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saponaria pumila/lymphoma

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Activity of a monoclonal antibody-saporin-6 conjugate against B-lymphoma cells.

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A monoclonal antibody reactive with the immunoglobulin heavy chain (TEC IgM) has been conjugated to saporin-6 (SAP), which is the major ribosome-inactivating protein from the seeds of the plant Saponaria officinalis. Studies with Burkitt's lymphoma cell line Bjab 113 demonstrate that this

Recognition and killing of tumour cells expressing heat shock protein 65 kD with immunotoxins containing saporin.

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The expression of heat shock proteins (HSP) of the 65 kD family (groEL) has been observed by flow cytometry using murine monoclonal antibody (MoAb) anti-HSP 65 kD (ML30) on the surface of B (Daudi) or T (H9) lymphoma cells, on a monocyte cell line (U937) and also on a primary culture of a human

B-cell restricted saporin immunotoxins: activity against B-cell lines and chronic lymphocytic leukemia cells.

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B cell-restricted immunotoxins were constructed by conjugating anti-B monoclonal antibodies to saporin, the major ribosome inactivating protein from the seeds of the plant Saponaria officinalis. HD37-SAP is directed against CD19, the broadest B cell-specific determinant. HD39-SAP and HD6-SAP
The ribosome-inactivating protein saporin, from Saponaria officinalis, was coupled by a disulfide bond to monoclonal anti-Thy 1.1 antibody (OX7) and to its F(ab')2 fragment. The immunotoxins were at least as toxic as the plant toxin ricin to the Thy 1.1-expressing cell lines AKR-A and BW5147 in

Saponins from Saponaria officinalis L. Augment the Efficacy of a Rituximab-Immunotoxin.

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Triterpenoidal saponins are synthesized in the roots of Saponaria officinalis L. The same plant is also a source for the toxin Saporin, which is a ribosome-inactivating protein. Triterpenoidal saponins are known to increase the cytotoxicity of Saporin by modulating its intracellular trafficking.
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