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Somatostatin Receptors in Malignant Lymphomas: Targets for Radiotherapy?

Virgil A.S.H. Dalm, PhD1, Leo J. Hofland, PhD1, Cornelia M. Mooy, MD, PhD2, Marlijn A. Waaijers1, Peter M. van Koetsveld1, Anton W. Langerak, PhD3, Frank T.J. Staal, PhD3, Aart-Jan van der Lely, MD, PhD1, Steven W.J. Lamberts, MD, PhD1 and Martin P. van Hagen, MD, PhD1,3

1 Department of Internal Medicine, Erasmus Medical Center, Rotterdam, The Netherlands
2 Department of Ophthalmic Pathology, Erasmus Medical Center, Rotterdam, The Netherlands
3 Department of Immunology, Erasmus Medical Center, Rotterdam, The Netherlands



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FIGURE 1. Autoradiography experiments on lymphomas. (Top) Binding of [125I-Tyr3]octreotide, represented by black spots, to rat brain (A), GH-producing tumor (B), both used as positive controls, and example of 1 lymphoma studied (C), lymphoma no. 6. (Bottom) Binding of [125I-Tyr3]octreotide is displaced by excess unlabeled octreotide.

 


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FIGURE 2. Membrane binding studies. Scatchard analysis of [125I-Tyr3]octreotide binding on human B and myeloid cell lines: {diamond}, B-CLL (dissociation constant [Kd] = 0.8 nmol/L, n = 50 fmol/mg); {blacksquare}, APD cell line (Kd = 0.7 nmol/L, n = 40 fmol/mg); •, TMM cell line (Kd = 0.4 nmol/L, n = 100 fmol/mg); {blacktriangledown}, JY cell line (Kd = 0.4 nmol/L, n = 195 fmol/mg); {triangleup}, CC2B cell line (Kd = 0.8 nmol/L, n = 460 fmol/mg).

 


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FIGURE 3. Internalization experiment using CC2B, JY, TMM, APD, and B-CLL cells. Cells were incubated either with [125I-Tyr3]octreotide alone or with [125I-Tyr3]octreotide and excess of unlabeled octreotide (1 µmol/L) for 30, 60, and 120 min, respectively. At each time point, internalization was measured. Results are presented as amount of radiolabeled compound internalized by cell in fmol/106 cells and as degree of internalization for 106 cells as percentage of administered dose.

 





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