Juvenile hormone binding protein traffic — Interaction with ATP synthase and lipid transfer proteins

Juvenile hormone (JH) controls insect development, metamorphosis and reproduction. In insect hemolymph a significant proportion of JH is bound to juvenile hormone binding protein (JHBP), which serves as a carrier supplying the hormone to the target tissues. To shed some light on JHBP passage within...

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Veröffentlicht in:Biochimica et biophysica acta 2009-09, Vol.1788 (9), p.1695-1705
Hauptverfasser: Zalewska, Marta, Kochman, Agata, Estève, Jean-Pierre, Lopez, Frédéric, Chaoui, Karima, Susini, Christiane, Ożyhar, Andrzej, Kochman, Marian
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container_issue 9
container_start_page 1695
container_title Biochimica et biophysica acta
container_volume 1788
creator Zalewska, Marta
Kochman, Agata
Estève, Jean-Pierre
Lopez, Frédéric
Chaoui, Karima
Susini, Christiane
Ożyhar, Andrzej
Kochman, Marian
description Juvenile hormone (JH) controls insect development, metamorphosis and reproduction. In insect hemolymph a significant proportion of JH is bound to juvenile hormone binding protein (JHBP), which serves as a carrier supplying the hormone to the target tissues. To shed some light on JHBP passage within insect tissues, the interaction of this carrier with other proteins from Galleria mellonella (Lepidoptera) was investigated. Our studies revealed the presence of JHBP within the tracheal epithelium and fat body cells in both the membrane and cytoplasmic sections. We found that the interaction between JHBP and membrane proteins occurs with saturation kinetics and is specific and reversible. ATP synthase was indicated as a JHBP membrane binding protein based upon SPR-BIA and MS analysis. It was found that in G. mellonella fat body, this enzyme is present in mitochondrial fraction, plasma membranes and cytosol as well. In the model system containing bovine F 1 ATP synthase and JHBP, the interaction between these two components occurs with K d = 0.86 nM. In hemolymph we detected JHBP binding to apolipophorin, arylphorin and hexamerin. These results provide the first demonstration of the physical interaction of JHBP with membrane and hemolymph proteins which can be involved in JHBP molecule traffic.
doi_str_mv 10.1016/j.bbamem.2009.04.022
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subjects Animals
Apolipoproteins - metabolism
Arylphorin
ATP synthase
Carrier Proteins - metabolism
Fat Body - chemistry
Fat Body - ultrastructure
Hemolymph - metabolism
Hexamerin
Insect Proteins - metabolism
Juvenile hormone binding protein
Juvenile Hormones - metabolism
Life Sciences
Lipophorin
Membrane Proteins - metabolism
Mitochondrial Proton-Translocating ATPases - metabolism
Moths
Neurons and Cognition
Protein Transport - physiology
Surface Plasmon Resonance
title Juvenile hormone binding protein traffic — Interaction with ATP synthase and lipid transfer proteins
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