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• W2150280983 abstract "Fatty acid synthetase (FAS) is overexpressed in various tumor tissues, and its inhibition and/or malonyl-CoA accumulation have been correlated to apoptosis of tumor cells. It is widely recognized that both ω-3 and ω-6 polyunsaturated fatty acids (PUFAs) depress FAS expression in liver, although epidemiological and experimental reports attribute antitumor properties only to ω-3 PUFA. Therefore, we investigated whether lipogenic gene expression in tumor cells is differently regulated by ω-6 and ω-3 PUFAs. Morris hepatoma 3924A cells were implanted subcutaneously in the hind legs of ACI/T rats preconditioned with high-lipid diets enriched with linoleic acid or α-linolenic acid. Both-high lipid diets depressed the expression of FAS and acetyl-CoA carboxylase in tumor tissue, this effect correlating with a decrease in the mRNA level of their common sterol regulatory element binding protein-1 transcription factor. Hepatoma cells grown in rats on either diet did not accumulate malonyl-CoA. Apoptosis of hepatoma cells was induced by the α-linolenic acid-enriched diet but not by the linoleic acid-enriched diet.Therefore, in this experimental model, apoptosis is apparently independent of the inhibition of fatty acid synthesis and of malonyl-CoA cytotoxicity. Conversely, it was observed that apoptosis induced by the α-linolenic acid-enriched diet correlated with a decrease in arachidonate content in hepatoma cells and decreased cyclooxygenase-2 expression. Fatty acid synthetase (FAS) is overexpressed in various tumor tissues, and its inhibition and/or malonyl-CoA accumulation have been correlated to apoptosis of tumor cells. It is widely recognized that both ω-3 and ω-6 polyunsaturated fatty acids (PUFAs) depress FAS expression in liver, although epidemiological and experimental reports attribute antitumor properties only to ω-3 PUFA. Therefore, we investigated whether lipogenic gene expression in tumor cells is differently regulated by ω-6 and ω-3 PUFAs. Morris hepatoma 3924A cells were implanted subcutaneously in the hind legs of ACI/T rats preconditioned with high-lipid diets enriched with linoleic acid or α-linolenic acid. Both-high lipid diets depressed the expression of FAS and acetyl-CoA carboxylase in tumor tissue, this effect correlating with a decrease in the mRNA level of their common sterol regulatory element binding protein-1 transcription factor. Hepatoma cells grown in rats on either diet did not accumulate malonyl-CoA. Apoptosis of hepatoma cells was induced by the α-linolenic acid-enriched diet but not by the linoleic acid-enriched diet. Therefore, in this experimental model, apoptosis is apparently independent of the inhibition of fatty acid synthesis and of malonyl-CoA cytotoxicity. Conversely, it was observed that apoptosis induced by the α-linolenic acid-enriched diet correlated with a decrease in arachidonate content in hepatoma cells and decreased cyclooxygenase-2 expression. High expression of fatty acid synthetase (FAS) and upregulation of fatty acid synthesis are typical features of tumor tissues (1Alo P.L. Visca P. Marci A. Mangoni A. Botti C. Di Tondo U. Expression of fatty acid synthase (FAS) as a predictor of recurrence in stage I breast carcinoma patients.Cancer. 1996; 77: 474-482Crossref PubMed Scopus (278) Google Scholar, 2Visca P. Sebastiani V. Pizer E.S. Botti C. De Carli P. Filippi S. Monaco S. Alo P.L. Immunohistochemical expression and prognostic significance of FAS and GLUT1 in bladder carcinoma.Anticancer Res. 2003; 23: 335-339PubMed Google Scholar, 3Pizer E. Lax S. Kuhajda F. Pasternack G. Kurman R. Fatty acid synthase expression in endometrial carcinoma: correlation with cell proliferation and hormone receptors.Cancer. 1998; 83: 528-537Crossref PubMed Scopus (147) Google Scholar, 4Rashid A. Pizer E.S. Moga M. Milgraum L.Z. Zahurak M. Pasternack G.R. Kuhajda F.P. Hamilton S.R. Elevated expression of fatty acid synthase and fatty acid synthetic activity in colorectal neoplasia.Am. J. Pathol. 