The soluble proteins of developing: Calliphora erythrocephala, particularly calliphorin, and similar proteins in other insects
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Cited by (122)
Nutrition regulates the expression of storage proteins in Bombyx mori via insulin-like/FoxO signaling pathway
2022, Insect Biochemistry and Molecular BiologyCitation Excerpt :In the 1960s, a serum protein was found in the fat body of the Calliphora vicina larva. This protein, named the storage protein (SP), exists in a granular form in the fat body and is also found in high concentrations in the hemolymph (Munn et al., 1971; Munn and Greville, 1969). Following the discovery of SPs in Calliphora vicina, other insects, especially species of Lepidoptera and Diptera, have been discovered to contain similar proteins.
Metabolic adjustment of the larval fat body in Hermetia illucens to dietary conditions
2017, Journal of Asia-Pacific EntomologyCitation Excerpt :First isolated from Calliphora erythrocephala, the fly hexamerin (calliphorin or LSP-1) is produced by the fat body and constitutes the main soluble protein in the hemolymph (Munn et al., 1969). Later on, LSP-1 was described in other Diptera species (Munn and Greville, 1969). A second hexamerin, LSP-2, is present in this insect order as well.
Lysine acetylation stabilizes SP2 protein in the silkworm Bombyx mori
2016, Journal of Insect PhysiologyCitation Excerpt :Storage proteins (SPs) are widespread in Lepidoptera and Diptera and belong to the same protein family with hemocyanin in Arthropods (Adachi et al., 2005). SP2 is one of the storage proteins that is highly expressed in silkworm hemolymph (Munn and Greville, 1969). We first confirmed that the increased lysine acetylation level by TSA could improve the survival of H2O2-treated BmN cells via up-regulation of the protein level of SP2, which contains anti-apoptosis activity.
Cloning and characterization of a riboflavin-binding hexamerin from the larval fat body of a lepidopteran stored grain pest, Corcyra cephalonica
2016, Comparative Biochemistry and Physiology Part - B: Biochemistry and Molecular BiologyCitation Excerpt :Insect hexamerins are predominantly synthesized and expressed in the fat body and secreted into the hemolymph (Burmester, 1999; Telfer and Kunkel, 1991; Wang and Haunerland, 1991). Hexamerins are primarily known to function as storage proteins that provide energy for non-feeding periods (Munn et al., 1967; Munn and Greville, 1969) but recent evidence demonstrate them as a versatile molecule. Hexamerins may transport hormones such as ecdysteroids (20HE) (Enderle et al., 1983) and juvenile hormone (JH) (Braun and Wyatt, 1996).
Expression and evolution of hexamerins from the tobacco hornworm, Manduca sexta, and other Lepidoptera
2015, Insect Biochemistry and Molecular BiologyCitation Excerpt :This agrees with the analyses of the genomes, which show no orthologs of the lepidopteran hexamerins in other insect orders. When the hexamerins were discovered in the larvae of various holometabolous insects, they were considered mainly as storage proteins that provide energy and amino acids for metamorphosis (Burmester, 1999a; Munn et al., 1967; Munn and Greville, 1969; Telfer and Kunkel, 1991). This view is, in fact, supported in M. sexta for the arylphorins, MRSP, MMRSP, and Hex6, which show massive accumulation of their mRNAs in the fifth larval instar just before pupation (Fig. 3).
A hexamerin protein, AgSP-1, is associated with diapause in the boll weevil
2002, Journal of Insect Physiology