A novel germline mutation in Peroxisome Proliferator-Activated Receptor γ gene associated with large intestine polyp formation and dyslipidemia (209 visite)
Bba-Gen Subjects (ISSN: 0925-4439, 0006-3002, 1570-9639), 2010; 1802(6): 572-581.
Tipo di articolo: Journal Article,
Impact factor: 2.773, Impact factor a 5 anni: 2.751
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-77952240564&partnerID=40&md5=f0a185472554530c6ce54fec0f6a1265
Parole chiave: Colorectal Cancer, Dyslipidemia, Loss-Of-Function Mutation, Peroxisome Proliferator-Activated Receptor, High Density Lipoprotein Cholesterol, Insulin, Low Density Lipoprotein Cholesterol, Peroxisome Proliferator Activated Receptor Gamma, Triacylglycerol, Adult, Aged, Amino Acid Substitution, Article, Cancer Localization, Cell Proliferation, Cholesterol Blood Level, Clinical Article, Colon Carcinogenesis, Colon Polyp, Colonoscopy, Controlled Study, Female, Gene Mutation, Genetic Association, Germ Line, Glucose Blood Level, Histopathology, Human, Human Cell, Human Tissue, Hypertension, In Vitro Study, In Vivo Study, Insulin Blood Level, Ligand Binding, Lipid Metabolism, Liver Metastasis, Loss Of Function Mutation, Non Insulin Dependent Diabetes Mellitus, Nucleotide Sequence, Obesity, Priority Journal, Protein Expression, Protein Function, Triacylglycerol Blood Level, Wild Type, Adenocarcinoma, Adolescent, 80 And Over, Animals, Base Sequence, Binding Sites, Cercopithecus Aethiops, Colonic Neoplasms, Cos Cells, Dna Primers, Germ-Line Mutation, Intestinal Polyps, Loss Of Heterozygosity, Middle Aged, Models, Molecular, Nih 3t3 Cells, Pedigree, Ppar Gamma, Recombinant Proteins, Transfection, Young Adult,
Affiliazioni:
*** IBB - CNR ***
Department of Biological and Environmental Sciences, University of Sannio, Via Port'Arsa, 11, 82100 Benevento, Italy
Institute of Genetics and Biophysics, A. Buzzati-Traverso CNR, Via P. Castellino, 113, 80131 Napoli, Italy
Department of Biochemistry and Medical Biotechnologies, University of Naples Federico II, Via S. Pansini, 5, 80131 Napoli, Italy
Fatebenefratelli Hospital, Division of Medical Oncology, Viale Principe di Napoli, 82100 Benevento, Italy
Department of Chemistry, University of Naples Federico II, Monte S. Angelo, 80100 Napoli, Italy
Riferimenti:
Francis, G.A., Fayard, E., Picard, F., Auwerx, J., Nuclear receptors and the control of metabolism (2003) Ann. Rev. Physiol., 65, pp. 261-31
Spiegelman, B.M., PPARγ: adipogenic regulator and thiazolidinedione receptor (1998) Diabetes, 47, pp. 507-514
Feige, J.N., Gelman, L., Michalik, L., Desvergne, B., Wahli, W., From molecular action to physiological outputs: peroxisome proliferator-activated receptors are nuclear receptors at the crossroads of key cellular functions (2006) Prog. Lipid Res., 45, pp. 120-159
Willson, T.M., Lambert, M.H., Kliewer, S.A., Peroxisome proliferator-activated receptor γ and metabolic disease (2001) Annu. Rev. Biochem., 70, pp. 341-367
Knouff, C., Auwerx, J., Peroxisome proliferator-activated receptor-γ calls for activation in moderation: lessons from genetics and pharmacology (2004) Endocr. Rev., 25, pp. 899-918
Sarraf, P., Mueller, E., Smith, W.M., Wright, H.M., Kum, J.B., Aaltonen, L.A., de la Chapelle, A., Eng, C., Loss-of-function mutations in PPARγ associated with human colon cancer (1999) Mol Cell, 3, pp. 799-804
Ristow, M., Muller-Wieland, D., Pfeiffer, A., Krone, W., Kahn, C.R., Obesity associated with a mutation in a genetic regulator of adipocyte differentiation (1998) N. Engl. J. Med., 339, pp. 953-959
