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Visualization of the plasmin receptor on carcinoma cells
Author(s) -
Correc P.,
Zhang S.,
Komano O.,
Laurent M.,
Burtin P.
Publication year - 1992
Publication title -
international journal of cancer
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.475
H-Index - 234
eISSN - 1097-0215
pISSN - 0020-7136
DOI - 10.1002/ijc.2910500517
Subject(s) - plasmin , biotinylation , microbiology and biotechnology , propidium iodide , receptor , cancer cell , biology , chemistry , biochemistry , cancer , apoptosis , enzyme , genetics , programmed cell death
In order to visualize the receptor for plasmin and plasminogen present on human carcinoma cells, SWI116 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.