The regulation of major haemolymph protein synthesis: Changes in mRNA content during the development of Bombyx mori larvae

Bosquet, G.; Guillet, Christelle; Calvez, B.; Chavancy, Gérard

doi:10.1016/0020-1790(89)90006-1

Cited by 18 publications

(6 citation statements)

References 27 publications

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“…Since the fat body is the major source of hemolymph proteins, a corresponding activity in its mRNA synthesis can be assumed (Bosquet et al, 1989). Juvenile hormone is not only the main factor in stimulating protein synthesis (Keeley, 1978), but also in enhancing the export of hemolymph proteins by the fat body (Kanost et al, 1990).…”

Section: Discussionmentioning

confidence: 99%

Concentration of hemolymph proteins during postembryonic worker development of Africanized honey bees in Brazil and Carniolans in Europe

Michelette

Engels

1995

Apidologie

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Summary — The profiles of hemolymph protein content during postembryonic development of honey bees (Apis mellifera) were determined for the first time. Larval and pupal worker stages of Africanized honey bees in Brazil and Carniolans in Germany were studied. A rapid increase in protein concentration was found in the late larval stages, followed by a decrease in prepupae and a minimum amount near the pupal moult period. In the early pupal stages, the protein concentration increased again, and then decreased until adult eclosion. Only the first protein peak in spinning L5 was more pronounced in the Africanized honey bees. No differences between the hemolymph protein profiles of Africanized bees and Carniolans could be detected during pupal development. The duration of several larval and pupal stages was shorter in Africanized than in Carniolan workers. The data reflect the general characteristics of the Africanized biotype reared in tropical conditions exhibiting accelerated patterns of development and lower body weight at emergence in comparison to the European Apis subspecies reared in temperate conditions. The ontogenetic patterns described for hemolymph protein concentration in preimaginal honey bee development are also discussed, specifically in regard to the regulation of metamorphosis in holometabolous insects.

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Section: Discussionmentioning

confidence: 99%

Concentration of hemolymph proteins during postembryonic worker development of Africanized honey bees in Brazil and Carniolans in Europe

Michelette

Engels

1995

Apidologie

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“…It is the most abundant among 30K proteins (30Kc6, 30Kc12, 30Kc19, 30Kc21, and 30Kc23) in hemolymph with molecular weights of about 30 kDa [ 2 ]. These “30K proteins” are synthesized in fat body cells and accumulate in the hemolymph during the fifth instar larval to early pupal stages [ 3 , 4 ]. They are then transferred from the hemolymph to fat body cells during metamorphosis from larva to pupa and are deposited there until use [ 5 , 6 ].…”

Section: Introductionmentioning

confidence: 99%

Dimerization of 30Kc19 protein in the presence of amphiphilic moiety and importance of Cys‐57 during cell penetration

Park

Sohn

Yeo

et al. 2014

Biotechnology Journal

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Recently, the recombinant 30Kc19 protein, originating from silkworm hemolymph of Bombyx mori has attracted attention due to its cell-penetrating property and potential application as a protein delivery system. However, this observation of penetration across cell membrane has raised questions concerning the interaction of the protein-lipid bilayer. Here, we report a dimerization propensity of the 30Kc19 protein in the presence of amphiphilic moieties; sodium dodecyl sulfate (SDS) or phospholipid. Native PAGE showed that the 30Kc19 monomer formed a dimer when SDS or phospholipid was present. In the glutathione-S-transferase (GST) pull-down assay, supplementation of the 30Kc19 protein to mammalian cell culture medium showed dimerization and penetration; due to phospholipids at the cell membrane, the main components of the lipid bilayer. Mutagenesis was performed, and penetration was observed by 30Kc19 C76A and not 30Kc19 C57A, which meant that the presence of cysteine at position 57 (Cys-57) is involved in dimerization of the 30Kc19 at the cell membrane during penetration. We anticipate application of the native 30Kc19 protein with high cell-penetrating efficiency for delivery of cargos to various cell types. The intracellular cargo delivery using the 30Kc19 protein is a non-virus derived (e.g. TAT) delivery method, which can open up new approaches for the delivery of therapeutics in bioindustries, such as pharma- and cosmeceuticals.

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“…During the fifth instar larval to early pupal stages, these "30 K proteins" are synthesized in fat body cells and accumulated in the hemolymph [24,25]. During metamorphosis from larva to pupa, these proteins are http://dx.doi.org/10.1016/j.procbio.2015.03.008 1359-5113/© 2015 Elsevier Ltd. All rights reserved.…”

Section: Introductionmentioning

confidence: 99%

Enhancement of human erythropoietin production in Chinese hamster ovary cells through supplementation of 30Kc19-30Kc6 fusion protein

Park

Choi

Lee

et al. 2015

Process Biochemistry

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The regulation of major haemolymph protein synthesis: Changes in mRNA content during the development of Bombyx mori larvae

Cited by 18 publications

References 27 publications

Concentration of hemolymph proteins during postembryonic worker development of Africanized honey bees in Brazil and Carniolans in Europe

Concentration of hemolymph proteins during postembryonic worker development of Africanized honey bees in Brazil and Carniolans in Europe

Dimerization of 30Kc19 protein in the presence of amphiphilic moiety and importance of Cys‐57 during cell penetration

Enhancement of human erythropoietin production in Chinese hamster ovary cells through supplementation of 30Kc19-30Kc6 fusion protein

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