Effects of antiestrogen versus antiprogestin on transformed and nontransformed steroid receptors

Theoretical and experimental studies have illustrated a potential source of error in sedimentation coefficients obtained by sucrose density gradient centrifugation of proteins undergoing reversible self-association. The error stems from the excluded volume (molecular crowding) effect of the sucrose on the activity coefficients of monomeric and polymeric states. The consequent displacement of the equilibrium position in favor of polymeric state(s) is a function of sucrose concentration, and can therefore result in failure to detect the equilibrium coexistence of monomer if 5% sucrose suffices to displace the equilibrium completely toward dimer. In less extreme situations, it may result in the evaluation of an average sedimentation coefficient whose magnitude is a function of sucrose concentration and hence of the distance migrated into the sucrose gradient. These features are illustrated by the results of computer-simulated sedimentation of reversibly dimerizing systems in a sucrose gradient, and by conventional sedimentation velocity experiments on yeast enolase.

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Effects of Molecular Crowding on Protein Self-Association: A Potential Source of Error in Sedimentation Coefficients Obtained by Zonal Ultracentrifugation in a Sucrose Gradient

Cann

Coombs²,

Howlett³

et al. 1994

Biochemistry

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Ligands induce conformational changes in the carboxyl-terminus of progesterone receptors which are detected by a site-directed antipeptide monoclonal antibody.

Weigel

Beck

Estes

et al. 1992

Molecular Endocrinology

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We have prepared a monoclonal antibody, C-262, to a synthetic peptide that contains the carboxy-terminal 14 amino acids from progesterone receptors (PR). This sequence is 100% conserved in all species of PRs that have been cloned to date, suggesting that this antibody will recognize all mammalian and avian PR. The C-262 antibody recognizes both native and denatured forms of the receptor. However, it does not recognize PR when they are bound to the hormone agonists progesterone or R5020. Surprisingly the antibody does recognize PR when they are bound to the steroid antagonist RU486. This suggests that progestin agonists induce a conformational change in the receptor that occludes the C-262 epitope in the carboxyl-terminus, whereas unliganded receptors and receptors bound with RU486 assume distinct conformations that leaves the C-terminal tail accessible to the C-262 antibody.

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Effects of antiestrogen versus antiprogestin on transformed and nontransformed steroid receptors

Cited by 2 publications

References 24 publications

Effects of Molecular Crowding on Protein Self-Association: A Potential Source of Error in Sedimentation Coefficients Obtained by Zonal Ultracentrifugation in a Sucrose Gradient

Effects of Molecular Crowding on Protein Self-Association: A Potential Source of Error in Sedimentation Coefficients Obtained by Zonal Ultracentrifugation in a Sucrose Gradient

Ligands induce conformational changes in the carboxyl-terminus of progesterone receptors which are detected by a site-directed antipeptide monoclonal antibody.

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