Grommes, C., Landreth, G., Heneka, M.T., Antineoplastic effects of peroxisome proliferator activated receptor γ agonists (2004) Lancet Oncol., 7, pp. 419-429
Sabatino, L., Casamassimi, A., Peluso, G., Barone, M.V., Capaccio, D., Migliore, C., Monelli, P., Colantuoni, V., A novel peroxisome proliferator-activated receptor γ isoform with dominant negative activity generated by alternative splicing (2005) J. Biol. Chem., 280, pp. 26517-26525
Barroso, I., Gurnell, M., Crowley, V.E., Agostini, M., Schwabe, J.W., Soos, M.A., Maslen, G.L., O'Rahilly, S., Dominant negative mutations in human PPARγ associated with severe insulin resistance, diabetes mellitus and hypertension (1999) Nature, 402, pp. 880-883
Savage, D.B., Tan, G.D., Acerini, C.L., Jebb, S.A., Agostini, M., Gurnell, M., Williams, R.L., O'Rahilly, S., Human metabolic syndrome resulting from dominant-negative mutations in the nuclear receptor peroxisome proliferator-activated receptor γ (2003) Diabetes, 52, pp. 910-917
Peverali, F.A., Ramqvist, T., Saffrich, R., Pepperkok, R., Barone, M.V., Philipson, L., Regulation of G1 progression by E2A and Id helix-loop-helix proteins (1994) EMBO J., 13, pp. 4291-4301
Barone, M.V., Courtneidge, S.A., Myc but not Fos rescue of PDGF signaling block caused by kinase-inactive Src (1995) Nature, 378, pp. 509-512
Pancione, M., Forte, N., Sabatino, L., Tomaselli, E., Parente, D., Febbraro, A., Colantuoni, V., Reduced γ-catenin and peroxisome proliferator-activated receptor γ expression levels are associated with colorectal cancer metastatic progression: correlation with tumor-associated macrophages, cyclooxygenase 2, and patient outcome (2009) Hum. Pathol., 40, pp. 714-725
Yeh, J.J., Marsh, D.J., Zedenius, J., Dwight, T., Delbridge, L., Robinson, B.G., Eng, C., Fine-structure deletion mapping of 10q22-24 identifies regions of loss of heterozygosity and suggests that sporadic follicular thyroid adenomas and follicular thyroid carcinomas develop along distinct neoplastic pathways (1999) Genes Chromosomes Cancer, 26, pp. 322-328
Kinzler, K.W., Vogelstein, B., Lessons from hereditary colorectal cancer (1996) Cell, 87, pp. 159-170
Gupta, R.A., Sarraf, P., Mueller, E., Brockman, J.A., Prusakiewicz, J.J., Eng, C., Willson, T.M., DuBois, R.N., Peroxisome proliferator-activated receptor γ mediated differentiation: a mutation in colon cancer cells reveals divergent and cell type-specific mechanisms (2003) J. Biol. Chem., 278, pp. 22669-22677
Girnun, G.D., Smith, W.M., Drori, S., Sarraf, P., Mueller, E., Eng, C., Nambiar, P., Spiegelman, B.M., APC-dependent suppression of colon carcinogenesis by PPARγ (2002) Proc. Natl. Acad. Sci. U.S.A., 99, pp. 13771-13776
Teresi, R.E., Shaiu, C.W., Chen, C.S., Chatterjee, V.K., Waite, K.A., Eng, C., Increased PTEN expression due to transcriptional activation of PPARγ by lovastatin and rosiglitazone (2006) Int. J. Cancer, 118, pp. 2390-2398
Annicotte, J.S., Iankova, I., Miard, S., Fritz, V., Sarruf, D., Abella, A., Berthe, M.L., Iborra, F., Peroxisome proliferator-activated receptor γ regulates E-cadherin expression and inhibits growth and invasion of prostate cancer (2006) Mol. Cell. Biol., 26, pp. 7561-7574
Wang, D., Dubois, R.N., Peroxisome proliferator-activated receptors and progression of colorectal cancer (2008) PPAR Res, p. 931074
Pascual, G., Fong, A.L., Ogawa, S., Gamliel, A., Li, A.C., Perissi, V., Rose, D.W., Glass, C.K., A SUMOylation-dependent pathway mediates transrepression of inflammatory response genes by PPARγ (2005) Nature, 437, pp. 759-763
Iatropoulos, M.J., Williams, G.M., Proliferation markers (1996) Exp. Toxicol. Pathol., 48, pp. 175-181