1997; 150: 201-208PubMed Google Scholar, 5Swinnen J.V. Roskams T. Joniau S. Van Poppel H. Oyen R. Baert L. Heyns W. Verhoeven G. Overexpression of fatty acid synthase is an early and common event in the development of prostate cancer.Int. J. Cancer. 2002; 98: 19-22Crossref PubMed Scopus (301) Google Scholar). Population studies of human cancer suggest that high FAS expression and tumor virulence are closely related (6Yang Y-A. Han W.F. Morin P.J. Chrest F.J. Pizer E.S. Activation of fatty acid synthesis during neoplastic transformation: role of mitogen-activated protein kinase and phosphatidylinositol 3-kinase.Exp. Cell Res. 2002; 279: 80-90Crossref PubMed Scopus (180) Google Scholar). Although the mechanisms underlying FAS overexpression in cancer are largely unknown, recent evidence (7Yang Y-A. Morin P.J. Han W.F. Chen T. Bornman D.M. Gabrielson E.W. Pizer E.S. Regulation of fatty acid synthase expression in breast cancer by sterol regulatory element binding protein-1c.Exp. Cell Res. 2003; 282: 132-137Crossref PubMed Scopus (134) Google Scholar, 8Swinnen J.V. Heemers H. Deboel L. Foufelle F. Heyns W. Verhoeven G. Stimulation of tumour-associated fatty acid synthase expression by growth factor activation of the sterol regulatory element-binding protein pathway.Oncogene. 2000; 19: 5173-5181Crossref PubMed Scopus (163) Google Scholar, 9Heemers H. Maes B. Foufelle F. Heyns W. Verhoeven G. Swinnen J.V. Androgens stimulate lipogenic gene expression in prostate cancer cells by activation of the sterol regulatory element-binding protein cleavage activating protein/sterol regulatory element-binding protein.Mol. Endocrinol. 2001; 15: 1817-1828Crossref PubMed Scopus (0) Google Scholar, 10Li J.N. Mahmoud M.A. Han W.F. Ripple M. Pizer E.S. Sterol regulatory element-binding protein-1 participates in the regulation of fatty acid synthase expression in colorectal neoplasia.Exp. Cell Res. 2000; 261: 159-165Crossref PubMed Scopus (84) Google Scholar) strongly suggests that, as in liver, FAS gene transcription in tumor cells is modulated by the sterol regulatory element binding protein-1 (SREBP-1). SREBP-1 is synthesized as an integral protein of the endoplasmic reticulum membranes. As its C-terminal regulatory domain interacts with SREBP cleavage-activating protein (SCAP), the SREBP/SCAP complex migrates to the Golgi membranes, where a two-step cleavage catalyzed by a serine protease [site-1 protease (S1P)] and a metalloprotease [site-2 protease (S2P)] is responsible for the release of the N-terminal sequence of SREBP-1 in the cytoplasm. At the nuclear level, mature SREBP-1, a transcription factor of the basic helix-loop-helix leucine zipper family, activates genes encoding FAS and other lipogenic enzymes by interacting with sterol response elements present in their promoter region (11Nohturfft A. DeBose-Boyd R.A. Scheek S. Goldstein J.L. Brown M.S. Sterols regulate cycling of SREBP cleavage-activating protein (SCAP) between endoplasmic reticulum and Golgi.Proc. Natl. Acad. Sci. USA. 1999; 96: 11235-11240Crossref PubMed Scopus (192) Google Scholar). Insulin and dietary carbohydrates activate FAS gene transcription by this mechanism, whereas dietary polyunsaturated fatty acids (PUFAs) of both ω-6 and ω-3 series negatively modulate FAS expression by depressing SREBP-1 mRNA level and reducing the cleavage of the native protein (12Worgall T.S. Sturley S.L. Seo T. Osborne T.F. Deckelbaum R.J. Polyunsaturated fatty acids decrease expression of promoters with sterol regulatory elements by decreasing levels of mature sterol regulatory element-binding protein.J. Biol. Chem. 1998; 273: 25537-25540Abstract Full Text Full Text PDF PubMed Scopus (260) Google Scholar, 13Moon Y.S. Latasa M-J. Griffin M.J. Sul H.S. Suppression of fatty acid synthase promoter by polyunsaturated fatty acids.J. Lipid Res. 2002; 43: 691-698Abstract Full Text Full Text PDF PubMed Google Scholar). Recently, it was found that pharmacological