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Annexin II is the membrane receptor that mediates the rapid actions of 1α,25‐dihydroxyvitamin D 3
Author(s) -
Baran Daniel T.,
Quail John M.,
Ray Rahul,
Leszyk John,
Honeyman Thomas
Publication year - 2000
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/(sici)1097-4644(20000701)78:1<34::aid-jcb4>3.0.co;2-z
Subject(s) - annexin a2 , annexin , annexin a1 , western blot , receptor , calcitriol receptor , chemistry , microbiology and biotechnology , calcium , biochemistry , biology , apoptosis , gene , organic chemistry
1α,25‐Dihydroxyvitamin D 3 has been shown to exert its effects by both genomic (minutes to hours) and rapid (seconds to minutes) mechanisms. The genomic effects are mediated by interaction with the nuclear vitamin D receptor. We show that the vitamin D analog, [ 14 C]‐1α,25‐dihydroxyvitamin D 3 bromoacetate, is specifically bound to a protein (molecular weight 36 kDa) in the plasma membrane of rat osteoblastlike cells (ROS 24/1). The plasma membrane protein labeled with the bromoacetate analog was identified as annexin II by sequence determination and Western blot. Partially purified plasma membrane proteins (PI 6.9–7.4) and purified annexin II exhibited specific and saturable binding for [ 3 H]‐1α,25‐dihydroxyvitamin D 3 . Antibodies to annexin II inhibited [ 14 C]‐1α,25‐dihydroxyvitamin D 3 bromoacetate binding to ROS 24/1 plasma membranes, immunoprecipitated the ligand–protein complex, and inhibited 1α,25‐dihydroxyvitamin D 3 –induced increases in intracellular calcium in ROS 24/1 cells. The results indicate that annexin II may serve as a receptor for rapid actions of 1α,25‐dihydroxyvitamin D 3 . J. Cell. Biochem. 78:34–46, 2000. © 2000 Wiley‐Liss, Inc.