity, diurnal variation and exercise on circulating levels of matrix metalloproteinases (MMP)-2 and-9, and their inhibitors, tissue inhibitors of matrix metalloproteinases (TIMP)-1 and-2. Thromb Res 2005; 115: 205–10
   PubMed Web of Science ®Google Scholar
• Cooper TW, Eisen AZ, Stricklin GP, Welgus HG. Platelet-derived collagenase inhibitor: characterization and subcellular localization. Proc Natl Acad Sci USA 1985; 82: 2779–83
   PubMed Web of Science ®Google Scholar
• Kodama S, Iwata K, Iwata H, Yamashita K, Hayakawa T. Rapid one-step sandwich enzyme-immunoassay for tissue inhibitor of metalloproteinases: an application for rheumatoid-arthritis serum and plasma. J Immunol Methods 1990; 127: 103–8
   PubMed Web of Science ®Google Scholar
• Plumpton TA, Clark IM, Plumpton C, Calvin J, Cawston TE. Development of an enzyme-linked-immunosorbent-assay to measure total TIMP-1 (free TIMP-1 and TIMP-1 in combination with matrix-metalloproteinases) and measurement of TIMP-1 and CRP in serum. Clin Chim Acta 1995; 240: 137–54
   PubMed Web of Science ®Google Scholar
• Jung K, Nowak L, Lein M, Henke W, Schnorr D, Loening SA. What kind of specimen should be selected for determining tissue inhibitor of metalloproteinase-1 (TIMP-1) in blood?. Clin Chim Acta 1996; 254: 97–100
   PubMed Web of Science ®Google Scholar
• Jung K, Meisser A, Bischof P. Blood sampling as critical preanalytical determinant to use circulating MMP and TIMP as surrogate markers for pathological processes. Int J Cancer 2005; 116: 1000–1
   PubMed Web of Science ®Google Scholar
• Holten-Andersen MN, Brunner N, Christensen IJ, Jensen V, Nielsen HJ. Levels of tissue inhibitor of metalloproteinases-1 in blood transfusion components. Scand J Clin Lab Invest 2002; 62: 223–30
   PubMed Web of Science ®Google Scholar
• Holten-Andersen MN, Schrohl AS, Brunner N, Nielsen HJ, Hogdall CK, Hogdall EV. Evaluation of sample handling in relation to levels of tissue inhibitor of metalloproteinases-1 measured in blood by immunoassay. Int J Biol Markers 2003; 18: 170–6
   PubMed Web of Science ®Google Scholar
• Cooksley S, Hipkiss JB, Tickle SP, Holmesievers E, Docherty AJP, Murphy G, et al. Immunoassays for the detection of human collagenase, stromelysin, tissue inhibitor of metalloproteinases (TIMP) and enzyme-inhibitor complexes. Matrix 1990; 10: 285–91
   PubMedGoogle Scholar
• Clark IM, Powell LK, Wright JK, Cawston TE. Polyclonal and monoclonal-antibodies against human tissue inhibitor of metalloproteinases (TIMP) and the design of an enzyme-linked-immunosorbent-assay to measure TIMP. Matrix 1991; 11: 76–85
   PubMedGoogle Scholar
• Lu XQ, Levy M, Weinstein IB, Santella RM. Immunological quantitation of levels of tissue inhibitor of metalloproteinase-1 in human colon cancer. Cancer Res;51:6231–5.