inhibitors of FAS are selectively cytotoxic to tumor cells in culture and in vivo (14Pizer E.S. Jackisch C. Wood F.D. Pasternack G.R. Davidson N.E. Kuhajda F.P. Inhibition of fatty acid synthesis induces programmed cell death in human breast cancer cells.Cancer Res. 1996; 56: 2745-2747PubMed Google Scholar, 15Kuhajda F.P. Pizer E.S. Li J.N. Mani N.S. Frehywot G.L. Townsend C.A. Synthesis and antitumor activity of an inhibitor of fatty acid synthase.Proc. Natl. Acad. Sci. USA. 2000; 97: 3450-3454Crossref PubMed Scopus (511) Google Scholar, 16Li J.N. Gorospe M. Chrest F.J. Kumaravel T.S. Evans M.K. Han W.F. Pizer E.S. Pharmacological inhibition of fatty acid synthase activity produces both cytostatic and cytotoxic effects modulated by p53.Cancer Res. 2001; 61: 1493-1499PubMed Google Scholar, 17Pizer E.S. Chrest F.J. DiGiuseppe J.A. Han W.F. Pharmacological inhibitors of mammalian fatty acid synthase suppress DNA replication and induce apoptosis in tumor cell lines.Cancer Res. 1998; 58: 4611-4615PubMed Google Scholar). In particular, the FAS inhibitors cerulenin (2S,3R-epoxy-4-oxo-7E,10E-dodecadienamide) and C75 (3-carboxy-4-octyl-2-methylenebutyrolactone) induce a rapid decline of fatty acid synthesis in tumor cells, with subsequent reduction of DNA synthesis, cell cycle arrest, and apoptosis (16Li J.N. Gorospe M. Chrest F.J. Kumaravel T.S. Evans M.K. Han W.F. Pizer E.S. Pharmacological inhibition of fatty acid synthase activity produces both cytostatic and cytotoxic effects modulated by p53.Cancer Res. 2001; 61: 1493-1499PubMed Google Scholar, 17Pizer E.S. Chrest F.J. DiGiuseppe J.A. Han W.F. Pharmacological inhibitors of mammalian fatty acid synthase suppress DNA replication and induce apoptosis in tumor cell lines.Cancer Res. 1998; 58: 4611-4615PubMed Google Scholar). The hypothesized link between the depression of de novo fatty acid synthesis and cytotoxicity to tumor cells is reinforced by the observation that ω-3 PUFAs possess anti-cancer properties. Indeed, ω-3 PUFAs, whose role as physiological modulators of FAS gene transcription is widely recognized, have been demonstrated to induce necrosis and apoptosis of tumor cells and to affect tumor growth and metastatic invasion (18Calviello G. Palozza P. Piccioni E. Maggiano N. Frattucci A. Franceschelli P. Bartoli G.M. Dietary supplementation with eicosapentaenoic and docosahexaenoic acid inhibit growth of Morris hepatocarcinoma 3924A in rats: effects on proliferation and apoptosis.Int. J. Cancer. 1998; 75: 699-705Crossref PubMed Scopus (124) Google Scholar, 19Diggle C.P. In vitro studies on the relationship between polyunsaturated fatty acids and cancer: tumour or tissue specific effects?.Prog. Lipids Res. 2002; 41: 240-253Crossref PubMed Scopus (60) Google Scholar, 20Hirose M. Masuda A. Ito N. Kamano K. Okuyama H. Effects of dietary perilla oil, soybean oil and safflower oil on 7,12-dimethylbenz[a]anthracene (DMBA) and 1,2-dimethyl-hydrazine (DMH)-induced mammary gland and colon carcinogenesis in female SD rats.Carcinogenesis. 1990; 11: 731-735Crossref PubMed Scopus (84) Google Scholar, 21Reddy B.S. Burill C. Rigotty J. Effect of diets high in omega-3 and omega-6 fatty acids on initiation and postinitiation stages of colon carcinogenesis.Cancer Res. 1991; 51: 487-491PubMed Google Scholar, 22Karmali R.A. Marsh J. Fuchs C. Effect of omega-3 fatty acids on growth of a rat mammary tumor.J. Natl. Cancer Inst. 1984; 73: 457-461Crossref PubMed Scopus (345) Google Scholar, 23Hudson E.A. Beck S.A. Tisdale M.J. Kinetics of the inhibition of tumour growth in mice by eicosapentaenoic acid-reversal by linoleic acid.Biochem. Pharmacol. 1993; 45: 2189-2194Crossref PubMed Scopus (40) Google Scholar, 24Sauer L.A. Dauchy R.T. The effect of omega-6 and omega-3 fatty acids on 3H-thymidine incorporation in hepatoma 7288CTC perfused in situ.Br. J. Cancer. 