Abstract：
:We determined whether two naturally occurring steroids, cortisol and 17beta-estradiol (E2), can rapidly modulate the activity of an important membrane protein, human erythrocyte (RBC) Na+,K+-ATPase, an enzyme that does not bind either hormone directly. We also determined the membrane binding locations for cortisol and E2 and their effects on membrane molecular structure and fluidity. Direct application of both steroids to intact human RBC significantly altered maximum ouabain-sensitive 86Rb uptake within 5 min: Cortisol decreased it by 24%, whereas E2 increased it by 18%. As determined by small angle x-ray diffraction, these steroids occupied distinct time-averaged binding locations in the RBC membrane, cortisol localizing near the bilayer surface, 14-29 A from the bilayer center, and E2 localizing deep within the hydrocarbon core, 0-7 A from the bilayer center. Neither steroid significantly changed overall bilayer width or membrane fluidity. These data suggest that cell membrane protein function can be altered rapidly and differentially by naturally occurring steroids. This effect did not appear to be related to the different binding locations of the steroids in the membrane or to their influence on membrane fluidity.
journal_name
Life Scijournal_title
Life sciencesauthors
Golden GA,Mason RP,Tulenko TN,Zubenko GS,Rubin RTdoi
10.1016/s0024-3205(99)00360-4subject
Has Abstractpub_date
1999-01-01 00:00:00pages
1247-55issue
12eissn
0024-3205issn
1879-0631pii
S0024320599003604journal_volume
65pub_type
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