The fate of the larval storage protein calliphorin during adult development of Calliphora vicina

Levenbook, L.; Bauer, Adelia C.

doi:10.1016/0020-1790(84)90086-6

Cited by 105 publications

(51 citation statements)

References 29 publications

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“…Since holometabolous insects do not feed during metamorphosis, they depend on material previously accumulated during the larval period. Amino acids and energy are supplied by proteins that have been selectively taken up by the fat body before pupation (Levenbook and Bauer, 1984). Most of the incorporated haemolymph proteins belong to the class of hexamerins, hemocyanin-related insect proteins named according to their composition of six identical or closely related subunits (Telfer and Kunkel, 1991).…”

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confidence: 99%

Developmentally Controlled Cleavage of the Calliphora Arylphorin Receptor and Posttranslational Action of the Steroid Hormone 20‐Hydroxyecysone

Burmester

Scheller

1997

European Journal of Biochemistry

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In response to a rise in ecdysteroid titre, fat body cells of insect larvae take up storage proteins from the haemolymph by receptor-mediated endocytosis. Here we show that the receptor responsible for incorporation of the major haemolymph protein arylphorin of the blowfly, Calliphora vicina, is subject to an unusual posttranslational processing that involves three distinct cleavage steps. After the removal of a 17-amino-acid signal peptide, a receptor precursor of 141 kDa is released. Before reaching the cell surface, the precursor is cleaved a second time, giving rise to the active 92-kDa arylphorin receptor, plus a 48-kDa peptide. The function of this 48-kDa peptide may be the prevention of premature ligandreceptor interaction in the endoplasmic reticulum. 20-Hydroxyecdysone initiates a third cleavage step of the arylphorin receptor, which results in a 62-kDa arylphorin binding protein and a 30-kDa peptide. Contrary to the standard model of steroid hormone action, the process which give rise to receptor cleavage can be induced by 20-hydroxyecdysone in vivo and in vitro even in absence of protein biosynthesis.

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confidence: 99%

Developmentally Controlled Cleavage of the Calliphora Arylphorin Receptor and Posttranslational Action of the Steroid Hormone 20‐Hydroxyecysone

Burmester

Scheller

1997

European Journal of Biochemistry

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“…It is subsequently stored in protein granules and used to build adult proteins during metamorphosis (Levenbook and Bauer, 1984). It has been demonstrated in C. vicina, as well as in many other insects, that a rise in ecdysteroid titre is responsible for induction of hexamerin uptake (e.g., Collins, 1969;Lepesant et al, 1978;Tojo et al, 1981;Ueno and Natori, 1982;Burmester and Scheller, 1995a).…”

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confidence: 99%

Conservation of Hexamerin Endocytosis in Diptera

Burmester

Scheller

1997

European Journal of Biochemistry

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In cyclorrhaphan Diptera at least two different types of haemolymph proteins exist which belong to the class of hexamerins. In the last larval instar of Calliphora vicina, the highly aromatic hexamerin, arylphorin, and the second hexamerin, PII, make up about 90% of haeniolymph proteins. Both of these proteins are selectively taken up by the fat body cells at the end of larval life and share a common membrane-bound receptor. In addition, hexamerins and possible hexamerin receptors of Calliphora vicina, Calliphora vomitoria, Drosophila melanogaster, Ceratitis capitata, Sarcophaga bullata, Musca domestica and Protophormia terraenovae were investigated. Uptake of arylphorin by the larval fat bodies of Calliphoru vicina as well asarylphorin-receptor binding can be competed in vitro by haemolymph from other Diptera. Therefore, hexamerin-receptor binding must be conserved among related cyclorrhaphan Diptera and between different types of hexamerins within a species. As the degree of competition is in good agreement with the presumed phylogenetic distances between these species, the method described here provides a simple tool to estimate evolutionary distances.

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“…We have reported previously [5] that the arylphorins drosophilin, calliphorin, and manducin are crosslinked in vitro in a reaction mixture with the sclerotizing agent N-acetyldopamin (NADA) [6 ] or N-/?-alanyldopamin (NBAD) [7] and monophenol monooxigenase. It thus appeared that arylphorins eventually may play a role in cuticle sclerotization, in addition to their function as storage proteins (see [3] and references cited there in). However, before the biological relevance of arylphorins for cuticle sclerotization can be eval uated in detail, it is necessary to prove a participa tion in this process by an experimental approach.…”

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confidence: 99%

“…Thus, an unambiguous chemical identification of a crosslink partial structure has not been reported with full details. Likewise, very little is known on the identity of structural polypeptides participating in the formation of crosslinks.Applications of immunological [2], radiochem ical [2,3], and histochemical (K. Scheller, personal …”

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confidence: 99%

Incorporation of Radiolabeled Tyrosine, N-Acetyldopamine, N-β-Alanyldopamine, and the Arylphorin Manducin into the Sclerotized Cuticle of Tobacco Hornworm (Manduca sexta) Pupae

Grün

Peter

1984

Zeitschrift Für Naturforschung C

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Sclerotization of the cuticle depends in many insects on the oxidation of 1 ,2 -diphenolic substrates in the outer parts of the integument. Reactive intermediates such as o-quinones, /?-quinonemethides or free radicals, which may be generated during the oxidative transformations are thought to effect covalent crosslinking of structural proteins by Michael-type additions and/or free radical poly merizations (for a recent review see [1]). Chem ical models are apparently consistent with such theories. However, structures of crosslinks in sclerotized cuticle are essentially unknown due to the difficulties encountered in attempts to isolate soluble deriv atives of native structures from the exoskeleton. Thus, an unambiguous chemical identification of a crosslink partial structure has not been reported with full details. Likewise, very little is known on the identity of structural polypeptides participating in the formation of crosslinks.Applications of immunological [2], radiochem ical [2,3], and histochemical (K. Scheller, personal

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The fate of the larval storage protein calliphorin during adult development of Calliphora vicina

Cited by 105 publications

References 29 publications

Developmentally Controlled Cleavage of the Calliphora Arylphorin Receptor and Posttranslational Action of the Steroid Hormone 20‐Hydroxyecysone

Developmentally Controlled Cleavage of the Calliphora Arylphorin Receptor and Posttranslational Action of the Steroid Hormone 20‐Hydroxyecysone

Conservation of Hexamerin Endocytosis in Diptera

Incorporation of Radiolabeled Tyrosine, N-Acetyldopamine, N-β-Alanyldopamine, and the Arylphorin Manducin into the Sclerotized Cuticle of Tobacco Hornworm (Manduca sexta) Pupae

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