NDLI: Development of prolactin receptor antagonists with reduced pH-dependence of receptor binding.

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Development of prolactin receptor antagonists with reduced pH-dependence of receptor binding.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Hansen, Mathilde J. Kaas Olsen, Johan G. Bernichtein, Sophie O'Shea, Charlotte Sigurskjold, Bent W. Goffin, Vincent Kragelund, Birthe B.
Description	Country affiliation: Denmark Author Affiliation: Hansen MJ ( Department of Biology, University of Copenhagen, Ole Maaløes Vej 5, DK-2200 Copenhagen N, Denmark.)
Abstract	The cytokine hormone prolactin has a vast number of diverse functions. Unfortunately, it also exhibits tumor growth promoting properties, which makes the development of prolactin receptor antagonists a priority. Prolactin binds to its cognate receptor with much lower affinity at low pH than at physiological pH and since the extracellular environment around solid tumors often is acidic, it is desirable to develop antagonists that have improved binding affinity at low pH. The pK(a) value of a histidine side chain is â ¼6.8 making histidine residues obvious candidates for examination. From evaluation of known molecular structures of human prolactin, of the prolactin receptor and of different complexes of the two, three histidine residues in the hormone-receptor binding site 1 were selected for mutational studies. We analyzed 10 variants by circular dichroism spectroscopy, affinity and thermodynamic characterization of receptor binding by isothermal titration calorimetry combined with in vitro bioactivity in living cells. Histidine residue 27 was recognized as a central hot spot for pH sensitivity and conservative substitutions at this site resulted in strong receptor binding at low pH. Pure antagonists were developed earlier and the histidine mutations were introduced within such background. The antagonistic properties were maintained and the high affinity at low pH conserved. The implications of these findings may open new areas of research in the field of prolactin cancer biology.
File Format	HTM / HTML
ISSN	09523499
Issue Number	4
Volume Number	24
e-ISSN	10991352
Journal	Journal of Molecular Recognition
Language	English
Publisher	Wiley
Publisher Date	2011-07-01
Publisher Place	Great Britain (UK)
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Molecular Biology Prolactin Metabolism Receptors, Prolactin Antagonists & Inhibitors Calorimetry Circular Dichroism Histidine Chemistry Humans Hydrogen-ion Concentration Models, Molecular Mutagenesis, Site-directed Nuclear Magnetic Resonance, Biomolecular Genetics Protein Binding Protein Conformation Recombinant Proteins Thermodynamics Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Structural Biology Molecular Biology

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