Plasma concentration of tissue inhibitor of matrix metalloproteinase 1 in patients with colorectal carcinoma

Yukawa, Norio; Yoshikawa, Takaki; Amaki, Makoto; Sugimasa, Yukio; Takemiya, Shoji; Yanoma, Shunsuke; Noguchi, Yoichiro; Takanashi, Yoshinori

doi:10.1046/j.0007-1323.2001.01930.x

Cited by 22 publications

(17 citation statements)

References 23 publications

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“…Langers et al (Langers et al, 2012) have found that high expression of MMP-2 and MMP-9 in the mucosa of colon cancer patients is associated with a 5-year mean survival (Grigioni et al, 1994;Sier et al, 1996). In this study, we found similar results regarding MMP-2 and MMP-9 expression in EGISTs, i.e., the expression of MMP-2 and MMP-9 was associated with tumor progression, which is consistent with previous findings (Grigioni et al, 1994;Sier et al, 1996;Zeng et al, 1996;Ring et al, 1997;Yukawa et al, 2001;Zhang et al, 2003;Liu et al, 2010;Langers et al, 2012). However, our current study did not show the underlying molecular mechanisms responsible for upregulation of MMP-2 and MMP-9 in EGISTs or how MMP-2 and MMP-9 proteins promote EGIST progression.…”

Section: Discussionsupporting

confidence: 82%

“…Additionally, MMP-9 mRNA expression and early recurrence and serious prognosis of colorectal cancer have been significantly linearly correlated (Zeng et al, 1996). Furthermore, the MMP-9 inhibitor TIMP-1 has been shown to be inversely associated with colon cancer progression (Yukawa et al, 2001). In addition, the overexpression of MMP-9 induces angiogenesis and enhances tumor growth by degrading the ECM and increasing the invasion and metastasis ability of tumor cells.…”

Section: Discussionmentioning

confidence: 95%

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Association of Matrix Metalloproteinase (MMP)-2 and -9 Expression with Extra-gastrointestinal Stromal Tumor Metastasis

Wang¹,

Ma²,

Jin³

et al. 2014

Asian Pacific Journal of Cancer Prevention

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Matrix metalloproteinase (MMP)-2 and MMP-9 are important proteases involved in invasion and metastasis of various tumors. Extra-gastrointestinal stromal tumors (EGISTs) are rare neoplasms. This study was performed to assess MMP-2 and MMP-9 expression in EGIST tissue samples for association with clinicopathological data from the patients. Twenty-one surgical EGIST tissue specimens were collected for analysis of MMP-2 and MMP-9 expression using immunohistochemistry. MMP-2 and MMP-9 proteins were expressed in all of the epithelial cell types of EGISTs, whereas they were only expressed in 75% of the spindle cell type, although there was no statistically significant difference (p>0.05). Expression of MMP-2 and MMP-9 proteins was associated with tumor size, mitotic rate, tumor necrosis, and distant metastasis (p<0.05). MMP-2 expression was linked with MMP-9 levels (p<0.05). However, there was no correlation between MMP-9 expression and age, sex, primary site, or cell morphology in any of these 21 EGIST patients (p>0.05). Moreover, expression of MMP-2 and MMP-9 proteins increased with the degree of EGIST risk. This study provided evidence of an association of MMP-2 and MMP-9 expression with advanced EGIST behavior.Keywords: Extra-gastrointestinal stromal tumor (EGIST) -MMP-2 -MMP-9 -tumor invasion and metastasis -biomarker

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Section: Discussionsupporting

confidence: 82%

Section: Discussionmentioning

confidence: 95%

Association of Matrix Metalloproteinase (MMP)-2 and -9 Expression with Extra-gastrointestinal Stromal Tumor Metastasis

Wang¹,

Ma²,

Jin³

et al. 2014

Asian Pacific Journal of Cancer Prevention

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“…Our study is the first to show that high TIMP-1 in HNSCC is not only associated with unfavorable cause-specific survival but also with an earlier relapse. These data are in line with those reporting high levels of tissue TIMP-1 to be related to disease progression in patients with breast or colorectal cancer (39,40). High preoperative TIMP-1 level was very recently found to correlate with a poor relapse-free survival in primary node -negative breast carcinoma (41).…”

Section: Discussionsupporting

confidence: 78%

Tissue Inhibitor of Matrix Metalloproteinase-1 Is Prognostic in Head and Neck Squamous Cell Carcinoma: Comparison of the Circulating and Tissue Immunoreactive Protein

