Juvenile hormone acid: Evidence for a hormonal function in induction of vitellogenin in larvae ofManduca sexta

Ismail, Sheikh M.; Satyanarayana, K.; Bradfield, James Y.; Dahm, Karl H.; Bhaskaran, G.

doi:10.1002/(sici)1520-6327(1998)37:4<305::aid-arch6>3.0.co;2-p

Cited by 45 publications

(22 citation statements)

References 40 publications

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“…However, recent evidence shows that the role of hemolymph JHE is more likely to produce the biologically active JH acid required to induce tissue competence for metamorphosis (4,5). Similarly, it is possible that JH diol may also possess some previously unrecognized biological function.…”

Section: Discussionmentioning

confidence: 99%

“…Step 4 , 0.1 M sodium phosphate (pH 7.0), and 10% sucrose) for several hours prior to loading. Elution of JHDK was accomplished using a two-step gradient from 0 to 100% buffer E (buffer D without 2.0 M (NH 4 ) 2 SO 4 ) over 40 min at 0.4 ml/min and from 100% buffer E to 50% solvent A (50% propanol/H 2 O) over 10 min.…”

Section: Isolation and Purification Of Jhdkmentioning

confidence: 99%

“…Samples were analyzed using a SAX column (SynchroPak AX 300, 100 ϫ 4.6 mm, 8 m, 1000 Å, SynChrom, Inc.) equilibrated with 0.02 M NH 4 ϩ phosphate (pH 3.8). The column was eluted with a PerkinElmer Instruments HPLC (described above) using a gradient of 0 -100% 2.0 M NH 4 ϩ phosphate over 40 min with a flow rate of 1 ml/min. An identical blank gradient was run to clean the column between analyses.…”

Section: Enzyme Assaysmentioning

confidence: 99%

“…However, recent studies have identified a hormonal role for JH acid (compound 2; see Fig. 7) (4,5), suggesting that JHE is more than an inactivating enzyme. Recently, a cytochrome P450 terpenoid hydroxylase was discovered in the corpora allata of Diploptera punctata; this enzyme may play a role in the temporal suppression of JH titer in the cockroach by metabolizing JH III to 12-hydroxy-JH III (6).…”

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confidence: 99%

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Juvenile Hormone Diol Kinase

Maxwell

Welch

Schooley

2002

Journal of Biological Chemistry

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Manduca sexta juvenile hormone diol kinase (JHDK) catalyzes the conversion of juvenile hormone (JH) diol to JH diol phosphate. JHDK may be the first example of a phosphotransferase directly involved in the catabolism and inactivation of a lipid-soluble hormone. JHDK is an enzyme crucial for secondary metabolism of JH and possesses high specificity and catalytic efficiency for JH diol. In this study, the purification and characterization of native JHDK are described; its enzymatic properties are examined; and its role in cellular JH metabolism is explored. Using a variety of potential substrates, we show that JHDK has a preference for ATP, but will catalyze the formation of JH diol phosphate with GTP as the phosphate donor. JHDK has a nanomolar K m for JH I diol and a low micromolar value for MgATP. JH II and III diols also serve as phosphate acceptors with low micromolar K m , whereas other diol derivatives of terpenoid esters structurally similar to JH metabolites are not phosphorylated. The reaction proceeds via a sequential Bi Bi mechanism. JHDK is active as a homodimer with a subunit molecular mass of 20 kDa. JHDK binds 5-p-fluorosulfonylbenzoyladenosine and is inhibited by micromolar levels of Ca 2؉ .Juvenile hormones (compound 1; see Fig. 7) are sesquiterpenoids produced in the corpora allata of insects. They travel to target tissues through the hemolymph via a juvenile hormone (JH) 1 -binding protein, where they serve to modulate development, metamorphosis, and sexual maturation (1). During metamorphosis and larval development, JH titers are strictly regulated through biosynthesis and catabolism (2, 3). JH esterase (JHE) and JH epoxide hydrolase are regarded as the enzymes responsible for JH catabolism. However, recent studies have identified a hormonal role for JH acid (compound 2; see Fig. 7) (4, 5), suggesting that JHE is more than an inactivating enzyme. Recently, a cytochrome P450 terpenoid hydroxylase was discovered in the corpora allata of Diploptera punctata; this enzyme may play a role in the temporal suppression of JH titer in the cockroach by metabolizing JH III to 12-hydroxy-JH III (6).Most identifications of JH metabolites in the past have involved studies using either hemolymph or whole organisms, making it difficult to distinguish the role of intracellular JH metabolism. Two studies have been conducted using Manduca sexta tissues dissected and maintained in vitro, one with Malpighian tubules (7) and the other with fat body and imaginal discs (8). The classic model for JH metabolism in insects consists of two primary pathways of inactivation: epoxide hydrolysis to form the diol metabolites and ester cleavage to form the acid metabolites. However, there have been many reports indicating very polar JH metabolites (9 -15). We identified and characterized JH diol phosphate (JHDP; compound 11; Fig. 1), one such polar metabolite, and suggested that it is the principal end product of JH I metabolism in M. sexta (11).We isolated and characterized JH diol kinase (JHDK) from the Malpighian tubules o...

