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E Angles-Cano, A Balaton, B Le Bonniec, E Genot, J Elion and Y Sultan
Monoclonal antibodies (MAbs) to vascular plasminogen activator (vPA), the
tissue-type plasminogen activator (tPA) in human plasma, were produced to
be used as probes for immunochemical analysis. Human tissue sections and
one of these MAbs were used to demonstrate the endothelial origin of
plasma-tPA by immunohistochemistry. To produce MAbs, mice were immunized
with semipurified vPA isolated from postocclusion human venous blood.
Primed spleen cells were fused with the mouse myeloma cell line NS-1.
Screening for MAb-producing hybridomas was performed with postocclusion
euglobulins as a source of antigen by means of a solid-phase fibrin-vPA
immunoassay. The selective and high-affinity binding of vPA for fibrin
ensures the specificity and sensitivity of this test. Thus, eight
hybridomas secreting MAbs to vPA were selected, cloned, and established as
permanent hybridoma cell lines. Immunohistochemical analysis of cryostat
sections of human tissues was performed with EA-delta 12D, a MAb having no
inhibitory effect against vPA activity but binding to vPA with a high
affinity. Thus, the only structures immunostained were endothelial cells of
venules, capillaries, and arterioles. The EA-delta 12D monoclonal
localization of plasma vPA in the endothelial lining of blood vessels
provides evidence that tPA in plasma originates from the vascular wall and
validates its designation as vascular plasminogen activator, ie, vPA. Also,
our results are consistent with the fact that vPA in blood and tPA in
tissues are immunologically identical and have a common endothelial origin.
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| Copyright © 1985 by American Society of Hematology Online ISSN: 1528-0020 | |||||||||
