Serum matrix metalloproteinase-2 and its density in men with prostate cancer as a new predictor of disease extension

Gohji, Kazuo; Fujimoto, Noboru; Hara, Isao; Fujii, Akio; Gotoh, Akinobu; Okada, Hiroshi; Arakawa, Soichi; Kitazawa, Sohei; Miyake, Hideaki; Kamidono, Sadao; Nakajima, Motowo

doi:10.1002/(sici)1097-0215(19980220)79:1<96::aid-ijc18>3.0.co;2-f

Cited by 112 publications

(70 citation statements)

References 22 publications

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“…Many studies have demonstrated that MMPs correlate with cancer metastases. [5][6][7][8][9][10] Although MMP-2 and -9 were detected in tissues and cells of the prostate, 9 MMP-2 was also expressed in the stromal cells. 12 MMP-2 and -9 were thought to be the key matrix matalloproteinases involved in cancer cell invasion and metastases, since their overexpression could be induced by many factors such as cytokines, growth factors and oncogenes.…”

Section: Discussionmentioning

confidence: 99%

“…Elevated levels of MMP-2 and -9 in the plasma and urine have been correlated with metastasis in prostate cancer patients. 5,6 Secretion of MMP-2 and -9 induce tumor angiogenesis in prostate cancer cells. 7,8 Pettaway and colleagues found that the expression of MMP-2 and -9 mRNA, in comparison with E-cadherin expression, at biopsy could predict advanced prostate cancer at radical prostatectomy.…”

Section: Introductionmentioning

confidence: 99%

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Type IV collagenase (matrix metalloproteinase-2 and -9) in prostate cancer

Zhang

Shi

Feng

et al. 2004

Prostate Cancer Prostatic Dis

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Background: The type IV collagenases/gelatinases matrix metalloproteinase-2 (MMP-2) and -9 (MMP-9) play an important role in cancer invasion and metastasis. In the present study, we measured the expression of mRNAs and enzymatic activities of MMP-9 and -2 in prostate tissues and serum samples from men with or without prostate cancer. Methods: A total of 44 tissue samples (three from healthy volunteers, 21 from patients with benign prostate hyperplasia, 10 from patients with localized prostate cancer and 10 from patients with metastatic disease) and 71 serum samples were collected (20 from healthy volunteers, 26 from patients with benign prostatic hyperplasia, 10 from patients with localized cancer, 15 from patients with metastatic cancer). The level of mRNA for MMP-2 and -9 was determined by semiquantitative reverse transcriptase-polymerase chain reaction (RT-PCR). The enzymatic activity of MMPs was determined by zymography. Results: Expression of MMP-9 mRNA was significantly higher in malignant than in nonmalignant prostate tissues (Po0.001), while no significant difference of MMP-2 expression was detected in different prostate tissues. Results of zymography showed that there was significant difference in the enzymatic activity of MMP-9, but not MMP-2, among normal prostate, BPH, localized and metastatic prostate cancer tissues, serum samples (Po0.05). The active form of MMP-2, with a molecular mass of 62 kDa, was detected in normal prostate, BPH and prostate cancer tissues, but not in the serum samples. Moreover, there was a significant difference in the ratio of the active form (62 kDa) and proform (72 kDa) of MMP-2 among normal, BPH and prostate cancer tissues. This ratio was further increased in metastatic prostate cancer tissues. Conclusion: The activity of MMP-9 and the ratio of active form/proform of MMP-2 are associated with the progression and metastasis of prostate cancer.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Type IV collagenase (matrix metalloproteinase-2 and -9) in prostate cancer

Zhang

Shi

Feng

et al. 2004

Prostate Cancer Prostatic Dis

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“…67 In some studies, MMP determinations from patient serum have shown predictive value in estimation of metastasis risk. High serum levels of MMP-2 correlate with the presence of metastases in lung cancer 68 or to disease progression in patients with prostate cancer, 69 and a high serum MMP-9/E-cadherin ratio can predict metastasis of renal cell carcinoma. 70 …”

Section: Mmps As Predictors Of Recurrence or Metastasis Riskmentioning

confidence: 96%

Matrix metalloproteinases in cancer: Prognostic markers and therapeutic targets

Vihinen

Kähäri

2002

Intl Journal of Cancer

577

483

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Degradation of extracellular matrix is crucial for malignant tumour growth, invasion, metastasis and angiogenesis. Matrix metalloproteinases (MMPs) are a family of zinc-dependent neutral endopeptidases collectively capable of degrading essentially all matrix components. Elevated levels of distinct MMPs can be detected in tumour tissue or serum of patients with advanced cancer and their role as prognostic indicators in cancer is studied. In addition, therapeutic intervention of tumour growth and invasion based on inhibition of MMP activity is under intensive investigation and several MMP inhibitors are in clinical trials in cancer. In this review, we discuss the current view on the feasibility of MMPs as prognostic markers and as targets for therapeutic intervention in cancer.

