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• W1551103852 abstract "Vol. 270, p. 28716 In this paper, we identified USF1 and USF2 as major components of complexes that bind to the fatty acid synthase (FAS) insulin response sequence (IRS) with gel shift assays, specific USF antibodies, and UV-cross-linking experiments. In addition, we found a down-regulation of the full-size 43-kDa USF1 at protein level in liver of fasted rats, and a 17-kDa USF1-related protein appeared to be of high content in liver of fasted rats and low in liver of refed rats. We have found that our observations of the regulation of USF1 protein are experimental artifacts caused by protein degradation. As described in the paper, nuclear extracts were prepared as previously described by Dignam et al.(1.Dignam J.D. Lebovitz R.M. Roeder R.G. Nucleic Acids Res. 1983; 11: 1475-1489Crossref PubMed Scopus (9153) Google Scholar), and nuclear extracts from liver of refed rats (RNE) were precipitated with 20-55% saturation of ammonium sulfate while the nuclear extracts from liver of fasted rats (FNE) were not subject to the ammonium sulfate precipitation step. When we repeated the RNE and FNE preparation in the presence of 0.2 mM EGTA and 10 μg/ml leupeptin without ammonium sulfate precipitation, we found both extracts showed the same DNA binding patterns consisting of only the slowest migrating Band 1 as the major band on gel shift assays (see Fig. 1). At the same time, we noticed a report by Watt and Molloy (2.Watt F. Molloy P.L. Nucleic Acids Res. 1993; 21: 5092-5100Crossref PubMed Scopus (93) Google Scholar) that m-calpain can specifically cleave USF1 leaving the binding and dimerization domains intact and capable of efficient DNA binding, and phenylmethylsulfonyl fluoride, which is the protease inhibitor used in the nuclear extract preparations in our paper, was incapable of blocking the USF1 digestion by m-calpain. The differences between FNE and RNE in Fig. 5 to Fig. 7 of our paper were, therefore, attributed to the preferential elimination of either the endogenous calcium or m-calpain in the rat liver nuclei by the ammonium sulfate precipitation. Being consistent with the data reported by Watt and Molloy(2.Watt F. Molloy P.L. Nucleic Acids Res. 1993; 21: 5092-5100Crossref PubMed Scopus (93) Google Scholar), we conclude that Band 2 contains the intermediate of USF1 digestion and the fastest migrating Band 3 results from more complete proteolysis of USF1 to peptides at a molecular size around 17 kDa. Only the slowest migrating Band 1 containing the intact 43-kDa USF1 is the major band present in both FNE and RNE. The findings that USF1 and USF2 are major components of complexes that bind FAS IRS and that USF2 was expressed at the same level in livers of fasted and refed rats still hold true. In view of the reanalysis of our data, we would like to withdraw the claim that protein levels of the 43-kDa USF1 and the 17-kDa USF1-related protein are regulated during fasting and refeeding." @default.
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• W1551103852 date "1996-03-01" @default.
• W1551103852 modified "2023-10-15" @default.
• W1551103852 title "Upstream stimulatory factors bind to insulin response sequence of the fatty acid synthase promoter. USF1 is regulated. A correction." @default.
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• W1551103852 doi "https://doi.org/10.1016/s0021-9258(17)45204-5" @default.
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