1992; 66: 297-303Crossref PubMed Scopus (68) Google Scholar). Nevertheless, it has to be pointed out that although PUFAs of both the ω-3 and ω-6 families act as negative modulators of FAS gene expression (12Worgall T.S. Sturley S.L. Seo T. Osborne T.F. Deckelbaum R.J. Polyunsaturated fatty acids decrease expression of promoters with sterol regulatory elements by decreasing levels of mature sterol regulatory element-binding protein.J. Biol. Chem. 1998; 273: 25537-25540Abstract Full Text Full Text PDF PubMed Scopus (260) Google Scholar, 13Moon Y.S. Latasa M-J. Griffin M.J. Sul H.S. Suppression of fatty acid synthase promoter by polyunsaturated fatty acids.J. Lipid Res. 2002; 43: 691-698Abstract Full Text Full Text PDF PubMed Google Scholar), only some of them retard tumor cell growth and induce cell death (18Calviello G. Palozza P. Piccioni E. Maggiano N. Frattucci A. Franceschelli P. Bartoli G.M. Dietary supplementation with eicosapentaenoic and docosahexaenoic acid inhibit growth of Morris hepatocarcinoma 3924A in rats: effects on proliferation and apoptosis.Int. J. Cancer. 1998; 75: 699-705Crossref PubMed Scopus (124) Google Scholar, 19Diggle C.P. In vitro studies on the relationship between polyunsaturated fatty acids and cancer: tumour or tissue specific effects?.Prog. Lipids Res. 2002; 41: 240-253Crossref PubMed Scopus (60) Google Scholar, 20Hirose M. Masuda A. Ito N. Kamano K. Okuyama H. Effects of dietary perilla oil, soybean oil and safflower oil on 7,12-dimethylbenz[a]anthracene (DMBA) and 1,2-dimethyl-hydrazine (DMH)-induced mammary gland and colon carcinogenesis in female SD rats.Carcinogenesis. 1990; 11: 731-735Crossref PubMed Scopus (84) Google Scholar, 21Reddy B.S. Burill C. Rigotty J. Effect of diets high in omega-3 and omega-6 fatty acids on initiation and postinitiation stages of colon carcinogenesis.Cancer Res. 1991; 51: 487-491PubMed Google Scholar, 22Karmali R.A. Marsh J. Fuchs C. Effect of omega-3 fatty acids on growth of a rat mammary tumor.J. Natl. Cancer Inst. 1984; 73: 457-461Crossref PubMed Scopus (345) Google Scholar, 23Hudson E.A. Beck S.A. Tisdale M.J. Kinetics of the inhibition of tumour growth in mice by eicosapentaenoic acid-reversal by linoleic acid.Biochem. Pharmacol. 1993; 45: 2189-2194Crossref PubMed Scopus (40) Google Scholar, 24Sauer L.A. Dauchy R.T. The effect of omega-6 and omega-3 fatty acids on 3H-thymidine incorporation in hepatoma 7288CTC perfused in situ.Br. J. Cancer. 1992; 66: 297-303Crossref PubMed Scopus (68) Google Scholar, 25Horrobin D.F. Essential fatty acids, lipid peroxidation, and cancer.in: Horrobin D.F. ω-6 Essential Fatty Acids. Wiley-Liss, New York1990: 351-378Google Scholar). In light of this evidence, a cause-and-effect relationship between the depression of fatty acid synthesis and tumor cell cytotoxicity appears unlikely. This critical observation is reinforced by recent data demonstrating that a depression of fatty acid synthesis per se is not responsible for apoptosis of tumor cells. Indeed, 5-(tetradecyloxy)-2-furoic acid, an inhibitor of acetyl-CoA carboxylase (ACC), depresses fatty acid synthesis but is not cytotoxic to human breast cancer cells (26Pizer E.S. Thupari J. Han W.F. Pinn M.L. Chrest F.J. Frehywot G.L. Townsend C.A. Kuhajda F.P. Malonyl-coenzyme A is a potent mediator of cytotoxicity induced by fatty acid synthase inhibition in human breast cancer cells and xenografts.Cancer Res. 2000; 60: 213-218PubMed Google Scholar). Because both FAS and ACC inhibitors depress fatty acid synthesis but only FAS inhibitors induce malonyl-CoA accumulation in the cytoplasm, it has been inferred that malonyl-CoA mediates cytotoxicity induced by FAS inhibitors (26Pizer E.S. Thupari J. Han W.F. Pinn M.L. Chrest F.J. Frehywot G.L. Townsend C.A. Kuhajda F.P. Malonyl-coenzyme A is a potent mediator of cytotoxicity induced by fatty acid synthase inhibition in human breast cancer cells and xenografts.Cancer Res. 2000; 60: 213-218PubMed Google Scholar). This last hypothesis has been taken as the starting point for the present investigation, which aims to examine the possibility that dietary ω-3 PUFAs, but not ω-6 PUFAs, selectively affect