Humoral mediator‐dependent activation of the <i>Sarcophaga</i> lectin gene

Shiraishi, Akihiro; Natori, Shunji

doi:10.1016/0014-5793(88)80409-5

Cited by 13 publications

(4 citation statements)

References 8 publications

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“…Therefore, the larval hemolymph contains some factor essential for activation of the Surcophuga lectin gene. Moreover, a ligation experiment suggested that this factor is produced in the anterior part of the larval body in response to body injury [8].…”

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confidence: 99%

A novel mechanism of Sarcophaga lectin gene expression

Sugiyama

Natori

1991

European Journal of Biochemistry

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The Sarcophaga lectin gene, an acute‐phase‐responsive protein of Sarcophaga, was found to be activated when the fat body was incubated in phosphate‐buffered insect saline (10 mM NaH2PO4/Na2HPO4, pH 6.2, 2 mM NaHCO3, 1 mM MgCl2, 5 mM KCl, 1 mM CaCl2 and 120 mM NaCl). This activation was selectively suppressed by addition of 2‐mercaptoethanol. 2‐Mercaptoethanol did not affect the transcription directly, suggesting that the oxidation of the sulfhydryl group of a fat‐body protein is required for activation of the Sarcophaga lectin gene. This oxidation reaction seemed to occur immediately when the fat body was incubated in vitro, and once this reaction was initiated, 2‐mercaptoethanol no longer inhibited transcription of the Sarcophaga lectin gene. This gene is known to be activated when the larval‐body wall of Sarcophaga is injured. It is suggested that the Sarcophaga lectin gene is activated via this novel mechanism on its acute‐phase expression in vivo.

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confidence: 99%

A novel mechanism of Sarcophaga lectin gene expression

Sugiyama

Natori

1991

European Journal of Biochemistry

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“…On the basis of the results of a ligation experiment, we have suggested that a humoral factor released from the anterior part of the larva stimulates the synthesis of Sarcophaga lectin in the posterior fat body when the larval body wall is injured (40,41). Thus, LPS-responsive cells and defense protein-producing cells may be different, the former producing a mediator in response to LPS that activates the latter cells.…”

Section: Discussionmentioning

confidence: 99%

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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“…It is not certain whether all NIH-Sape-4 cells respond to LPS, because these cells are not derived from a single cell but are a mixture of multiple cell types. On the basis of the results of a ligation experiment, we have suggested that a humoral factor released from the anterior part of the larva stimulates the synthesis of Sarcophaga lectin in the posterior fat body when the larval body wall is injured (40,41). Thus, LPS-responsive cells and defense protein-producing cells may be different, the former producing a mediator in response to LPS that activates the latter cells.…”

Section: Discussionmentioning

confidence: 99%

Purification and Characterization of a 59-Kilodalton Protein That Specifically Binds to NF-κB-Binding Motifs of the Defense Protein Genes of Sarcophaga peregrina (the Flesh Fly)

Kobayashi

Matsui

Kubo

et al. 1993

Molecular and Cellular Biology

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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 beta-1,3-glucan. The 5' upstream regions of the defense protein genes were found to have common motifs showing similarity to the mammalian NF-kappa B-binding consensus sequence. A protein with affinity to the NF-kappa B-binding motif of the Sarcophaga lectin promoter was identified and purified to near homogeneity. This 59-kDa protein also bound to the NF-kappa B-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. peregrina.

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Humoral mediator‐dependent activation of the Sarcophaga lectin gene

Cited by 13 publications

References 8 publications

A novel mechanism of Sarcophaga lectin gene expression

A novel mechanism of Sarcophaga lectin gene expression

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).

Purification and Characterization of a 59-Kilodalton Protein That Specifically Binds to NF-κB-Binding Motifs of the Defense Protein Genes of Sarcophaga peregrina (the Flesh Fly)

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