Matrix metalloproteinases and tumor invasion: from correlation and causality to the clinic

Stetler-Stevenson, William G.; Hewitt, Robert E.; Corcoran, Marta L.

doi:10.1006/scbi.1996.0020

Cited by 322 publications

(203 citation statements)

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“…2,56 -58 The role of MMPs and their inhibitors in cancer progression has been extensively studied. 7,22,59 In prostate cancer tissues, increasing expression of MMPs-1, 24,25 -2, 26 -32 -3, 24,29 -7 33 and -9 27,34 has been associated with increasing cancer burden. However, these studies did not distinguish between expression by stromal or epithelial cells that may interact to cause cancer progression.…”

Section: Discussionmentioning

confidence: 99%

Characterization of expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases in prostate cancer cell lines

Daja

Niu

Zhao

et al. 2003

Prostate Cancer Prostatic Dis

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Stromal expression of some matrix metalloproteinases (MMPs) has been associated with increasing tumour burden in prostate cancer. We investigated the expression of mRNA (by RT-PCR) and protein (by zymography and western blotting) of MMPs and endogenous inhibitors (tissue inhibitors of metalloproteinases, TIMPs) in two parent epithelial prostate cancer cell lines and sublines of increasing invasive/metastatic potential. Expression of membrane type MMPs, MT1-MMP and MT3-MMP mRNA was higher in PC3-derived than in LNCaPderived lines, whereas MT2-MMP mRNA expression was higher in the LNCaPderived than in PC3-derived cell lines. Active MT1, MT2 and MT3-MMP protein levels were similar in all lines, but processed MT-MMPs, indicative of latent MMP activation, were increased in more aggressive sublines. Expression of MMP-1, MMP-13 and TIMP-1 was higher in the more aggressive sublines and may be implicated in invasive/metastatic ability. Regulation of MMP-1 and MMP-13 expression may offer important therapeutic options for treating patients with prostate cancer.

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Section: Discussionmentioning

confidence: 99%

Characterization of expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases in prostate cancer cell lines

Daja

Niu

Zhao

et al. 2003

Prostate Cancer Prostatic Dis

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“…These proteases belong to the plasminogen activator (PA) or to the matrix metalloproteinase (MMP) superfamilies. Increased expression of PA and MMPs in a variety of tumours, including breast cancer, are associated with a high metastatic potential and poor prognosis (Stetler Stevenson et al, 1996;Duffy et al, 1998). Invasive cells form specialized membrane protrusions, called invadopodia, that actively degrade the surrounding ECM (Kelly et al, 1994).…”

Section: H Thornton and M Baummentioning

confidence: 99%

Mammographic compression: a force to be reckoned with

1999

Br J Cancer

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“…Among these enzymes, urokinase and a variety of matrix matalloprotienases (MMPs) play important roles. [1][2][3][4] Among different MMPs, MMP-2 (or gelatinase A) and MMP-9 (or gelatinase B) collectively referred to as type IV collagenases or gelatinases, have been found to be specifically associated with prostate cancer metastasis. Elevated levels of MMP-2 and -9 in the plasma and urine have been correlated with metastasis in prostate cancer patients.…”

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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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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Matrix metalloproteinases and tumor invasion: from correlation and causality to the clinic

Cited by 322 publications

References 0 publications

Characterization of expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases in prostate cancer cell lines

Characterization of expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases in prostate cancer cell lines

Mammographic compression: a force to be reckoned with

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

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