apoptosis of hepatoma cells by increasing their cytoplasmic malonyl-CoA level. In addition to the malonyl-CoA hypothesis, we also considered the possibility that the cytotoxicity of ω-3 PUFAs to hepatoma cells might depend on the modulation of the mechanisms involved in eicosanoid production (27Bagga D. Wang L. Farias-Eisner R. Glaspy J.A. Reddy S.T. Differential effects of prostaglandin derived from omega-6 and omega-3 polyunsaturated fatty acids on COX-2 expression and IL-6 secretion.Proc. Natl. Acad. Sci. USA. 2003; 100: 1751-1756Crossref PubMed Scopus (537) Google Scholar). [α-32P]UTP (specific activity, 800 Ci/mmol) was obtained from Amersham Biosciences Europe (Milan, Italy). Rabbit polyclonal antibody against the N-terminal region of SREBP-1 (H-160: sc-8984) was purchased from Santa Cruz Biotechnology, Inc. (Santa Cruz, CA). Horseradish peroxidase-conjugated anti-rabbit immunoglobulin secondary antibody and all other chemicals were obtained from Sigma-Aldrich Co. (Milan, Italy). The animal-use protocol was approved by the Istituto Superiore della Sanità (Italian National Health Institute), Rome, Italy. Thirty-six male inbred ACI/T rats (∼200 g body weight), randomly divided into three groups, were housed individually in cages and placed in light-cycling rooms with alternating 12 h periods of light and darkness. All animals had free access to food and water. The first group was fed a standard pellet chow diet (Altromin-Rieper, Bolzano, Italy). The diet of the second and third groups was enriched with polyunsaturated lipids containing an excess of ω-6 and ω-3 PUFAs, respectively. The ω-6 PUFA-enriched diet was prepared by milling equal amounts of standard pellet and sunflower seeds (SS diet), whereas the ω-3 PUFA-enriched diet was prepared by milling the standard pellet with an equal amount of linseeds (LS diet). The resulting powders were pelleted again. The gross composition of the three diets is reported in Table 1. The fatty acid content of the three experimental diets was evaluated by gas chromatographic analysis of the fatty acid methyl esters obtained by transmethylation of the extracted lipids using methyleptadecanoate as an internal standard. Gas chromatographic analysis of fatty acid methyl esters was performed using a Carlo Erba Instruments (Milan, Italy) model HRGC 5300 gas chromatograph equipped with an SP-2330 capillary column (30 m × 0.25 mm; Supelco, Inc., Bellefonte, PA) and a flame ionization detector.TABLE 1Composition of experimental dietsNutrientsDietsCSSLSCarbohydrates (mg/g pellet)521.8343.1286.8 Lipids49.1210.7212.8 Proteins204.7211.2217.2 Fiber44.690.8104.3Energy (kJ/g)15.8219.1618.42Fatty acid distribution (%) 16:015.87.88.3 18:02.53.85.0 18:1 ω-922.724.119.7 18:2 ω-651.563.421.1 18:3 ω-35.80.745.7 20:5 ω-30.50.10.1 22:6 ω-30.60.10.1Rats were fed either standard pellet chow (C) or high-lipid diets obtained by milling equal weights of standard pellet with sunflower seeds (SS) or linseeds (LS). The powdered mixtures were pelleted again and analyzed for composition. Fatty acid distribution in the three diets was assessed by gas chromatographic analysis of fatty acid methyl esters. Open table in a new tab Rats were fed either standard pellet chow (C) or high-lipid diets obtained by milling equal weights of standard pellet with sunflower seeds (SS) or linseeds (LS). The powdered mixtures were pelleted again and analyzed for composition. Fatty acid distribution in the three diets was assessed by gas chromatographic analysis of fatty acid methyl esters. After 10 days of dietary conditioning, rats were subjected to subcutaneous transplantation of fast-growing Morris hepatoma 3924A cells, as previously described (18Calviello G. Palozza P. Piccioni E. Maggiano N. Frattucci A. Franceschelli P. Bartoli G.M. Dietary supplementation with eicosapentaenoic and docosahexaenoic acid inhibit growth of Morris hepatocarcinoma 3924A in rats: effects on proliferation and apoptosis.Int. J. Cancer. 