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Biologically Active Monoiodinated α-MSH Derivatives for Receptor Binding Studies Using Human Melanoma Cells

Eberle, Alex N. ; Verin, Vreni Jäggin ; Solca, Flavio ; Siegrist, Walter ; Küenlin, Caroline ; Bagutti, Claudia ; Stutz, Sibylla ; Girard, Jürg

Journal of receptor research, 1991, Vol.11 (1-4), p.311-322 [Periódico revisado por pares]

United States: Informa UK Ltd

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Título:
Biologically Active Monoiodinated α-MSH Derivatives for Receptor Binding Studies Using Human Melanoma Cells
Autor: Eberle, Alex N. ; Verin, Vreni Jäggin ; Solca, Flavio ; Siegrist, Walter ; Küenlin, Caroline ; Bagutti, Claudia ; Stutz, Sibylla ; Girard, Jürg
Assuntos: 550201 - Biochemistry- Tracer Techniques ; alpha-MSH - analogs & derivatives ; alpha-MSH - isolation & purification ; alpha-MSH - metabolism ; AMINES ; ANIMAL CELLS ; ANIMALS ; BASIC BIOLOGICAL SCIENCES ; BETA DECAY RADIOISOTOPES ; BIOCHEMICAL REACTION KINETICS ; Biological Assay ; BODY ; CHLORAMINES ; CHROMATOGRAPHY ; Chromatography, High Pressure Liquid ; Chromatography, Liquid ; DAYS LIVING RADIOISOTOPES ; DISEASES ; ELECTRON CAPTURE RADIOISOTOPES ; ENDOCRINE GLANDS ; FRACTIONATION ; GLANDS ; HORMONES ; Humans ; INTERMEDIATE MASS NUCLEI ; INTERNAL CONVERSION RADIOISOTOPES ; IODINE 125 ; IODINE ISOTOPES ; Iodine Radioisotopes ; ISOTOPE APPLICATIONS ; Isotope Labeling - methods ; ISOTOPES ; KINETICS ; LIGANDS ; LIQUID COLUMN CHROMATOGRAPHY ; MAMMALS ; MAN ; Melanoma - metabolism ; MELANOMAS ; MEMBRANE PROTEINS ; NEOPLASMS ; NUCLEI ; ODD-EVEN NUCLEI ; ORGANIC CHLORINE COMPOUNDS ; ORGANIC COMPOUNDS ; ORGANIC HALOGEN COMPOUNDS ; ORGANS ; PITUITARY GLAND ; PRIMATES ; PROTEINS ; RADIOASSAY ; RADIOISOTOPES ; Radioligand Assay ; REACTION KINETICS ; RECEPTORS ; Receptors, Pituitary Hormone - metabolism ; SEPARATION PROCESSES ; Tosyl Compounds ; TRACER TECHNIQUES ; TUMOR CELLS ; Tumor Cells, Cultured ; VERTEBRATES
É parte de: Journal of receptor research, 1991, Vol.11 (1-4), p.311-322
Descrição: Abstract Three different monolodinated radioligands of α-MSH (α-melanocyte-stimulating hormone) were compared in a binding assay with human D10 melanoma cells: [Tyr(125l)2]-α-MSH, [Tyr(125l)2, Nle4]-α-MSH, and [Tyr(125l)2, Nle4, D-Phe7]-α-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(125l)2-α-MSH led to a high degree of non-specific binding to the cells which could not be displaced by excess α-MSH and only partially by [Nle4]α-MSH. The [Tyr(125l)2, Nle4, D-Phe7]-α-MSH tracer gave similar results but with a much lower proportion of non-specific binding. On the other hand, [Tyr(1251)2]-a-MSH proved to be an excellent radioligand whose non-specific binding to the D10 cells was not higher than 20% of the total binding.
Editor: United States: Informa UK Ltd
Idioma: Inglês

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Biologically Active Monoiodinated α-MSH Derivatives for Receptor Binding Studies Using Human Melanoma Cells

Eberle, Alex N. ; Verin, Vreni Jäggin ; Solca, Flavio ; Siegrist, Walter ; Küenlin, Caroline ; Bagutti, Claudia ; Stutz, Sibylla ; Girard, Jürg

United States: Informa UK Ltd

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