Biologically active monoiodinated alpha-MSH derivatives for receptor binding studies using human melanoma cells.

Abstract

Three different monoiodinated radioligands of alpha-MSH (alpha-melanocyte-stimulating hormone) were compared in a binding assay with human D10 melanoma cells: [Tyr(125I)2]-alpha-MSH, [Tyr(125I)2,NIe4]-alpha-MSH, and [Tyr(125I)2,NIe4,D-Phe7]-alpha-MSH. They were prepared either by the classical chloramine T method or by the Enzymobead method. A simple and rapid purification scheme was developed consisting of a primary separation on reversed-phase C18 silica cartridges immediately after the iodination, followed by HPLC purification before each binding experiment. Biological testing of the three radioligands showed that they all retained high melanotropic activity in the B16 melanin assay and the Anolis melanophore assay. However, in human D10 melanoma cells, [Tyr(125I)2,NIe4]-alpha-MSH led to a high degree of non-specific binding to the cells which could not be displaced by excess alpha-MSH and only partially by [NIe4]-alpha-MSH. The [Tyr(125I)2,NIe4,D-Phe7]-alpha-MSH tracer gave similar results but with a much lower proportion of non-specific binding. On the other hand, [Tyr(125I)2]-alpha-MSH proved to be an excellent radioligand whose non-specific binding to the D10 cells was not higher than 20% of the total binding.

Statistics

0100200'97'99'01'03'05'07'09'11'13'15'17
Citations per Year

87 Citations

Semantic Scholar estimates that this publication has 87 citations based on the available data.

See our FAQ for additional information.

Cite this paper

@article{Eberle1991BiologicallyAM, title={Biologically active monoiodinated alpha-MSH derivatives for receptor binding studies using human melanoma cells.}, author={Alex N. Eberle and V J Verin and Flavio F Solca and Walter Siegrist and C K{\"{u}enlin and Claudia Bagutti and Stefan Stutz and Juerg Girard}, journal={Journal of receptor research}, year={1991}, volume={11 1-4}, pages={311-22} }