1998; 75: 699-705Crossref PubMed Scopus (124) Google Scholar). In particular, hepatoma excised from anaesthetized donors was trimmed of fat, muscle, connective tissue, blood, and obvious necrotic tissues and then gently homogenized in 10 vol of 0.9% NaCl. One milliliter aliquots of the cell suspension were inoculated subcutaneously in both hind legs of ACI/T acceptor rats. Tumors became palpable at 11 to 12 days after transplantation. On day 19 after transplantation, rats were killed, tumors were excised, and specimens of each tumor were separately frozen at −80°C for future analyses. The percentage of apoptotic cells was determined using the TUNEL technique (18Calviello G. Palozza P. Piccioni E. Maggiano N. Frattucci A. Franceschelli P. Bartoli G.M. Dietary supplementation with eicosapentaenoic and docosahexaenoic acid inhibit growth of Morris hepatocarcinoma 3924A in rats: effects on proliferation and apoptosis.Int. J. Cancer. 1998; 75: 699-705Crossref PubMed Scopus (124) Google Scholar, 28Gavriely Y. Sherman Y. Sasson S.A. Identification of programmed cells death in situ via specific labelling DNA fragmentation.J. Cell Biol. 1992; 119: 493-501Crossref PubMed Scopus (9167) Google Scholar). Aliquots of the frozen tumor tissue (about 0.5 g fresh weight) were homogenized in 10 vol of 0.25 M sucrose. Lipids were extracted according to Folch, Lees, and Sloane-Stanley (29Folch J. Lees M. Sloane-Stanley G.M. A simplified method for the isolation and purification of total lipids from animal tissues.J. Biol. Chem. 1957; 226: 497-509Abstract Full Text PDF PubMed Google Scholar), and fatty acid methyl esters obtained by acid-catalyzed transmethylation were analyzed by gas-liquid chromatography, as described above. Fatty acid composition of phosphatidylcholine was analyzed according to the same procedure after chromatographic isolation of the lipid class on SiO2 plates using chloroform-methanol-water (65:25:4, v/v/v) as a developing mixture. Total RNA was extracted from frozen specimens of liver and hepatoma tissues (about 0.5 g fresh tissue) by the cesium chloride purification procedure (30Chirgwin J.M. Przybyla A.E. MacDonald R.J. Rutter W.J. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease.Biochemistry. 1979; 18: 5294-5299Crossref PubMed Scopus (16652) Google Scholar). For RNA probes, fragments of mRNA encoding the proteins listed in Table 2 were amplified by reverse transcriptase-PCR from ACI/T rat liver RNA using the primers listed in the same table (31–45). The amplified products were subcloned into pCR 2.1 TOPO vector (Invitrogen) and verified by nucleotide sequencing. After plasmid linearization, antisense RNAs were transcribed with [α-32P]UTP (800 Ci/mmol) using T7 RNA polymerase (Promega).TABLE 2Sequences of PCR primers used for cloning cDNA fragmentsCopy RNA ProbePrimer PairPrimer SequencesNational Center for Biotechnology Information Accession NumberPCR ProductRef.bpSREBP-15′5′-AACCAAGACAGTGACTTCC-3′L1699522031Kim J. Tontoz P. Spiegelman B. Add1: a novel helix-loop-helix protein associated with adipocyte determination and differentiation.Mol. Cell. Biol. 1993; 13: 4753-4759Crossref PubMed Scopus (536) Google Scholar3′5′-ACGGGTACATCTTTACAGC-3′SREBP-1a5′5′-ATGGACGAGCTGCCTTCGGTGAGGCGGCT-3′NM_011480 (mouse)24732Inoue J. Sato R. A novel splicing isoform of mouse sterol regulatory element-binding protein-1 (SREBP-1).Biosci. Biotechnol. Biochem. 1999; 63: 243-245Crossref PubMed Scopus (4) Google Scholar3′5′-CCAGAGAGGAGCCCAGAGAAGCAG-3′SREBP-1c5′5′-GCGCGGACGACGGAGCCAT-3′L1699517231Kim J. Tontoz P. Spiegelman B. Add1: a novel helix-loop-helix protein associated with adipocyte determination and differentiation.Mol. Cell. Biol. 1993; 13: 4753-4759Crossref PubMed Scopus (536) Google Scholar3′5′-GCAGGAGAAGAGAAGCTCTC-3′Fatty acid synthase5′5′-TTGCCCGAGTCAGAGAACC-3′M7676724133Amy C.M. Witkowski A. Naggert J. Williams B. Randhawa Z. Smith S. Molecular cloning and sequencing of cDNAs encoding the entire rat fatty acid synthase.Proc. Natl. Acad. Sci. USA. 1989; 86: 3114-3118Crossref