Action of juvenile hormone (JH) esterase on the JH-JH binding protein complex. an in vitro model of JH metabolism in a caterpillar

Kazushige Touhara, Bryony C. Bonning, Bruce D. Hammock, Glenn D. Prestwich

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

A decline in juvenile hormone (JH) titer early in the last larval instar leads to the metamorphosis of lepidopterous larvae into pupae. Clearance of JH is associated with an increase in the level of JH-specific esterase (JHE) that hydrolyzes JH into the biologically inactive JH-acid. Experiments with purified recombinant JHBP (rJHBP) and with both natural and recombinant JHE (rJHE) were designed to test the hypothesis that JHBP "protects" JH from JHE degradation in insect hemolymph. First, at low JHE concentrations, the rate of hydrolysis of JHBP-bound JH by JHE was determined by the rate of dissociation of JH from JHBP. Second, the rate of hydrolysis of JH increased with increasing JHE concentrations even in the presence of excess JHBP. In contrast, JH was not hydrolyzed by a general carboxylesterase in the presence of JHBP. Third, the rate of JH hydrolysis when the JHBP-JH complex was added to JHBP-depleted hemolymph was essentially identical to that in undiluted hemolymph. Taken together, these results suggest that JHBP protects JH from nonspecific hydrolytic processes, while still allowing highly specific JHE to hydrolyze JH by recognizing the JH-JHBP complex. Finally, JHBP efficiently extracted JH from lipophilic depots (the so-called "refractory pool", resulting in more rapid degradation of JH by JHE. Thus, JHBP is crucial for maintaining and distributing JH in hemolymph in the absence of JHE, and may assist in the rapid clearance of JH in the presence of JHE.

Original languageEnglish (US)
Pages (from-to)727-734
Number of pages8
JournalInsect Biochemistry and Molecular Biology
Volume25
Issue number6
DOIs
StatePublished - 1995

Fingerprint

juvenile hormone esterase
hormone metabolism
Juvenile Hormones
juvenile hormones
Metabolism
binding proteins
insect larvae
Carrier Proteins
Esterases
esterases
Hemolymph
hemolymph
In Vitro Techniques
Hydrolysis
hydrolysis
Degradation
carboxylesterase

Keywords

  • Insect
  • JH binding protein
  • Metabolism
  • Metamorphosis
  • Protective role

ASJC Scopus subject areas

  • Insect Science
  • Biochemistry
  • Molecular Biology

Cite this

Action of juvenile hormone (JH) esterase on the JH-JH binding protein complex. an in vitro model of JH metabolism in a caterpillar. / Touhara, Kazushige; Bonning, Bryony C.; Hammock, Bruce D.; Prestwich, Glenn D.

In: Insect Biochemistry and Molecular Biology, Vol. 25, No. 6, 1995, p. 727-734.

Research output: Contribution to journalArticle

Touhara, Kazushige ; Bonning, Bryony C. ; Hammock, Bruce D. ; Prestwich, Glenn D. / Action of juvenile hormone (JH) esterase on the JH-JH binding protein complex. an in vitro model of JH metabolism in a caterpillar. In: Insect Biochemistry and Molecular Biology. 1995 ; Vol. 25, No. 6. pp. 727-734.
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AU - Prestwich, Glenn D.

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AB - A decline in juvenile hormone (JH) titer early in the last larval instar leads to the metamorphosis of lepidopterous larvae into pupae. Clearance of JH is associated with an increase in the level of JH-specific esterase (JHE) that hydrolyzes JH into the biologically inactive JH-acid. Experiments with purified recombinant JHBP (rJHBP) and with both natural and recombinant JHE (rJHE) were designed to test the hypothesis that JHBP "protects" JH from JHE degradation in insect hemolymph. First, at low JHE concentrations, the rate of hydrolysis of JHBP-bound JH by JHE was determined by the rate of dissociation of JH from JHBP. Second, the rate of hydrolysis of JH increased with increasing JHE concentrations even in the presence of excess JHBP. In contrast, JH was not hydrolyzed by a general carboxylesterase in the presence of JHBP. Third, the rate of JH hydrolysis when the JHBP-JH complex was added to JHBP-depleted hemolymph was essentially identical to that in undiluted hemolymph. Taken together, these results suggest that JHBP protects JH from nonspecific hydrolytic processes, while still allowing highly specific JHE to hydrolyze JH by recognizing the JH-JHBP complex. Finally, JHBP efficiently extracted JH from lipophilic depots (the so-called "refractory pool", resulting in more rapid degradation of JH by JHE. Thus, JHBP is crucial for maintaining and distributing JH in hemolymph in the absence of JHE, and may assist in the rapid clearance of JH in the presence of JHE.

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