   PubMed Web of Science ®Google Scholar
• Jung K, Nowak L, Lein M, Henke W, Schnorr D, Loening SA. What kind of specimen should be selected for determining tissue inhibitor of metalloproteinase-1 (TIMP-1) in blood?. Clin Chim Acta 1996; 254: 97–100
   PubMed Web of Science ®Google Scholar
• Oberg A, Hoyhtya M, Tavelin B, Stenling R, Lindmark G. Limited value of preoperative serum analyses of matrix metalloproteinases (MMP-2, MMP-9) and tissue inhibitors of matrix metalloproteinases (TIMP-1, TIMP-2) in colorectal cancer. Anticancer Res 2000; 20: 1085–91
   PubMed Web of Science ®Google Scholar
• Wurtz SO, Christensen IJ, Schrohl AS, Mouridsen H, Lademann U, Jensen V, et al. Measurement of the uncomplexed fraction of tissue inhibitor of metalloproteinases-1 in the prognostic evaluation of primary breast cancer patients. Mol Cell Proteomics 2005; 4: 483–91
   PubMed Web of Science ®Google Scholar
• Fletcher RH. Carcinoembryonic antigen. Ann Intern Med 1986; 104: 66–73
   PubMed Web of Science ®Google Scholar
• Hammer JH, Basse L, Svendsen MN, Werther K, Brünner N, Christensen IJ, et al. Impact of elective resection on plasma TIMP-1 levels in patients with colon cancer. Colorectal Dis 2000; 8: 168–72
   Web of Science ®Google Scholar
• Holten-Andersen MN, Fenger C, Nielsen HJ, Rasmussen AS, Christensen IJ, Brunner N, et al. Plasma TIMP-1 in patients with colorectal adenomas: a prospective study. Eur J Cancer 2004; 40: 2159–64
   PubMed Web of Science ®Google Scholar
• Glowinska-Olszewska B, Urban M. Elevated matrix metalloproteinase 9 and tissue inhibitor of metalloproteinase 1 in obese children and adolescents. Metabolism 2007; 56: 799–805
   PubMed Web of Science ®Google Scholar
• Cavusoglu E, Ruwende C, Chopra V, Yanamadala S, Eng C, Clark LT, et al. Tissue inhibitor of metalloproteinase-1 (TIMP-1) is an independent predictor of all-cause mortality, cardiac mortality, and myocardial infarction. Am Heart J 2006; 151: 1101–8
   PubMed Web of Science ®Google Scholar
• Nielsen HJ, Brünner N, Frederiksen C. Plasma tissue inhibitor of metalloproteinases-1 (TIMP-1), a novel biological marker in the detection of primary colorectal cancer. Scand J Gastroenterol 2008:000–00.
   Web of Science ®Google Scholar
• Benson AB III, Desch CE, Flynn PJ, Krause C, Loprinzi CL, Minsky BD, et al. 2000 Update of American Society of Clinical Oncology Colorectal Cancer surveillance guidelines. J Clin Oncol 2000; 18: 3586–8
   PubMed Web of Science ®Google Scholar
• Duffy MJ, van Dalen A, Haglund C, Hansson L, Klapdor R, Lamerz R, et al. Clinical utility of biochemical markers in colorectal cancer: European Group on Tumour Markers (EGTM) guidelines. Eur J Cancer 2003; 39: 718–27
   PubMed Web of Science ®Google Scholar
• Goldstein MJ, Mitchell EP. Carcinoembryonic antigen in the staging and follow-up of patients with colorectal cancer. Cancer Invest 2005; 23: 338–51
   PubMed Web of Science ®Google Scholar
• Holten-Andersen MN, Nielsen HJ, Sørensen S, Brünner N, Murphy G, Jensen V, et al. Predicting minimal residual disease during follow-up of colorectal cancer patients by measurement of tissue inhibitor of metalloproteinases-1 in plasma. Int J Biol Markers 2002; 17: 35–6
   Google Scholar
• Holten-Andersen MN, Nielsen HJ, Sorensen S, Jensen V, Brunner N, Christensen IJ. Tissue inhibitor of metalloproteinases-1 in the postoperative monitoring of colorectal cancer. Eur J Cancer 2006; 42: 1889–96
   PubMed Web of Science ®Google Scholar
• Yoshikawa T, Tsuburaya A, Kobayashi O, Sairenji M, Motohashi H, Yanoma S, et al. Prognostic value of tissue inhibitor of matrix metalloproteinase-1 in plasma of patients with gastric cancer. Cancer Lett 2000; 151: 81–6
   PubMed Web of Science ®Google Scholar
• Joo YE, Seo KS, Kim HS, Rew JS, Park CS, Kim SJ. Expression of tissue inhibitors of metalloproteinases (TIMPs) in gastric cancer. Dig Dis Sci 2000; 45: 114–21
   PubMed Web of Science ®Google Scholar
• Yoshikawa T, Tsuburaya A, Kobayashi O, Sairenji M, Motohashi H, Yanoma S, et al. Intratumoral concentrations of tissue inhibitor of matrix metalloproteinase 1 in patients with gastric carcinoma: a new biomarker for invasion and its impact on survival. Cancer 2001; 91: 1739–44
