Novel peature of expression of the sarcotoxin IA gene in development of Sarcophaga peregrina

Nanbu, Rika; Nakajima, Yuki; Ando, Kentaro; Natori, Shunji

doi:10.1016/0006-291x(88)90427-5

Cited by 35 publications

(16 citation statements)

References 13 publications

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“…Previously, we demonstrated that the sarcotoxin IA gene was transiently activated during the early pupal stage in Sarcophaga (18). To prove that sarcotoxin IA is in fact present in the pupae, we performed immunoblotting using pupal extracts prepared from pupae harvested at various developmental stages.…”

Section: Detection Of a 26-kda Protein That Cross-reacts Immunologicamentioning

confidence: 99%

A Novel Protease in the Pupal Yellow Body of Sarcophaga peregrina (Flesh Fly)

Nakajima

Tsuji

Homma

et al. 1997

Journal of Biological Chemistry

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We purified a novel serine protease with a molecular mass of 26 kDa from Sarcophaga pupae. This protease appeared almost exclusively in the yellow body, an organ that develops temporarily in the pupae of dipteran insects and expands to form the adult midgut by engulfing the larval midgut. cDNA analysis revealed that this protease consists of 239 amino acid residues and has significant structural similarity with bovine trypsin (about 40% sequence identity). The 26-kDa protease gene was transiently activated in 1-day-old pupae. The protease was found to cross-react immunologically with antibody against sarcotoxin IA, an antibacterial protein produced by this insect. It is suggested that this protease participates in the decomposition of the larval midgut in the yellow body during metamorphosis.

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Section: Detection Of a 26-kda Protein That Cross-reacts Immunologicamentioning

confidence: 99%

A Novel Protease in the Pupal Yellow Body of Sarcophaga peregrina (Flesh Fly)

Nakajima

Tsuji

Homma

et al. 1997

Journal of Biological Chemistry

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“…It was observed that transient mRNA accumulated at both embryonic and pupal stages (109). Accumulation of mRNA from genes that encode two other defense peptides (sarcotoxin I and sarcotoxin II) supported the observation of expression of this class of genes during development in naive (non acute-phase) insects (4,118).…”

Section: Immune Responsementioning

confidence: 55%

Differential Gene Expression in Insects: Transcriptional Control

Harshman¹,

James

1998

Annu. Rev. Entomol.

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Studies on transcriptional control of gene expression play a pivotal role in many areas of biology. In non-Drosophilid insects, the cuticle, chorion, immune response, silk gland, storage proteins, and vitellogenin are foci for advances in basic research on promoter elements and transcription factors. Insects offer other advantages for gene regulation studies, including the availability of applied problems. In non-Drosophilid insects, the most serious problem for transcriptional control studies is the lack of homologous in vivo expression systems. Once this deficiency is addressed, the full impact of research on transcription control will be realized throughout the field of entomology.

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“…We have detected transient expressions of various defense protein genes examined, except the sarcotoxin II genes in the early embryonic and pupal stages of Sarcophaga species (29,30,49). Thus, the same factor probably participates in the programmed expressions of these genes during development, although the triggering stimulus is different from that of their acute-phase expressions.…”

Section: Discussionmentioning

confidence: 91%

Purification and characterization of a 59-kilodalton protein that specifically binds to NF-kappa B-binding motifs of the defense protein genes of Sarcophaga peregrina (the flesh fly).

Kobayashi¹,

Matsui²,

Kubo³

et al. 1993

Mol. Cell. Biol.

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Various Sarcophaga peregrina (flesh fly) defense protein genes were shown to be activated when NIH-Sape-4 cells were cultured with bacterial lipopolysaccharides or 0-1,3-glucan. The 5' upstream regions of the defense protein genes were found to have common motifs showing similarity to the mammalian NF-KB-binding consensus sequence. A protein with affinity to the NF-KB-binding motif of the Sarcophaga lectin promoter was identified and purified to near homogeneity. This 59-kDa protein also bound to the NF-KB-binding motifs of other defense protein genes, e.g., sarcotoxin I and sarcotoxin II genes. This protein was found in both the cytoplasmic and the nuclear fractions of the cells, and it appeared to migrate from the cytoplasm to the nucleus on treatment of the cells with lipopolysaccharides. This 59-kDa protein is probably a transcriptional regulator of the genes for defense proteins of S. peregnna.

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Novel peature of expression of the sarcotoxin IA gene in development of Sarcophaga peregrina

Cited by 35 publications

References 13 publications

A Novel Protease in the Pupal Yellow Body of Sarcophaga peregrina (Flesh Fly)

A Novel Protease in the Pupal Yellow Body of Sarcophaga peregrina (Flesh Fly)

Differential Gene Expression in Insects: Transcriptional Control

Purification and characterization of a 59-kilodalton protein that specifically binds to NF-kappa B-binding motifs of the defense protein genes of Sarcophaga peregrina (the flesh fly).

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