Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound   Target Concepts: Gene/Protein Disease Symptom Drug Enzyme Compound

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Query: EC:3.4.21.7 (plasmin)
9,023 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Physiological concentrations of dihydrotestosterone (DHT) can specifically induce the release of fibrinolysin from androgen-dependent mammary carcinoma (Shionogi SC-115) cells in vitro. No fibrinolytic activity was observed in cells cultured either in the absence of DHT or presence of pharmacological concentrations of estrogen. Furthermore, an autonomous tumor derived from the Shionogi SC-115 cells produced fibrinolytic activity independent of added DHT or estrogen. These observations suggest a close correlation between fibrinolytic activity of a tumor and its ability to grow in vivo.
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PMID:Androgen-dependent fibrinolytic activity in a murine mammary carcinoma (Shionogi SC-115 cells) in vitro. 13 60

Three human bladder carcinoma cell lines, T 24, RT 4, and MANO, a human bladder nonmalignant epithelial cell line, HCV-29, and a human lung fibroblast line, 460 H1, were investigated for their ability to induce fibrinolytic, urokinase and plasmin inhibitory activities in cell culture, using serum-free medium, for up to 36 h. Generally, the non-malignant cell line and the fibroblast line had a greater ability to produce urokinase inhibitor than did the malignant cell lines. The amount produced varied greatly between cells and over the study period. A low concentration of plasminogen activator, immunologically identical with urokinase, and its accumulation in culture supernate were found with RT 4 after 12 h and 24 h cultivations, whereas no plasminogen activator was detected in all other cell lines for periods up to 36 h. No plasmin, non-specific protease or plasmin inhibitory activities were detected in any of the supernates from the cell lines.
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PMID:Fibrinolytic activity of in vitro cultivated human bladder cell lines. 14 45

It's well known that increased proteolytic activity in plasma as well as in interstitial fluids is often associated with malignant tumours. There are numerous reports that cell cultures of malignant origin contain plasminogen activators responsible for an increased proteolysis. Our studies showed that patients with a carcinoma excrete in their urine a significant higher amount of an acid-stable inhibitor than healthy patients. This urine inhibitor is a split product (MW: 30,000) of the Inter-alpha-trypsin inhibitor (MW: 180,000). We conclude that the increased amount of acid-stable split products is the result of increased proteolysis in patients with malignant tumours. In contrast to other authors we do not think that the activation of plasmin by plasminogen is responsible for the proteolytic cleavage of ITI. Otherwise proteolysis by Cathepsin G and granulocytic Elastase would be reasonable. So enhanced proteolysis seems to be a sign of general enzymatic change associated with transformation.
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PMID:[Studies for proteolysis in malignant tumours (author's transl)]. 31 47

Thromboplastic and fibrinolytic activities of V2 and V7 carcinomas, the two transplantable rabbit tumors of the same viral origin, were studied in relation to fibrin deposition and thrombus formation in the tumors. Thromboplastic activity of V7 carcinoma was comparatively high, while that of V2 carcinoma was as low as that of muscle tissue. More fibrin deposits in the stroma and more thrombi in the small vessels were found at the advancing border of V7 carcinoma than that of V2 carcinoma. These differences might be associated with higher thromboplastic activity of V7 carcinoma than that of V2 carcinoma. Fibrinolytic activity of both tumors was high and it was confirmed to be localized in the tumor cells by Todd's method. Fibrin deposits in the stroma were found more abundantly somewhat apart from the advancing border of the tumor nests of both tumors. It was suggested that plasmin activated by plasminogen activator released locally from the tumor cells might digest fibrin deposited in the stroma just close to the tumor nests.
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PMID:Thromboplastic and fibrinolytic activities of V2 and V7 carcinomas of rabbit, with special reference to fibrin deposition and thrombus formation in the tumors. 67 49

In order to visualize the receptor for plasmin and plasminogen present on human carcinoma cells, SW1116 and MCF7-MF cells were incubated with biotinylated plasminogen or plasmin and fluoresceinated streptavidin, and counterstained with propidium iodide. It was first demonstrated that biotinylation did not alter the binding properties of plasminogen and plasmin, provided that the biotinylation rate was around 2. Specific staining of tumor cells was obtained using these reagents. Images with green fluorescence were clearly visible as grains or contours at the surface of tumor cells. The localization of fluorescent grains was analyzed more precisely using confocal microscopy. The percentage of stained cells varied from one experiment to another between 10 and 60%. In no experiment were all the cells observed to be positive. Mitotic cells were more frequently stained than non-mitotic cells, suggesting a relationship between the presence of plasmin receptors and cell proliferation. This was confirmed by the use of Ki67 monoclonal antibody (MAb), as B-Pg-binding tumor cells generally had their nucleus stained by this antibody. Other images indicated staining of the extracellular matrix. Finally, 2 rat tumor-cell sub-lines of colonic origin (DHD K12 Pro-b and Reg-b) were shown to bind human biotinylated plasminogen, confirming the strong interspecies reactivity of plasmin receptors.
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PMID:Visualization of the plasmin receptor on carcinoma cells. 131 64

Cells from rat carcinoma cell lines PROb (giving progressive tumours) and REGb (giving regressive tumours) have cell surface receptors which bind specifically rat plasminogen and plasmin. Affinity for Pg was found to be higher in PROb (Kd = 10(-7) M) than in REGb cells (Kd = 5.10(-7) M) but with a concomitant decrease in the number of binding sites, 0.9 x 10(6)/cell (range from 0.6 to 1.2 x 10(6)) in PROb vs 3.6 x 10(6)/cell (range 1.2 to 6 x 10(6)) in REGb cells. The number and the affinity of binding sites varied in an opposite way in PROb and REGb cells. The difference in affinity parameters was unrelated to the degree of invasiveness of tumour cells in syngenetic rats. Bound plasmin retained its enzymatic activity, which indicates that its binding does not involve the catalytic active site. In cell solubilisates plasminogen receptor appeared as one major band situated in the area of 50-60 kDa.
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PMID:Plasminogen receptors on rat colon carcinoma cells. 132 56

