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Zinc binding to human lactogenic hormones and the human prolactin receptor
Author(s) -
Voorhees Jeffrey L.,
Rao Geeta Vittal,
Gordon Timothy J.,
Brooks Charles L.
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.04.019
Subject(s) - prolactin , prolactin receptor , hormone , zinc , receptor , chemistry , endocrinology , medicine , biology , biochemistry , organic chemistry
Zinc half sites are present in all human lactogenic hormones: human prolactin (hPRL), growth hormone (hGH), placental lactogens (hPL) and the hPRL receptor (hPRLr). The influence of divalent zinc (Zn 2+ ) as measured by intrinsic fluorescence or FRET in each of these hormones is unique and is affected by the presence of varying stoichiometries of hPRLr. These data show that both Zn 2+ and hPRLr binding influence hPRL conformers in an interdependent fashion. Although each of these three lactogenic hormones bind hPRLr and induce a biological response that is sensitive to the presence of increasing concentrations of Zn 2+ , each hormone is unique in the mechanistic details of this process.