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Melanin‐concentrating hormone binding to mouse melanoma cells in vitro
Author(s) -
Drozdz Roma,
Siegrist Walter,
Baker Bridget I.,
Chluba-de Tapia Johanna,
Eberle Alex N.
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00043-9
Subject(s) - melanin concentrating hormone , receptor , in vitro , radioligand , radioligand assay , medicine , endocrinology , melanoma , cell , melanin , chemistry , hormone , cell culture , binding site , biology , microbiology and biotechnology , biochemistry , neuropeptide , cancer research , genetics
An analogue of human melanin‐concentrating hormone (MCH) suitable for radioiodination was designed in which Tyr 13 was replaced by Phe and Val 19 by Tyr. The resulting monoiodinated [ 125 I][Phe 13 ,Tyr 19 ]‐MCH radioligand was biologically active and led to the discovery of high‐affinity binding sites on mouse B16‐F1, G4F and G4F‐7 melanoma cells. Saturation binding analysis with G4F‐7 cells revealed 1090 MCH receptors per cell and a K D of 1.18 × 10 −10 mol/l. Receptors for MCH were also found on rat PC12 phaeochromocytoma cells, human RE melanoma cells and COS‐7 cells. Competition binding analyses with other peptides such as α‐MSH, NPY and PACAP demonstrated that MCH receptor binding is specific. rANF(1–28) was found to be a weak competitor of MCH, indicating topological similarities between MCH and rANF(1–28) when interacting with MCH receptors.