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.

A DNA-binding protein for the Surcophagu lectin gene, ATBP (A/T-stretches-binding protein) was purified to homogeneity from the nuclear extract of NIH-Sape-4 cells. The molecular mass of ATBP determined under denaturing conditions was 53 kDa, but its native molecular mass estimated by gel-filtration chromatography was 430 kDa, suggesting that it is an octamer of the 53-kDa subunit. This protein bound to at least three DNA fragments from the Surcophaga lectin gene, two of them are in the 5'-upstream region and the other is in a region containing an intron. These fragments are very AT rich and inlaid with stretches of A or T residues (A/T stretches). ATBP was found to have affinity for poly[d(A-T)]. These results suggest that ATBP binds to A/T stretches in the three DNA fragments from this gene. Furthermore, longer DNA was found to be bound more effectively, suggesting that an octamer of the 53-kDa subunit has multiple binding sites for the DNA fragments and requires a relatively long DNA sequence for binding.Sarcophaga lectin is a galactose-binding protein purified from the hemolymph of Sarcophuga peregrina larvae [l]. When the body wall of larvae is injured, the fat body starts to synthesize this lectin and secretes it into the hemolymph 121. This lectin has been shown to be a defense protein participating in the elimination of foreign substances introduced into the abdominal cavity [3]. The same lectin also seems to play a role in the differentiation of imaginal discs because, when imaginal discs were cultured in the presence of 20-hydroxyecdysone, they synthesized this lectin and secreted it into the culture medium, and when this secreted Surcophaga lectin was blocked with its antibody or hapten sugar, galactose, differentiation of the discs was inhibited significantly [4]. Thus, it is likely that this Sarcophaga lectin has roles in both defense and development [5].We are interested in regulation of the expression of the Sarcophagu lectin gene, because it is expressed both in an acute phase (body injury and/or bacterial infection) and during development (in the early embryonic and pupal stages) [6]. To understand the mechanism of its gene expression, it is necessary to identify transcription factors that interact with its promoter region. Previously, we purified a 59-kDa protein that binds to a nuclear factor-lcB-like motif located in the 5'-upstream region of the Sarcophaga lectin gene from the nuclear extract of NIH-Sape-4 cells [7], an embryonic cell line of Sarcophaga expressing the Surcophaga lectin gene constitutively [8, 91. This paper describes the purification and characterization of a novel DNA-binding protein for the Sarcophaga lectin gene in the same nuclear extract of NIH-Sape-4 cells. ConCorrespondence to S. Natori, Faculty of Pharmaceutical Sciences, University of Tokyo, Bunkyo-ku, Tokyo, Japan 11 3Note. The nucleotide sequence of the Sarcophaga lectin gene has been deposited in the GSDB, DDBJ, EMBL and NCBI nucleotide sequence detabases with the accession number D14870. trary to the 59-kDa pr...

<b><i>Introduction:</i></b> <i>Helicobacter pylori</i> eradication is expected to significantly change the prevalence of Barrett’s esophagus (BE). However, few reports on this relationship exist. We analyzed the risk factors of BE using the current consensus on length of BE considering <i>H. pylori</i> infection status. <b><i>Methods:</i></b> We analyzed 10,122 individuals (5,962 men; mean age = 52.9 ± 9.9 years) who had undergone esophagogastroduodenoscopy as part of a medical checkup. Correlations among factors including <i>H. pylori</i> infectious status, endoscopic findings, and BE ≥1 cm were analyzed. <b><i>Results:</i></b> Prevalence of BE, long-segment BE, and esophageal adenocarcinoma was 22.5%, 0.014%, and 0%, respectively. Logistic regression analysis showed that the risk factors for BE were hiatal hernia (odds ratio [OR]: 2.89 [2.59–3.24]), female sex (OR: 0.52 [0.46–0.59]), social drinking (OR:0.77 [0.68–0.87]), <i>H. pylori</i> eradication therapy (OR: 1.34 [1.19–1.51]), proton pump inhibitor (PPI) use (OR: 1.52 [1.18–1.96]), bile reflux (OR: 1.18 [1.04–1.33]), age ≥50 years (OR: 1.13 [1.02–1.26]), and nonsteroidal anti-inflammatory drug (NSAID) use (OR: 1.29 [1.02–1.62]). Although reflux esophagitis (RE) was more common in <i>H. pylori</i>-negative patients (17.2%) than in those after <i>H. pylori</i> eradication therapy (11.8%, <i>p</i> &#x3c; 0.00001), the latter was correlated with BE, disputing RE as a strong risk factor for BE. Therefore, we conducted a subgroup analysis; most of the risk factors except for PPI use (<i>p</i> = 0.75), H2-receptor antagonist use (<i>p</i> = 0.078), and atrophic gastritis absence (<i>p</i> = 0.72) were positively correlated with BE after <i>H. pylori</i> eradication therapy compared with <i>H. pylori</i>-negative status. <b><i>Conclusions:</i></b> <i>H. pylori</i> eradication, bile reflux, PPI use, and NSAID use were risk factors for BE along with hiatal hernia, male sex, and older age.

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