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“…32 High MMP-2 and -9 levels in plasma also correlate with prostate cancer metastasis. [33][34][35] MMP-9 obviously contributes to metastasis, since inhibition of gelatinase reduces the migration and invasion of prostate cancer cells in mice. 36 CXCL12-stimulated bone marrow and peripheral blood CD34 þ cells secrete MMP-2 and MMP-9.…”

Section: Cxcr4-mediated Pca Migration and Invasionmentioning

confidence: 99%

CXCL12–CXCR4 interactions modulate prostate cancer cell migration, metalloproteinase expression and invasion

Singh

Grizzle

et al. 2004

Laboratory Investigation

208

186

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The mechanisms responsible for prostate cancer metastasis are incompletely understood at both the cellular and molecular levels. In this regard, chemokines are a family of small, cytokine-like proteins that induce motility of neoplastic cells, leukocytes and cancer cells. The current study evaluates the molecular mechanisms of CXCL12 and CXCR4 in prostate cancer cell migration and invasion. We report that functional CXCR4 is significantly expressed by prostate cancer cell lines, LNCaP and PC3, when compared with normal prostatic epithelial cells (PrEC). As measured using motility and invasion chamber assays, prostate cancer cells migrated and invaded through extracellular matrix components in response to CXCL12, at rates that corresponded to CXCR4 expression. Anti-CXCR4 antibodies (Abs) significantly impaired the migration and invasive potential of PC3 and LNCaP cells. CXCL12 induction also enhanced collagenase-1 (metalloproteinase-1 (MMP-1)) expression by LNCaP and PC3 cells. Collagenase-3 (MMP-13) was expressed by prostate cancer cells, but it was not expressed by PrEC cells or modulated by CXCL12. CXCL12 increased MMP-2 expression by LNCaP and PC3; however, MMP-9 expression was elevated only in PC3 cells after CXCL12-CXCR4 ligation. PC3 cells also expressed high levels of stromelysin-1 (MMP-3) after CXCL12 stimulation. CXCL12 also significantly Keywords: chemokine; metastasis; metalloproteinase; stromal cell-derived factor-1; SDF-1 Despite the obvious importance of metastasis, this process remains incompletely understood at both the cellular and molecular levels. 1 Many factors have been implicated in the process of metastasis, but the precise mechanisms for the directional migration of malignant cells into different organs is unknown. [2][3][4] In this regard, chemokines are a super family of small, cytokine-like proteins that inducethrough G-protein-coupled receptor and cytoskeletal rearrangement-the adhesion of neoplastic cells or leukocytes to endothelial cells as well as the directional migration of cancer cells. 5,6 The ability of neoplastic cells to penetrate the basement membrane and then invade the interstitial stroma to initiate the metastatic process is largely mediated by proteolysis. Many proteinases are capable of degrading extracellular matrix (ECM) components, but matrix metalloproteinases (MMPs) appear to be particularly important for matrix degradation. 6 These proteolytic enzymes are involved in connective tissue remodeling as well as in embryonic growth, ovulation, wound healing and menstruation. 7,8 Moreover, abnormal production of these proteinases is implicated in a number of pathological conditions. 9 It has been shown that CXCL12-CXCR4 interactions may play a role in the metastasis of prostate cancer to bone. 10 However, these interactions alone do not explain the metastasis pattern of prostate cancer or the potential for neoplastic prostate cells to migrate and invade other tissues. We have tested the hypothesis that prostate carcinomas use CXCR4-

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Serum matrix metalloproteinase-2 and its density in men with prostate cancer as a new predictor of disease extension

Cited by 112 publications

References 22 publications

Type IV collagenase (matrix metalloproteinase-2 and -9) in prostate cancer

Type IV collagenase (matrix metalloproteinase-2 and -9) in prostate cancer

Matrix metalloproteinases in cancer: Prognostic markers and therapeutic targets

CXCL12–CXCR4 interactions modulate prostate cancer cell migration, metalloproteinase expression and invasion

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