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Vol. 294, Issue 1, 61-72, July 2000
Molecular Pharmacology Laboratory, Department of Pharmacology, The
University of Melbourne, Victoria, Australia (N.T., G.C., E.T.Z.,
P.M.S.); and Receptor Systems Unit, Glaxo Wellcome Medicines Research
Centre, Stevenage, Hertfordshire, United Kingdom (S.M.F.)
Receptor activity modifying proteins (RAMPs) constitute a group of
three proteins, designated as RAMP1, 2, and 3, which are able to effect
functional changes in some members of the G protein-coupled receptor
family. Thus, RAMP1 or RAMP3 can modify the calcitonin receptor (CTR)
to also function as a high-affinity amylin receptor-like phenotype. To
examine the RAMP/CTR interaction, individual RAMPs were coexpressed
with either of the two human CTR (hCTR) isoforms, the insert negative
(hCTRI1
) or the insert positive (hCTRI1+), in
Chinese hamster ovary (CHO-P) or African monkey kidney (COS-7) cells.
CHO-P cells provide an environment conducive to a low, but significant,
level of amylin binding with either hCTR isoform alone, unlike in
COS-7, where RAMP coexpression is imperative for amylin binding. Also,
in CHO-P, hCTRI1 induced amylin binding with all three
RAMPs, in contrast to COS-7, where only RAMP1 or RAMP3 generate an
amylin receptor phenotype. hCTRI1+ induced high-affinity
amylin binding with any RAMP in either cell line. In COS-7 cells,
hCTRI1+/RAMP-generated receptor displayed high- and
low-affinity states, in contrast with the single-state binding seen
with hCTRI1/RAMP-generated receptor, whereas in CHO-P
cells a two-affinity state receptor phenotype was evident with both
hCTR isoforms. Endogenous RAMP expression is low and similar between
cell lines. The results suggest that CTR/RAMP interaction in these
cells is complex with other cellular factors such as the levels of
different G proteins and/or receptor/RAMP stoichiometry following
heterologous coexpression contributing to the ultimate receptor phenotype.
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