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(Received for publication, April 10, 1996, and in revised form, June 25, 1996)
and
From the Monocyte chemoattractant protein-1 (MCP-1) is a
member of a family of chemotactic cytokines that induce directed
migration of leukocytes via activation of seven-transmembrane domain
receptors. To identify G-proteins that couple to the two forms of the
MCP-1 receptor, as well as to related chemokine receptors, we have
performed cotransfection experiments in mammalian cells. In COS-7
cells, the type A and type B MCP-1 receptors coupled to
G
Gladstone Institute of Cardiovascular
Disease, the § Department of Medicine, and the
¶ Daiichi Research Center, University of California,
San Francisco, California 94141-9100
i, Gq, and G16, whereas
the macrophage inflammatory protein-1/RANTES (regulated on
activation, normal T cell-expressed and secreted) receptor (C-CR1)
coupled to Gi and Gq but failed to couple
to G16. In HEK-293 cells, however, the MCP-1 receptors
and C-CR1 coupled to Gq but failed to couple to
G16. In contrast, the interleukin-8 and C5a receptors
did not couple to Gq in either COS-7 or HEK-293 cells
but did couple to G16. Exchange of intracellular loops
between the MCP-1 and interleukin-8 receptors to create chimeric
receptors revealed that the third loop of the MCP-1 receptor accounted
for virtually all of the coupling to Gq. We conclude
that the MCP-1 and related chemokine receptors couple to multiple
G-proteins, that coupling is cell type-specific, and that the third
intracellular loop of the C-C type receptors mediates Gq
coupling.
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