Manduca sexta structure

Gruber, G., Radermacher, M., Ruiz, T., Godovac-Zimmermann, J., Canas, B., Kleine-Kohlbrecher, D., Huss, M., Harvey, W. R., and Wieczorek, H. (2000). Three-dimensional structure and subunit topology of the Vi ATPase from Manduca sexta midgut. Biochemistry 39, 8609-8616. 

Taylor, B. (1969). Geographical range and circadian rhythms. Nature 222, 296-297. Tolbert L. and Hildebrand J. (1981) Organization and synaptic ultrastructure of glomeruli in the antennal lobes of the moth Manduca sexta a study using thin sections and freeze-structure. Phil. Trans. R. Soc. London Ser B 213, 279-301. 

Lee K. and Strausfeld N. J. (1990). Structure, distribution and number of surface sensilla and their receptor cells on the olfactory appendage of the male moth Manduca sexta. J. Neurocytol. 19, 519-538. 

Shields V. D. C. and Hildebrand J. G. (1999a) Fine structure of antennal sensilla of the female sphinx moth, Manduca sexta (Lepidoptera Sphingidae). I. Trichoid and basiconic sensilla. Can. J. Zool. 77, 290-301. 

Eclosion hormone (EH) is a novel insect neurohormone that acts on the nervous system to trigger a stereotyped set of behaviors. The gene that encodes EH was isolated from the moth Manduca sexta and has provided a molecular means to determine the structure of EHs from a variety of insects. Only a few (2-4) neurons in the CNS produce EH and these cells appear to release the peptide both locally within the CNS and systemically into the blood. The former is responsible for causing the behavioral responses while the latter acts on various peripheral targets. 

Svoboda and co-workers (Svoboda and Robbins, 1967 1968 Svoboda et al., 1967 1969) found that triparanol, 2-(4-chlorophenyl)-l-[4-(2-diethylamino-ethoxy)phenyl]-l-(4-tolyl) ethanol and 22,25-diazacholesterol (99) inhibit sterol reductase and also disrupt the normal growth and development of the larvae of tobacco homworm, Manduca sexta. Both compounds are known as inhibitors of steroid biosynthesis in vertebrates. 22,25-DiazacholesteroI is a hypocholeste-rolaemic agent acting as a competitive antagonist of cholesterol. A similar activity was found later for 25-azacholesterol (100). For the determination of the minimum structural requirements of activity, Svoboda and Robbins synthesised and tested... 

Structure-activity studies are an indirect method to investigate a possible interaction of AKH peptides with their receptor proteins. For various members of the AKH family a vast body of literature has accumulated, employing bioassays such as lipid mobilization in locusts and the tobacco hommoth Manduca sexta, carbohydrate mobilization in various cockroach species, the activation of phosphorylase in the larvae of M. sexta, or the inhibition of fatty acid synthesis in the fat body of locusts [10, 33, 37, 53]. Contrary to most other invertebrate neuropeptides, the insect members of the AKH family do not have a core sequence which is essential for potency, however, the N-terminal pGlu residue and the C-terminal amide are important, as well as the aromatics at position 4 and 8. To achieve full efficacy, all amino acids are apparently important. There is also no superagonist found and also no inhibitor. 

Cecropins. Cecropins (169) were isolated from the larval hemolymph of the giant silkworm moth, Hyalophora cecropia, on the basis of their antibacterial activity subsequent to bacterial injection. Cecropins are also produced by Drosophila (170) and the larva of the tobacco homworm, Manduca sexta (110). Similar compounds called sarcotoxins (171) are produced by the flesh fly, Sarcophaga. Cecropins (169) are specific for prokaryotic cell lysis in contrast to melittin, which lyses eukaryotic cell membranes as well. Cecropins are characterized structurally by a concentration of basic... 

An aqueous extract of RJ produced hypoglycemia when injected into larvae of Manduca sexta. The application of specific radioimmunoassay to the partially purified extract showed that RJ contains several insulin-like peptides, the major immunoreactive component of which had an apparent mol. wt similar to that of bovine insulin. These results suggested the existence of a peptide in the honeybee having both biological and structural similarities to vertebrate insulin [90]. Partially purified extracts from honeybees (Apis mellifera), and extracts from their separated heads, cross-reacted in a porcine insulin radioimmunoassay. The active extracts displaced porcine insulin from rat liver insulin receptors and showed insulin-like activity with rat adipocytes that could be abolished with bovine insulin antiserum. The presence of an insulin... 

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