JBC Biosymposia, Inc.

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Yurkow, E. J.
Right arrow Articles by Laskin, J. D.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Yurkow, E. J.
Right arrow Articles by Laskin, J. D.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

J. Biol. Chem., Vol. 262, Issue 18, 8439-8442, 06, 1987

Characterization of a photoalkylated psoralen receptor in HeLa cells

EJ Yurkow and JD Laskin

Psoralens in combination with ultraviolet light are potent modulators of epidermal cell growth and differentiation. Responsive cell types contain specific, saturable, high-affinity binding sites for the psoralens. These binding sites become covalently modified by the psoralen molecule following ultraviolet light exposure. In the present studies the psoralen receptor, labeled with [3H]8-methoxypsoralen, was visualized in the cytoplasmic and plasma membrane fractions of HeLa cells following sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The receptor had an apparent molecular mass of approximately 22,000 daltons and was shown to be sensitive to protease, but not nuclease treatment. The radiolabeled receptor could not be visualized in nuclear extracts of cells. Covalent binding of the radioligand to the receptor protein was inhibited by excess unlabeled 8- methoxypsoralen, indicating that covalent psoralen-receptor binding was saturable. In addition, the covalently modified receptor was found to persist in cells for over 5 h. The presence of a cellular protein that exhibits specific affinity for the psoralens and becomes photoalkylated by these compounds, together with previous data showing that the psoralens have direct effects on the cell surface membranes, supports our model that some of the biological effects of photoactivated psoralens are receptor-mediated.
Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 1987 by the American Society for Biochemistry and Molecular Biology.