PubMed Scopus (134) Google Scholar3′5′-CGTCCACAATAGCTTCATAGC-3′Acetyl-CoA carboxylase5′5′-GTCATGCCTCCGAGAACC-3′J0380818034Lopez-Casillas F. Bai D.H. Luo X.N. Kong I.S. Hermodson M.A. Kim K.H. Structure of the coding sequence and primary amino acid sequence of acetyl-coenzyme A carboxylase.Proc. Natl. Acad. Sci. USA. 1988; 85: 5784-5788Crossref PubMed Scopus (138) Google Scholar3′5′-GCCAATCCACTCGAAGACC-3′ATP citrate lyase5′5′-GATCAAACGTCGAGGAAAGC-3′J0521023035Elshourbagy N.A. Near J.C. Kmetz P.J. Sathe G.M. Southan C. Strickler J.E. Gross M. Young J.F. Wells T.N. Groot P.H. Rat ATP citrate-lyase. Molecular cloning and sequence analysis of a full-length cDNA and mRNA abundance as a function of diet, organ and age.J. Biol. Chem. 1990; 265: 1430-1435Abstract Full Text PDF PubMed Google Scholar3′5′-CCCTTCATGGTGGAACAGG-3′Peroxisome proliferator activated receptor-α5′5′-ACTGGATGACAGTGACATTTCC-3′NM_01319623836Goettlicher M. Widmark E. Li Q. Gustafsson J.A. Fatty acid activate a chimera of the clofibric acid-activated receptor and glucocorticoid receptor.Proc. Natl. Acad. Sci. USA. 1992; 89: 4653-4657Crossref PubMed Scopus (800) Google Scholar3′5′-CTTGATGACCTGCACGAGC-3′Carnitine palmitoyltransferase-15′5′-CAGAACACGGCAAAATGAGC-3′L0773622737Esser V. Britton C.H. Weis B.C. Foster D.W. McGarry J.D. Cloning, sequencing and expression of a cDNA encoding rat liver carnitine palmitoyltransferase I. Direct evidence that a single polypeptide is involved in inhibitor interaction and catalytic function.J. Biol. Chem. 1993; 268: 5817-5822Abstract Full Text PDF PubMed Google Scholar3′5′-GAGGTTGACAGCAAATCCTG-3′Acyl-CoA oxidase5′5′-CCACATATGACCCCAAGACC-3′J0275221938Miyazawa S. Hayashi H. Hijikata M. Ishii N. Kagamiyama H. Osumi T. Hashimoto T. Complete nucleotide sequence of cDNA and predicted sequence of rat acyl-CoA oxidase.J. Biol. Chem. 1987; 262: 8131-8137Abstract Full Text PDF PubMed Google Scholar3′5′-GATATCCCCGACAGTGATGC-3′SREBP-1 cleavage-activating protein5′5′-CTGAGAGACAGCTCAGGGACC-3′U67060 (Cricetus)30239Hua X. Nohturfft A. Goldstein J.L. Brown M.S. Sterol resistance in CHO cells traced to point mutation in SREBP cleavage-activating protein.Cell. 1996; 87: 415-426Abstract Full Text Full Text PDF PubMed Scopus (427) Google Scholar3′5′-GATGGTGTACGAGACCGTCCT-3′Site-1 protease5′5′-TGCTCACACTTGAAGATCACC-3′AF09482129740Seidah N.G. Mowla S.J. Hamelin J. Mamarbachi A.M. Benjannet S. Toure B.B. Basak A. Munzer J.S. Marcinkiewicz J. Zhong M. Barale J.C. Lazure C. Murphy R.A. Chretien M. Marcinkiewicz M. Mammalian subtilisin/kexin isozyme SKI-1. A widely expressed proprotein convertase with a unique cleavage specificity and cellular localization.Proc. Natl. Acad. Sci. USA. 1999; 96: 1321-1326Crossref PubMed Scopus (249) Google Scholar3′5′-GACATTAGCACCTGTGTATCC-3′Site-2 protease5′5′-TGCAACTTATATCACCAGTCCA-3′AF01961120041Rawson R.B. Zelenski N.G. Nijhawan D. Ye J. Sakai J. Hasan M.T. Chang T.Y. Brown M.S. Goldstein J.L. Complementation cloning of S2P, a gene encoding a putative metalloprotease required for intramembrane cleavage of SREBPs.Mol. Cell. 1997; 1: 47-57Abstract Full Text Full Text PDF PubMed Scopus (395) Google Scholar3′5′-CACAAAAAGGCCTCTGGGTC-3′C/EBPα5′5′-GGCTGGAGCCCCTGTACGAGC-3′NM_01252420942Lincoln A.J. Williams S.C. Johnson P.F. A revised sequence of the rat C/EBP gene.Genes Dev. 1994; 8: 1131-1132Crossref PubMed Scopus (14) Google Scholar3′5′-GCAGTGTGCGATCTGGAACTGC-3′C/EBPβ5′5′-CCTCTTCGCCGACGACTACG-3′NM_02412521643Descombes P. Chojkier M. Lichtsteiner S. Falvey E. Schibler U. LAP, a novel member of the C/EBP gene family, encodes a liver-enriched transcriptional activator protein.Genes Dev. 1990; 4: 1541-1551Crossref PubMed Scopus (420) Google Scholar3′5′-CAGGGCGAACGGGAAGCCG-3′C/EBPδ5′5′-AGAGCGCCATCGACTTCAGC-3′NM_01315428044Kageyama R. Sasai Y. Nakanishi S. Molecular characterization of transcription factors that bind to the cAMP responsive region of the substance P precursor gene. cDNA cloning of a novel C/EBP-related factor.J. Biol. Chem. 1991; 266: 15525-15531Abstract Full Text PDF PubMed Google Scholar3′5′-CCAAGCTCACCACTGTCTGC-3′Cyclooxygenase-25′5′-AAGATAGTGATCGAAGACTACG-3′S6772225445Feng L. Sun W. Xia Y. Tang W.W. Chanmugam P. Soyoola E. Wilson C.B. Hwang D. Cloning two isoforms of rat cyclooxygenase: differential regulation of their expression.Arch. Biochem. Biophys. 