Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression
Complete nucleotide sequences of major plasma protein genes of Bombyx mori
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Cited by (27)
Enhancement of human erythropoietin production in Chinese hamster ovary cells through supplementation of 30Kc19-30Kc6 fusion protein
2015, Process BiochemistryCitation Excerpt :Silkworm hemolymph consists of a group of structurally related proteins with a molecular weight of approximately 30 kDa, including 30Kc6, 30Kc12, 30Kc19, 30Kc21, and 30Kc23. 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 transferred from the hemolymph to fat body cells and are deposited there until use [26,27].
Identification and characterization of a novel cell-penetrating peptide of 30Kc19 protein derived from Bombyx mori
2014, Process BiochemistryCitation Excerpt :These proteins have molecular weights of around 30 kDa, and 30Kc19 protein is the most abundant among 30K proteins (30Kc6, 30Kc12, 30Kc19, 30Kc21 and 30Kc23) in the hemolymph [37]. During the 5th instar larva to early pupa stage, these 30K proteins are synthesized in fat body cells and accumulate in the hemolymph [38,39]. They are then transferred from the hemolymph to fat body cells during metamorphosis from larva to pupa, and are deposited there until later use [40,41].
Identification of a functional element in the promoter of the silkworm (bombyx mori) fat body-specific gene Bmlp3
2014, GeneCitation Excerpt :Interestingly, changes in the level of 30 K protein mRNA in the fat body reflect changes in the hemolymph concentration of 30 K proteins, indicating that transcription is the major mode of 30 K protein gene regulation. B. mori hemolymph proteins have proven to be good models for studying the developmental regulation of gene expression (Izumi et al., 1981; Mori et al., 1991a, 1991b). The availability of the complete genome sequence of B. mori provides a unique opportunity to identify genes encoding 30 K proteins and determining how they are developmentally regulated.
A protein delivery system using 30Kc19 cell-penetrating protein originating from silkworm
2012, BiomaterialsCitation Excerpt :30Kc19 is a member of the 30K protein family (30Kc6, 30Kc12, 30Kc19, 30Kc21 and 30Kc23), which is a family of similar structured proteins found in silkworm hemolymph that have molecular weights around 30 kDa [19,20]. These proteins are synthesized in fat body cells and accumulate in the hemolymph during the final instar (5th instar) larvae and the early pupal stage [21,22]. During metamorphosis from larvae to pupae, the 30K proteins are transferred from the hemolymph to fat body cells where they are deposited [23,24].
The homeodomain protein PBX participates in JH-related suppressive regulation on the expression of major plasma protein genes in the silkworm, Bombyx mori
2005, Insect Biochemistry and Molecular BiologyInsect cytokine growth-blocking peptide triggers a termination system of cellular immunity by inducing its binding protein
2003, Journal of Biological ChemistryCitation Excerpt :By a combination of primary PCR using these primers and following 5′- and 3′-RACE PCR, GBP-binding protein cDNA was isolated and sequenced (Fig. 3A). The deduced 430-amino acid sequence with a molecular mass of 49.5 kDa is a novel protein containing a C-terminal region displaying limited homology to several insect lipoproteins such as 30k-lipoprotein (28) and microvitellogenin (29) (Fig. 3B). Further, this protein appears not to have a signal peptide and transmembrane domain.
The sequence data in this paper have been submitted to the EMBL/Genbank Data Libraries under the accession numbers X54734 (21G1) and X54736 (19G1).