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Section: Discussionmentioning

confidence: 99%

Section: Isolation and Purification Of Jhdkmentioning

confidence: 99%

Section: Enzyme Assaysmentioning

confidence: 99%

mentioning

confidence: 99%

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Juvenile Hormone Diol Kinase

Maxwell

Welch

Schooley

2002

Journal of Biological Chemistry

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“…In solitary insects, different stages of the female reproductive cycle (previtellogenesis, vitellogenesis, oviposition, and brood care) are linked and involve coupled physiological and behavioral changes (Finch and Rose, 1995;Lin and Lee, 1998;Miyatake, 2002). Juvenile hormone and ecdysone are key hormones controlling vitellogenesis in many insect species (Brownes, 1994;Hiremath and Jones, 1992;Ismail et al, 1998;Sankhon et al, 1999;Socha et al, 1991). In addition, they regulate behavioral transitions associated with changes in reproductive state such as the shift from foraging for nectar in previtello-genic females to protein foraging in vitellogenic individuals, as it occurs in the mosquito-Culex nigripalpus (Hancock and Foster, 2000).…”

Section: B Phenotypic Architecturementioning

confidence: 99%

The Development and Evolution of Division of Labor and Foraging Specialization in a Social Insect (Apis mellifera L.)

Page

Scheiner

Erber

et al. 2006

Current Topics in Developmental Biology

151

135

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How does complex social behavior evolve? What are the developmental building blocks of division of labor and specialization, the hallmarks of insect societies? Studies have revealed the developmental origins in the evolution of division of labor and specialization in foraging worker honeybees, the hallmarks of complex insect societies. Selective breeding for a single social trait, the amount of surplus pollen stored in the nest (pollen hoarding) revealed a phenotypic architecture of correlated traits at multiple levels of biological organization in facultatively sterile female worker honeybees. Verification of this phenotypic architecture in "wild-type" bees provided strong support for a "pollen foraging syndrome" that involves increased senso-motor responses, motor activity, associative learning, reproductive status, and rates of behavioral development, as well as foraging behavior. This set of traits guided further research into reproductive regulatory systems that were co-opted by natural selection during the evolution of social behavior. Division of labor, characterized by changes in the tasks performed by bees, as they age, is controlled by hormones linked to ovary development. Foraging specialization on nectar and pollen results also from different reproductive states of bees where nectar foragers engage in prereproductive behavior, foraging for nectar for self-maintenance, while pollen foragers perform foraging tasks associated with reproduction and maternal care, collecting protein.

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Cloning, partial purification and in vivo developmental profile of expression of the juvenile hormone epoxide hydrolase of Ctenocephalides felis

Keiser

Brandt

Silver

et al. 2002

Arch Insect Biochem Physiol

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cDNAs encoding two different epoxide hydrolases (nCfEH1 and nCfEH2) were cloned from a cDNA library prepared from the wandering larval stage of the cat flea, Ctenocephalides felis. Predicted translations of the open reading frames indicated the clones encoded proteins of 464 (CfEH1) and 465 (CfEH2) amino acids. These proteins have a predicted molecular weight of 53 kDa and a putative 22 amino acid N-terminal hydrophobic membrane anchor. The amino acid sequences are 77% identical, and both are homologous to previously isolated epoxide hydrolases from Manduca sexta, Trichoplusia ni, and Rattus norvegicus. Purification of native juvenile hormone epoxide hydrolase (JHEH) from unfed adult cat fleas generated a partially pure protein that hydrolyzed juvenile hormone III to juvenile hormone III-diol. The amino terminal sequence of this;50-kDa protein is identical to the deduced amino terminus of the protein encoded by the nCfEH1 clone. Affinity-purified rabbit polyclonal antibodies raised against Escherichia coli-expressed HisCfEH1 recognized a approximately 50-kDa protein present in the partially purified fraction containing JHEH activity. Immunohistochemistry experiments using the same affinity-purified rabbit polyclonal antibodies localized the epoxide hydrolase in developing oocytes, fat body, and midgut epithelium of the adult flea. The presence of JHEH in various flea life stages and tissues was assessed by Northern blot and enzymatic activity assays. JHEH mRNA expression remained relatively constant throughout the different flea larval stages and was slightly elevated in the unfed adult flea. JHEH enzymatic activity was highest in the late larval, pupal, and adult stages. In all stages and tissues examined, JHEH activity was significantly lower than juvenile hormone esterase (JHE) activity, the other enzyme responsible for JH catalysis.

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Juvenile hormone acid: Evidence for a hormonal function in induction of vitellogenin in larvae ofManduca sexta

Cited by 45 publications

References 40 publications

Juvenile Hormone Diol Kinase

Juvenile Hormone Diol Kinase

The Development and Evolution of Division of Labor and Foraging Specialization in a Social Insect (Apis mellifera L.)

Cloning, partial purification and in vivo developmental profile of expression of the juvenile hormone epoxide hydrolase of Ctenocephalides felis

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