Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10872102 | FEBS Letters | 2011 | 6 Pages |
Abstract
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 (Zn2+) 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 Zn2+ 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 Zn2+, each hormone is unique in the mechanistic details of this process.
Keywords
TPENN,N,N′,N′-tetrakis(2-pyridylmethyl)ethylenediaminehPRL7-Diethylamino-3-(4′-maleimidylphenyl)-4-methylcoumarinHPLDTTCPMhGHZn2+Förster resonance energy transferFRETHumanConformation changedithiothreitolZincFluorescencePlacental lactogenHuman placental lactogenGrowth hormoneHuman growth hormoneProlactinHuman prolactinprolactin receptor
Related Topics
Life Sciences
Agricultural and Biological Sciences
Plant Science
Authors
Jeffrey L. Voorhees, Geeta Vittal Rao, Timothy J. Gordon, Charles L. Brooks,