We have screened six human squamous carcinoma cell lines for their ability to invade connective tissue by using the experimentally modified chorioallantoic membrane of a chick embryo as an in vivo model of invasion. In confirmation of our earlier studies, all the invasive cell lines expressed high levels of surface-bound urokinase type plasminogen activator (uPA). However, some cell lines expressing this activity were not invasive, suggesting that surface uPA, although necessary, was not sufficient. Since in addition to fibronectin, that can be degraded by uPA or plasmin, chorioallantoic membrane connective tissue contains collagen, we examined the profile of collagenases secreted by the various cell lines in search for an activity that would coincide with the invasive phenotype. We found, using gelatin substrate gels, that type IV gelatinase was produced by all six cell types tested, three cell types produced the M(r) 92,000 gelatinase, and three a lower-molecular-weight activity, which we identified by immunoprecipitation with specific antibodies, and by a direct assay of activity, as interstitial collagenase. Only the latter cells were found to be highly invasive. We showed previously that continuous culture in vitro of one of the carcinoma cell lines, HEp3, led to a gradual extinction of their malignant phenotype. To confirm the correlation between invasion and the production of interstitial collagenase, we examined these two functions in cells freshly isolated from a HEp3 tumor and intermittently during passage in vitro. We found that, although the surface uPA activity was slightly diminished in the in vitro grown cultures, it was still within the range of values found in highly malignant cells, suggesting that it is not the reason for the decrease in invasiveness. In contrast, the reduction in interstitial collagenase closely followed the loss of the invasive phenotype; after 30 in vitro passages the cells were almost completely devoid of interstitial collagenase and unable to invade. The decrease in collagenase activity was not the result of an increased tissue inhibitor of metalloproteinases production.
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PMID:Invasion of connective tissue by human carcinoma cell lines: requirement for urokinase, urokinase receptor, and interstitial collagenase. 133 82

Proteinase species secreted by 10 human gastric carcinoma cell lines were analyzed by gelatin zymography and immunoblotting. These cell lines were classified into the following three groups with respect to proteinase secretion: cell lines secreting mainly gelatinases A and/or B; those secreting multiple types of serine proteinases; and those scarcely secreting these enzymes. Two cell lines of the second group, STKM-1 and MKN28, hardly secreted metalloproteinases but secreted the following four types of serine proteinases: (a) two trypsin-like enzymes (M(r) 26,000 and 24,000 in proenzyme forms); (b) a tissue kallikrein-like enzyme (M(r) 150,000 in a complex form); (c) a plasmin-like enzyme (M(r) 70,000); and (d) a plasminogen activator (urokinase-type, M(r) 57,000, from STKM-1 and tissue-type, M(r) 70,000, from MKN28). The M(r) 70,000 plasmin-like enzyme was also detected at lower levels in the conditioned media of four other cell lines (MKN1, MKN45, NUGC-3, and KATO III). The M(r) 24,000 proenzyme of the trypsin-like enzyme was purified from the serum-free conditioned medium of STKM-1. The proenzyme was activated by enterokinase treatment or autolytically by incubation at neutral pH, decreasing its apparent molecular weight from 24,000 to 23,000 on nonreducing sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The activated enzyme extensively degraded fibronectin, laminin, and gelatins and to lesser extents type I, III, IV, and V collagens at 30 degrees C. These results suggest that the matrix serine proteinases may play a major role in the matrix degradation by some kinds of human cancer cells.
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PMID:Multiple secretion of matrix serine proteinases by human gastric carcinoma cell lines. 138 87

Addition of purified plasmin or plasminogen (0.1 microM) to serum-free culture media elevated cellular D-myo-inositol 1,4,5-trisphosphate (InsP3) levels in human colorectal carcinoma cells within 1 h to double those of control cells. This was accompanied by decreases in cellular phosphatidylinositol bisphosphate by 40% in cells exposed to fibrinolytic ligands for up to 1 h. The effect was not due to opening of Ca2+ channels of the type blocked by 5 microM nifedipine, and 100 microM EGTA, a Ca2+ chelator, did not suppress plasmin's ability to elevate InsP3. Binding assays at 4 degrees C with 125I-labelled plasmin indicated maximum binding within 1 h suggesting that the effects of plasmin may be associated with its cell-binding function. These cells could convert exogenous plasminogen to plasmin with endogenous activation and this was accompanied by a decrease in radioactive phosphatidylinositol well below control levels (13% of control). Our results contribute to evidence for the association of plasmin-binding sites with a signalling system. A cell signalling system indirectly or directly associated with plasmin binding, would permit carcinoma cells to coordinate extracellular fibrinolysis with cell migration and motility through second messengers.
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PMID:Cell signalling associated with fibrinolytic ligand binding to human colorectal carcinoma cells. 164 62

We have previously demonstrated the existence of a receptor for plasmin and plasminogen on carcinoma cells, either from human or rat origin. We show here that these receptors have a strong interspecific reactivity. This conclusion is based on binding assay of 125I labelled plasminogens and fluorescence experiments using biotinylated human plasminogen. In all these experiments cells from one species could bind plasminogen from the other species and interspecific inhibition was observed as well.
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PMID:A receptor for plasminogen and plasmin on human and rat carcinoma cells. Evidence for strong interspecific reactivity. 166 26


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