Ruokolainen¹,

Pääkkö

Turpeenniemi‐Hujanen³

2005

Clinical Cancer Research

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Purpose:Tissue inhibitors of metalloproteinases (TIMP) are capable of inhibiting the matrix metalloproteinases, but they also possess other biological functions. Little is known about the role of TIMP-1in the progression and spreading of cancer cells among patients with head and neck squamous cell carcinoma (HNSCC). In this study, the pretreatment serum levels of TIMP-1or the overexpression of TIMP-1 immunoreactive protein in the primary tumor was correlated to the clinical course in patients with HNSCC. Experimental Design:TheTIMP-1immunoreactive protein was studied in 74 cases representing HNSCC. The tissue immunoreactive protein was evaluated from paraffin-embedded tumor sections in 68 cases using immunohistologic staining with a specific antibody, and in 68 cases the pretreatment serum levels of TIMP-1 were quantitatively measured by ELISA assay. The results were compared with the clinicopathologic factors of the disease and the patients'outcome. Results: A positive correlation was found between the size of the primary tumor (T) and the circulating TIMP-1 level (P = 0.021) or the positive immunoreaction of TIMP-1 in tumor (P = 0.039). The 5-year cause-specific survival was significantly lower in patients presenting with a high serum TIMP-1 level than in those with a low level of TIMP-1 (38% versus 64%, P = 0.034). They also had an unfavorable 5-year relapse-free survival rate (37% versus 56%, respectively). Similarly, the expression of TIMP-1 in tumor was prognostic for shortened survival, the 5-year cumulative relapse-free survival being 42% in patients with a TIMP-1^positive tumor versus 75% in cases with a negative tumor (P = 0.035). TissueTIMP-1positivity also seemed associated to the cause-specific survival (P = 0.075) and to be connected with later lymph node or hematogenic relapses. Conclusions:This study shows for the first time that both circulating and tissueTIMP-1 immunoreactive protein predicts the clinical course and dissemination in HNSCC, suggesting that TIMP-1 might be related to both tumor growth and metastasis in HNSCC.

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“…Marked overexpression of TIMP-1 or PAI-1 using recombinant adenoviral vectors in ECs does not block morphogenesis, but completely inhibits plasminogen/plasmin or plasma kallikrein-induced and MMP-dependent capillary tube regression. Furthermore, recent studies have indicated surprisingly high levels of TIMP-1 in the plasma of patients with a variety of cancers, including colon, gastric, breast, and lung cancer (Pellegrini et al, 2000;Yoshikawa et al, 2001;Yukawa et al, 2001). These data indicate that TIMP-1 and PAI-1, and perhaps other proteinase inhibitors synthesized by tumors, may block the vascular regression response to facilitate the maintenance of the tumor angiogenic vasculature.…”

Section: Capillary Tube Formation and Maintenance: A Balance Between mentioning

confidence: 89%

Molecular basis of endothelial cell morphogenesis in three‐dimensional extracellular matrices

2002

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Although many studies have focused on blood vessel development and new blood vessel formation associated with disease processes, the question of how endothelial cells (ECs) assemble into tubes in three dimensions (i.e., EC morphogenesis) remains unanswered. EC morphogenesis is particularly dependent on a signaling axis involving the extracellular matrix (ECM), integrins, and the cytoskeleton, which regulates EC shape changes and signals the pathways necessary for tube formation. Recent studies reveal that genes regulating this matrix-integrin-cytoskeletal (MIC) signaling axis are differentially expressed during EC morphogenesis. The Rho GTPases represent an important class of molecules involved in these events. Cdc42 and Rac1 are required for the process of EC intracellular vacuole formation and coalescence that regulates EC lumen formation in three-dimensional (3D) extracellular matrices, while RhoA appears to stabilize capillary tube networks. Once EC tube networks are established, supporting cells, such as pericytes, are recruited to further stabilize these networks, perhaps by regulating EC basement membrane matrix assembly. Furthermore, we consider recent work showing that EC morphogenesis is balanced by a tendency for newly formed tubes to regress. This morphogenesis-regression balance is controlled by differential gene expression of such molecules as VEGF, angiopoietin-2, and PAI-1, as well as a plasmin-and matrix metalloproteinase-dependent mechanism that induces tube regression through degradation of ECM scaffolds that support EC-lined tubes. It is our hope that this review will stimulate increased interest and effort focused on the basic mechanisms regulating capillary tube formation and regression in 3D extracellular matrices. Anat Rec 268: 252-275, 2002.

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Plasma concentration of tissue inhibitor of matrix metalloproteinase 1 in patients with colorectal carcinoma

Abstract: These data suggest that the plasma concentration of TIMP-1 correlates with both invasion and metastasis in patients with colorectal carcinoma.

Cited by 22 publications

References 23 publications

Association of Matrix Metalloproteinase (MMP)-2 and -9 Expression with Extra-gastrointestinal Stromal Tumor Metastasis

Association of Matrix Metalloproteinase (MMP)-2 and -9 Expression with Extra-gastrointestinal Stromal Tumor Metastasis

Tissue Inhibitor of Matrix Metalloproteinase-1 Is Prognostic in Head and Neck Squamous Cell Carcinoma: Comparison of the Circulating and Tissue Immunoreactive Protein

Molecular basis of endothelial cell morphogenesis in three‐dimensional extracellular matrices

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