Platt, A.M., Mowat, A.M., Mucosal macrophages and the regulation of immune responses in the intestine (2008) Immunol. Lett., 119, pp. 22-31
Mori, M., Shimono, R., Adachi, Y., Matsuda, H., Kuwano, H., Sugimachi, K., Ikeda, M., Saku, M., Transitional mucosa in human colorectal lesions (1990) Dis. Colon Rectum, 33, pp. 498-501
Gampe, R.T., Montana, V.G., Lambert, M.H., Miller, A.B., Bledsoe, R.K., Milburn, M.V., Kliever, S.A., Xu, E.H., Asymmetry in the PPARγ /RXRγ crystal structure reveals the molecular basis of heterodimerization among nuclear receptors (2000) Mol. Cell, 5, pp. 545-555
Uppenberg, J., Svensson, C., Jaki, M., Bertilsson, G., Jendeberg, L., Berkenstam, A., Crystal structure of the ligand binding domain of the human nuclear receptor PPARγ (1998) J. Biol. Chem., 273, pp. 31108-31112
Petersen, M.T., Jonson, P.H., Petersen, S.B., Amino acid neighbours and detailed conformational analysis of cysteines in proteins (1999) Protein Eng., 12, pp. 535-548
Kraulis, P.J., MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures (1991) J. Appl. Crystallogr., 24, pp. 946-950
Rogler, G., Significance of anti-inflammatory effects of PPARγ agonists? (2006) Gut, 55, pp. 1067-1069
Alberici, P., Gaspar, C., Franken, P., Gorski, M.M., de Vries, I., Scott, R.J., Ristimäki, A., Fodde, R., Smad4 haploinsufficiency: a matter of dosage (2008) Pathogenetics, 1, pp. 2-12
Eng, C., Schneider, K., Fraumeni, J.F., Li, F.P., Third international workshop on collaborative interdisciplinary studies of p53 and other predisposing genes in Li-Fraumeni syndrome (1997) Cancer Epidemiol. Biomarkers Prev., 6, pp. 379-383
Russell-Swetek, A., West, A.N., Mintern, J.E., Jenkins, J., Rodriguez-Galindo, C., Ribeiro, R., Zambetti, G.P., Identification of a novel TP53 germline mutation E285V in a rare case of paediatric adrenocortical carcinoma and choroid plexus carcinoma (2008) J. Med. Genet., 45, pp. 603-606
Ikezoe, T., Miller, C.W., Kawano, S., Heaney, A., Williamson, E.A., Hisatake, J., Green, E., Koeffler, H.P., Mutational analysis of the peroxisome proliferator-activated receptor gamma gene in human malignancies (2001) Cancer Res., 61, pp. 5307-5310
Tsai, Y.S., Kim, H.J., Takahashi, N., Kim, H.S., Hagaman, J.R., Kim, J.K., Maeda, N., Hypertension and abnormal fat distribution but not insulin resistance in mice with P465L PPARγ (2004) J. Clin. Invest, 114, pp. 163-175
Meredith, D., Panchatcharam, M., Miriyala, S., Tsai, Y.S., Morris, A.J., Maeda, N., Stouffer, G.A., Smyth, S.S., Dominant-negative loss of PPARγ function enhances smooth muscle cell proliferation, migration, and vascular remodeling (2009) Arterioscler. Thromb. Vasc. Biol., 29, pp. 465-471
Francis, G. A., Fayard, E., Picard, F., Auwerx, J., Nuclear receptors and the control of metabolism (2003) Ann. Rev. Physiol., 65, pp. 261-31
Spiegelman, B. M., PPAR: adipogenic regulator and thiazolidinedione receptor (1998) Diabetes, 47, pp. 507-514
Feige, J. N., Gelman, L., Michalik, L., Desvergne, B., Wahli, W., From molecular action to physiological outputs: peroxisome proliferator-activated receptors are nuclear receptors at the crossroads of key cellular functions (2006) Prog. Lipid Res., 45, pp. 120-159
Willson, T. M., Lambert, M. H., Kliewer, S. A., Peroxisome proliferator-activated receptor and metabolic disease (2001) Annu. Rev. Biochem., 70, pp. 341-367
Savage, D. B., Tan, G. D., Acerini, C. L., Jebb, S. A., Agostini, M., Gurnell, M., Williams, R. L., O'Rahilly, S., Human metabolic syndrome resulting from dominant-negative mutations in the nuclear receptor peroxisome proliferator-activated receptor (2003) Diabetes, 52, pp. 910-917
