Yamagami S, Tanaka H, Endo N
Pharmaceutical Discovery Research Laboratories, Teijin Institute for Biomedical Research, Asahigaoka, Hino, Tokyo, Japan.
FEBS Lett. 1997 Jan 6;400(3):329-32. doi: 10.1016/s0014-5793(96)01411-1.
We studied the activities of the monocyte chemoattractant proteins MCP-1, MCP-2 and MCP-3 on human embryonic kidney 293-EBNA cells transfected with the MCP-1 receptor (CC CKR2B). At 4 nM, MCP-2 induced a Ca2+ influx which was as potent as that with MCP-1 at 4 nM, although the increase by MCP-2 became saturated at higher concentrations. In addition, all three MCPs showed dose-dependent inhibition of adenylyl cyclase activity stimulated by forskolin (IC50 values: 0.3 nM for MCP-1, 7 nM for MCP-2, and 1.5 nM for MCP-3). In conclusion, our data indicate that MCP-2 can exert its effects through the MCP-1 receptor, CC CKR2B.
我们研究了单核细胞趋化蛋白MCP-1、MCP-2和MCP-3对转染了MCP-1受体（CC CKR2B）的人胚肾293-EBNA细胞的活性。在4 nM时，MCP-2诱导的Ca2+内流与4 nM的MCP-1相当，尽管MCP-2在更高浓度时增加趋于饱和。此外，所有三种MCP均表现出对福斯可林刺激的腺苷酸环化酶活性的剂量依赖性抑制（IC50值：MCP-1为0.3 nM，MCP-2为7 nM，MCP-3为1.5 nM）。总之，我们的数据表明MCP-2可通过MCP-1受体CC CKR2B发挥其作用。
