Activation of human breast carcinoma collagenase through plasminogen activator

Paranjpe, Meera S.; Engel, Linda W.; Young, Nathaniel A.; Liotta, Lance A.

doi:10.1016/0024-3205(80)90067-3

Cited by 149 publications

(44 citation statements)

References 16 publications

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“…Plasmin has a relatively broad specificity, being able to degrade known extracellular matrix glycoproteins and to activate latent collagenase (52,54,60). The affinity of plasminogen and plasminogen activators for laminin (61), fibronectin (62), and fibrin (45) further suggests the importance of these proteinases in the turnover of matrix components.…”

Section: Abbreviations Used In This Papermentioning

confidence: 99%

Distinct localizations of urokinase-type plasminogen activator and its type 1 inhibitor under cultured human fibroblasts and sarcoma cells

Pöllänen¹,

Saksela²,

Salonen³

et al. 1987

The Journal of Cell Biology

296

127

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Abstract. We studied the immunocytochemical localization of urokinase-type plasminogen activator (u-PA) and the type 1 plasminogen activator inhibitor (PAI-1) in human fibroblasts and sarcoma cells, using both polyclonal and monoclonal antibodies. The u-PA was found to be located at discrete cell-substratum contact sites, and also at areas of cell-cell contacts, whereas PAI-1 was distributed as a homogenous carpet excluding strialike areas on the substrate under the cells. To confirm the extracellular localization of u-PA and PAIl, we stained the cells live at 0°C before fixation. A double-labeling experiment showed different distribution of u-PA and PAI-1 under the cells, and especially their peripheral parts. The staining pattern of u-PA and PAI-1 resisted treatment with 0.2% saponin followed by mechanical removal of cells, a method previously reported to isolate focal contact membranes of fibroblasts. We further demonstrated the deposition of u-PA to the contact areas of cells obtained by saponin treatment by zymography, and that of PAI-1 by metabolic labeling, reverse zymography, immunoblotting, and immunoprecipitation. Fibronectin was also present in the preparations. The deposition of both PAI-1 and fibronectin by the sarcoma cells was enhanced, after treating the cells with 10 -6 M dexamethasone. The confinement of u-PA to discrete contact sites and the more uniform distribution of PAI-1 on the cell substratum may explain how cells producing large amounts of enzyme inhibitors can produce PAmediated focal proteolysis.

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Section: Abbreviations Used In This Papermentioning

confidence: 99%

Distinct localizations of urokinase-type plasminogen activator and its type 1 inhibitor under cultured human fibroblasts and sarcoma cells

Pöllänen¹,

Saksela²,

Salonen³

et al. 1987

The Journal of Cell Biology

296

127

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“…Pro-uPA may be secreted by migrating or stromal cells in the environment of migrating cells and may be activated while bound to specific uPA receptors expressed on the cell surface of invading cells (15). uPA promotes the degradation of ECM proteins either acting alone or through activation of plasminogen to plasmin (6), which, in turn, may initiate an extracellular cascade leading to the activation of the pro-metalloproteinases (6,16,17). A possible role for CL in invasion and metastasis is supported by reports of a correlation between a high CL expression and high levels of invasion or metastasis in particular tumor types (reviewed by Gottesman and co-workers (7)).…”

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confidence: 99%

Characterization of Downstream Ras Signals That Induce Alternative Protease-dependent Invasive Phenotypes

Silberman¹,

Janulis

Schultz

1997

Journal of Biological Chemistry

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“…A number of investigators have suggested that a high activity of this enzyme in a tumour may destroy peritumoural tissues (Dano et al, 1985;Colombi et al, 1986). Plasmin degrades proteins of the extracellular tumour stroma and of the basement membrane (fibrin, fibronectin, laminin) (Duffy, 1987;Reich et al, 1988) and activates procollagenase IV, which degrades collagen (Paranjpe et al, 1980). This tumourassociated proteolysis provides the basis for tumour cell invasion and facilitates the release and subsequent metastasis of tumour cells.…”

mentioning

confidence: 99%

Breast cancer prognosis is poor when total plasminogen activator activity is low

Yamashita

Ogawa²,

Inada³

et al. 1993

Br J Cancer

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Summary Plasminogen activator (PA) is a serine protease which exists in two forms: tissue-type (t-PA) and urokinase-type (u-PA). The activity (<60 unitmg-' vs >,60 unitmg-' protein) was found to be a significant prognostic factor for disease-free and overall survival of about the same import as lymph node involvement. Furthermore, the combination of total PA activity and nodal status could be even more precise in predicting survival times and probabilities in individual patients. This retrospective study demonstrates the total PA activity is a valuable prognostic factor in determining prognosis in human breast cancer.

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Activation of human breast carcinoma collagenase through plasminogen activator

Cited by 149 publications

References 16 publications

Distinct localizations of urokinase-type plasminogen activator and its type 1 inhibitor under cultured human fibroblasts and sarcoma cells

Distinct localizations of urokinase-type plasminogen activator and its type 1 inhibitor under cultured human fibroblasts and sarcoma cells

Characterization of Downstream Ras Signals That Induce Alternative Protease-dependent Invasive Phenotypes

Breast cancer prognosis is poor when total plasminogen activator activity is low

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