   PubMed Web of Science ®Google Scholar
• Mimori K, Mori M, Shiraishi T, Fujie T, Baba K, Haraguchi M, et al. Clinical significance of tissue inhibitor of metalloproteinase expression in gastric carcinoma. Br J Cancer 1997; 76: 531–6
   PubMed Web of Science ®Google Scholar
• Fong KM, Kida Y, Zimmerman PV, Smith PJ. TIMP1 and adverse prognosis in non-small cell lung cancer. Clin Cancer Res 1996; 2: 1369–72
   PubMed Web of Science ®Google Scholar
• Gouyer V, Conti M, Devos P, Zerimech F, Copin MC, Creme E, et al. Tissue Inhibitor of metalloproteinase 1 is an independent predictor of prognosis in patients with nonsmall cell lung carcinoma who undergo resection with curative intent. Cancer 2005; 103: 1676–84
   PubMed Web of Science ®Google Scholar
• Ylisirnio S, Hoyhtya M, Turpeenniemi-Hujanen T. Serum matrix metalloproteinases -2, -9 and tissue inhibitors of metalloproteinases -1, -2 in lung cancer–TIMP-1 as a prognostic marker. Anticancer Res 2000; 20: 1311–6
   PubMed Web of Science ®Google Scholar
• Ylisirnio S, Hoyhtya M, Makitaro R, Paaakko P, Risteli J, Kinnula VL, et al. Elevated serum levels of type I collagen degradation marker ICTP and tissue inhibitor of metalloproteinase (TIMP) 1 are associated with poor prognosis in lung cancer. Clin Cancer Res 2001; 7: 1633–7
   PubMed Web of Science ®Google Scholar
• Aljada IS, Ramnath N, Donohue K, Harvey S, Brooks JJ, Wiseman SM, 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: 3218–29
   PubMed Web of Science ®Google Scholar
• Suemitsu R, Yoshino I, Tomiyasu M, Fukuyama S, Okamoto T, Maehara Y. Serum tissue inhibitors of metalloproteinase-1 and -2 in patients with non-small cell lung cancer. Surg Today 2004; 34: 896–901
   PubMed Web of Science ®Google Scholar
• Ree AH, Florenes VA, Berg JP, Maelandsmo GM, Nesland JM, Fodstad O. 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: 1623–8
   PubMed Web of Science ®Google Scholar
• Nakopoulou L, Giannopoulou I, Stefanaki K, Panayotopoulou E, Tsirmpa I, Alexandrou P, 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: 307–13
   PubMed Web of Science ®Google Scholar
• McCarthy K, Maguire T, McGreal G, McDermott E, O'Higgins N, Duffy MJ. High levels of tissue inhibitor of metalloproteinase-1 predict poor outcome in patients with breast cancer. Int J Cancer 1999; 84: 44–8
   PubMed Web of Science ®Google Scholar
• Schrohl AS, Christensen IJ, Pedersen AN, Jensen V, Mouridsen H, Murphy G, 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 Proteomics 2003; 2: 164–72
   PubMed Web of Science ®Google Scholar
• Schrohl AS, Holten-Andersen MN, Peters HA, Look MP, Meijer-van Gelder ME, Klijn JGM, et al. Tumor tissue levels of tissue inhibitor of metalloproteinase-1 as a prognostic marker in primary breast cancer. Clin Cancer Res 2004; 10: 2289–98
   PubMed Web of Science ®Google Scholar
• Nakopoulou L, Giannopoulou I, Lazaris AC, Alexandrou P, Tsirmpa I, Markaki S, et al. The favorable prognostic impact of tissue inhibitor of matrix metalloproteinases-1 protein overexpression in breast cancer cells. APMIS 2003; 111: 1027–36
   PubMed Web of Science ®Google Scholar
• Hayes DF, Bast RC, Desch CE, Fritsche H, Jr, Kemeny NE, Jessup JM, et al. Tumor marker utility grading system: a framework to evaluate clinical utility of tumor markers. J Natl Cancer Inst 1996; 88: 1456–66
   PubMed Web of Science ®Google Scholar
• Schrohl AS, Meijer-van Gelder ME, Holten-Andersen MN, Christensen IJ, Look MP, Mouridsen HT, et al. Primary tumor levels of tissue inhibitor of metalloproteinases-1 are predictive of resistance to chemotherapy in patients with metastatic breast cancer. Clin Cancer Res 2006; 12: 7054–8
   PubMed Web of Science ®Google Scholar
• Sørensen NM, Bystrom P, Christensen IJ, Berglund A, Nielsen HJ, Brunner N, et al. TIMP-1 Is significantly associated with objective response and survival in metastatic colorectal cancer patients receiving combination of irinotecan, 5-fluorouracil, and folinic acid. Clin Cancer Res 2007; 13: 4117–22
   PubMed Web of Science ®Google Scholar