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Annexin II is the membrane receptor that mediates the rapid actions of 1α,25-dihydroxyvitamin D3

✍ Scribed by Daniel T. Baran; John M. Quail; Rahul Ray; John Leszyk; Thomas Honeyman

Publisher
John Wiley and Sons
Year
2000
Tongue
English
Weight
404 KB
Volume
78
Category
Article
ISSN
0730-2312

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✦ Synopsis

1␣,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]-1␣,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]-1␣,25-dihydroxyvitamin D 3 . Antibodies to annexin II inhibited [ 14 C]-1␣,25-dihydroxyvitamin D 3 bromoacetate binding to ROS 24/1 plasma membranes, immunoprecipitated the ligand-protein complex, and inhibited 1␣,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 1␣,25-dihydroxyvitamin D 3 .

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