1993; 307: 361-368Crossref PubMed Scopus (458) Google Scholar3′5′-GAATGACTCAACAAAGTGAGC-3′C/EBP, CCAAT enhancer binding protein; SREBP-1, sterol regulatory element binding protein-1. Open table in a new tab C/EBP, CCAAT enhancer binding protein; SREBP-1, sterol regulatory element binding protein-1. As preliminary tests indicated that β-actin mRNA level in hepatoma cells is significantly affected by dietary manipulations, 18S mRNA was used as an internal control for RNase protection assays (46Blanquicett C. Johnson M.R. Heslin M. Diasio R.B. Housekeeping gene variability in normal and carcinomatous colorectal and liver tissues: applications in pharmacogenomic gene expression studies.Anal. Biochem. 2002; 303: 209-214Crossref PubMed Scopus (102) Google Scholar). RNA samples were subjected to RNase protection assay using the RPA III™ kit (Ambion, Inc., Austin, TX), 10 μg of RNA from ACI/T rat liver or hepatoma, 100,000 cpm of the specific antisense probe, and 2,000–20,000 cpm of antisense pTRI RNA 18S (80 bp protected fragment; Ambion) with a 5- to 50-fold lower specific activity, to give an 18S signal comparable to that of the test mRNAs. After digestion with RNase A/T1, the protected fragments were separated on 8 M urea/6.0% polyacrylamide gels. The gels were dried and subjected to quantitative analysis using an Instant Imager autoradiography system (Packard BioScience Co., IL). Frozen specimens from ACI/T rat liver and tumor tissue were homogenized in 7% SDS. Aliquots of the homoge" @default.
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• W2150280983 cites W1573804402 @default.
• W2150280983 cites W1595100801 @default.
• W2150280983 cites W1598643430 @default.
• W2150280983 cites W1603478517 @default.
• W2150280983 cites W1967608697 @default.
• W2150280983 cites W1969933703 @default.
• W2150280983 cites W1971797498 @default.
• W2150280983 cites W1971999946 @default.
• W2150280983 cites W1972527774 @default.
• W2150280983 cites W1986261554 @default.
• W2150280983 cites W1986712359 @default.
• W2150280983 cites W1987231965 @default.
• W2150280983 cites W2000066670 @default.
• W2150280983 cites W2000183234 @default.
• W2150280983 cites W2008887768 @default.
• W2150280983 cites W2012551512 @default.
• W2150280983 cites W2019319173 @default.
• W2150280983 cites W2020587158 @default.
• W2150280983 cites W2023595441 @default.
• W2150280983 cites W2026628125 @default.
• W2150280983 cites W2030795161 @default.
• W2150280983 cites W2032691440 @default.
• W2150280983 cites W2040735050 @default.
• W2150280983 cites W2042207719 @default.
• W2150280983 cites W2045016464 @default.
• W2150280983 cites W2045182776 @default.
• W2150280983 cites W2053388585 @default.
• W2150280983 cites W2054918431 @default.
• W2150280983 cites W2054947177 @default.
• W2150280983 cites W2058031342 @default.
• W2150280983 cites W2059010575 @default.
• W2150280983 cites W2060331274 @default.
• W2150280983 cites W2060333964 @default.
• W2150280983 cites W2081458493 @default.
• W2150280983 cites W2095885440 @default.
• W2150280983 cites W2116470680 @default.
• W2150280983 cites W2119577005 @default.
• W2150280983 cites W2122391469 @default.
• W2150280983 cites W2129011493 @default.
• W2150280983 cites W2138282645 @default.
• W2150280983 cites W2138302361 @default.
• W2150280983 cites W2142137533 @default.
• W2150280983 cites W2144764527 @default.
• W2150280983 cites W2145995281 @default.
• W2150280983 cites W2149563543 @default.
• W2150280983 cites W2168526937 @default.
• W2150280983 cites W2317973866 @default.
• W2150280983 cites W2318568264 @default.
• W2150280983 cites W2339179515 @default.
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