Relationship of hemolymph juvenile hormone-binding protein to lipophorin in Leucophaea maderae

Rayne, Richard C.; Koeppe, John K.

doi:10.1016/0020-1790(88)90075-3

Cited by 25 publications

(4 citation statements)

References 22 publications

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“…Also in Leucophnea mczderae, both ovarian and egg 220-kDa juvenile-hormone-binding proteins were found to have antigenic determinants similar to those of the haemolymph juvenile-hormone carrier (which is apolipophorin I). suggesting that the binding of juvenile hormone to this protein is involved in mediating the action of lipophorin, e. g. it might enable oocyte receptors to recognize the lipophorin molecule [32]. It has been previously shown that some steroid-carrier and vitamin-carrier proteins have membrane-bound receptors which recognize the complex of ligand with its carrier protein [33 -361.…”

Section: Discussionmentioning

confidence: 99%

Conformational change of the haemolymph juvenile‐hormone‐binding protein from Galleria mellonella (L)

Wieczorek

Kochman

1991

European Journal of Biochemistry

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A juvenile‐hormone‐binding protein (juvenile‐hormone carrier), isolated fromGalleria mellonella haemolymph, was treated with trypsin, chymotrypsin, carboxypeptidase A and subtilisin. Among these enzymes, only subtilisin was able to affect juvenile‐hormone‐binding activity of this protein. With SDS/PAGE it was shown that juvenile‐hormone‐binding protein, a 32‐kDa peptide, is first slowly converted into a 30‐kDa molecule, then into two or three smaller‐molecular‐mass species (20–25 kDa), which in turn were further digested to small peptides undetectable in PAGE. The 30‐kDa peptide has a 2.4‐times‐higher dissociation constant for juvenile hormone than the native protein. No binding activity was detected for 20–25‐kDa peptides. The rate of proteolysis of juvenile‐hormone‐binding protein was decreased by more than twofold in the presence of hormone, however, the overall cleavage pattern was unchanged. Under non‐denaturing conditions, free binding‐protein molecules could be separated from juvenile‐hormone–binding‐protein complex due to a slower electrophoretic mobility of the complex. As judged from ultracentrifugation and cross‐linking experiments, binding of the hormone to its haemolymph carrier does not induce formation of oligomers, but shifts the sedimentation coefficient from 2.30S to 2.71S. It is conclude that juvenile‐hormone binding induces a conformational transition of its carrier protein. This hormone‐induced change might have a physiological significance for signal transmission.

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Section: Discussionmentioning

confidence: 99%

Conformational change of the haemolymph juvenile‐hormone‐binding protein from Galleria mellonella (L)

Wieczorek

Kochman

1991

European Journal of Biochemistry

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“…It is also enantioselective, because the protein exhibits much higher affinity for the natural (10R)-JHIII than for the unnatural (10s)-enantiomer. Each lipophorin molecule contains one JHIII-specific binding site, which is located on apolipophorin I (Rayne and Koeppe, 1988;de Kort and Koopmanschap, 1989;Okot-Kotber and Prestwich, 1991). Lipophorin was subsequently shown to be the JHBP in other insect species representing several orders: Dyctyoptera; Isoptera, and probably also in Hymenoptera and Diptera (de Kort et al, 1984;van Mellaert et al, 1985;Rayne and Koeppe, 1988;Shemshedini and Wilson, 1988;Okot-Kotber and Prestwich, 1991;King and Tobe, 1992;Lanzrein et al, 1993;Trowel1 et al, 1995).…”

Section: Juvenile Hormone Binding Proteinsmentioning

confidence: 99%

Regulation of JH titers: The relevance of degradative enzymes and binding proteins

Kort

Granger

1996

Arch. Insect Biochem. Physiol.

112

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Juvenile hormones play a crucial role in development, metamorphosis, and reproduction of insects. This mini‐review discusses the nature of the juvenile hormones identified in insects and their changes in concentration in the hemolymph during development and reproduction. The hemolymph titer is largely determined by the rate at which juvenile hormones are synthesized and released by the corpora allata, but other factors are also involved in titer regulation, such as the affinity and concentration of juvenile hormone binding proteins in the hemolymph and the rate of juvenile hormone degradation in hemolymph and tissues. Juvenile hormone specific esterases occur in hemolymph and tissues, whereas epoxide hydrolases, which may degrade the hormone, are exclusively tissue bound. The activities of these degradative enzymes and the concentration of binding proteins change during the insect life cycle and these changes are related to fluctuations in hormone titer. However, we are still a long way from understanding the subtle interactions between these components in regulation of juvenile hormone titers. In particular, our knowledge is hampered by lack of information about the types, concentrations, and affinities of intracellular juvenile hormone receptors. © 1996 Wiley‐Liss, Inc.

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“…Some JHBPs are lipophorins, that is, lipoproteins w ich also apparently shuttle lipids in insect hemolymph [34]. Those lipophorins have been isolated and characterized from Leptinofarsa decemlineutu [19], Periplunetu umericuna [19,35], and Leucophaeu maderue [36]. It appears likely that the JHBP in Z .…”

Section: Discussionmentioning

confidence: 99%

Juvenile hormone binding proteins of termites detected by photoaffinity labeling: Comparison of Zootermopsis nevadensis with two rhinotermitids

Okot-Kotber

Prestwich

1991

Arch Insect Biochem Physiol

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The hemolyrnph of each caste of the primitive dampwood termite Zootermopsis nevadensis (Isoptera, Termopsidae, Termopsinae) contains a high molecular mass lipoprotein which functions as a specific, high affinity carrier for juvenile hormone (JH) Ill, as detected by JH Ill-displaceable covalent modification by the tritium-labeled photoaffinity analog ( INTRODUCTIONJuvenile hormones are key control elements in the physiology of insect growth, development, reproduction, and caste control in social insects [1,2]. Luscher [3] underscored the fact that caste control in termites occurs as a result of changes in the JH* titers which are modulated by the environment. This role of JH and JH mimics has been demonstrated in a number of termite species, including lower termites, e.g., Knlotermes fluvicollis [4], &ticdifermesfiuvipes [5,6], and Zootermopsis nevudensis [7], and in the higher termites, e.g., Nnsutitermes exitiosus [S] and Macrotermes michaelseni 191.

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Relationship of hemolymph juvenile hormone-binding protein to lipophorin in Leucophaea maderae

Cited by 25 publications

References 22 publications

Conformational change of the haemolymph juvenile‐hormone‐binding protein from Galleria mellonella (L)

Conformational change of the haemolymph juvenile‐hormone‐binding protein from Galleria mellonella (L)

Regulation of JH titers: The relevance of degradative enzymes and binding proteins

Juvenile hormone binding proteins of termites detected by photoaffinity labeling: Comparison of Zootermopsis nevadensis with two rhinotermitids

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