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Evidence for increased αMSH receptor binding in the F 1 variant of B 16 melanoma cells grown in dialyzed fetal calf serum
Author(s) -
McQuillan A.,
Hutchinson M.,
Panasci L. C.
Publication year - 1989
Publication title -
journal of cellular physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.529
H-Index - 174
eISSN - 1097-4652
pISSN - 0021-9541
DOI - 10.1002/jcp.1041410208
Subject(s) - receptor , endocrinology , medicine , alpha (finance) , hormone , insulin , chemistry , fetus , biology , microbiology and biotechnology , pregnancy , genetics , construct validity , nursing , patient satisfaction
The specific binding of an αMSH analogue (Ac‐[Nle 4 , D‐Phe 7 ] αMSH 4–11 NH 2 ) was enhanced in the presence of 10% dialyzed fetal calf serum (FCS) as compared with 10% FCS (nondialyzed) in the F 1 variant of B 16 melanoma cells. The replenishment of dialyzed serum with adrenocorticotrophic hormone (ACTH) or insulin had no effect on the increased level of αMSH receptor binding in these cells. However, 10 nM αMSH or 1 μM ACTH under identical conditions significantly decreased the level of αMSH binding. Competitive binding studies involving the αMSH analogue revealed that the specificity of the receptor was restricted to the complete molecule of αMSH, our analogue, βMSH and ACTH 1–24 . ACTH 4–10 , which contains the amino acid sequence responsible for biological activity, showed a very low affinity for the receptor. Furthermore, we observed an interesting phenomenon unique to dialyzed FCS in that once the cells were grown to confluence and melanin was produced, the cells were no longer viable. However, in McCoy's medium, which is deficient in tyrosine, the cells did not produce melanin and remained viable.