Peverali, F. A., Ramqvist, T., Saffrich, R., Pepperkok, R., Barone, M. V., Philipson, L., Regulation of G1 progression by E2A and Id helix-loop-helix proteins (1994) EMBO J., 13, pp. 4291-4301
Barone, M. V., Courtneidge, S. A., Myc but not Fos rescue of PDGF signaling block caused by kinase-inactive Src (1995) Nature, 378, pp. 509-512
Yeh, J. J., Marsh, D. J., Zedenius, J., Dwight, T., Delbridge, L., Robinson, B. G., Eng, C., Fine-structure deletion mapping of 10q22-24 identifies regions of loss of heterozygosity and suggests that sporadic follicular thyroid adenomas and follicular thyroid carcinomas develop along distinct neoplastic pathways (1999) Genes Chromosomes Cancer, 26, pp. 322-328
Kinzler, K. W., Vogelstein, B., Lessons from hereditary colorectal cancer (1996) Cell, 87, pp. 159-170
Gupta, R. A., Sarraf, P., Mueller, E., Brockman, J. A., Prusakiewicz, J. J., Eng, C., Willson, T. M., DuBois, R. N., Peroxisome proliferator-activated receptor mediated differentiation: a mutation in colon cancer cells reveals divergent and cell type-specific mechanisms (2003) J. Biol. Chem., 278, pp. 22669-22677
Girnun, G. D., Smith, W. M., Drori, S., Sarraf, P., Mueller, E., Eng, C., Nambiar, P., Spiegelman, B. M., APC-dependent suppression of colon carcinogenesis by PPAR (2002) Proc. Natl. Acad. Sci. U. S. A., 99, pp. 13771-13776
Teresi, R. E., Shaiu, C. W., Chen, C. S., Chatterjee, V. K., Waite, K. A., Eng, C., Increased PTEN expression due to transcriptional activation of PPAR by lovastatin and rosiglitazone (2006) Int. J. Cancer, 118, pp. 2390-2398
Annicotte, J. S., Iankova, I., Miard, S., Fritz, V., Sarruf, D., Abella, A., Berthe, M. L., Iborra, F., Peroxisome proliferator-activated receptor regulates E-cadherin expression and inhibits growth and invasion of prostate cancer (2006) Mol. Cell. Biol., 26, pp. 7561-7574
Iatropoulos, M. J., Williams, G. M., Proliferation markers (1996) Exp. Toxicol. Pathol., 48, pp. 175-181
Platt, A. M., Mowat, A. M., Mucosal macrophages and the regulation of immune responses in the intestine (2008) Immunol. Lett., 119, pp. 22-31
Gampe, R. T., Montana, V. G., Lambert, M. H., Miller, A. B., Bledsoe, R. K., Milburn, M. V., Kliever, S. A., Xu, E. H., Asymmetry in the PPAR /RXR crystal structure reveals the molecular basis of heterodimerization among nuclear receptors (2000) Mol. Cell, 5, pp. 545-555
Petersen, M. T., Jonson, P. H., Petersen, S. B., Amino acid neighbours and detailed conformational analysis of cysteines in proteins (1999) Protein Eng., 12, pp. 535-548
Kraulis, P. J., MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures (1991) J. Appl. Crystallogr., 24, pp. 946-950
Tsai, Y. S., Kim, H. J., Takahashi, N., Kim, H. S., Hagaman, J. R., Kim, J. K., Maeda, N., Hypertension and abnormal fat distribution but not insulin resistance in mice with P465L PPAR (2004) J. Clin. Invest, 114, pp. 163-175
Bba-Gen Subjects (ISSN: 0925-4439, 0006-3002, 1570-9639), 2010; 1802(6): 572-581.
Tipo di articolo: Journal Article,
Impact factor: 2.773, Impact factor a 5 anni: 2.751
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-77952240564&partnerID=40&md5=f0a185472554530c6ce54fec0f6a1265
Parole chiave: Colorectal Cancer, Dyslipidemia, Loss-Of-Function Mutation, Peroxisome Proliferator-Activated Receptor, High Density Lipoprotein Cholesterol, Insulin, Low Density Lipoprotein Cholesterol, Peroxisome Proliferator Activated Receptor Gamma, Triacylglycerol, Adult, Aged, Amino Acid Substitution, Article, Cancer Localization, Cell Proliferation, Cholesterol Blood Level, Clinical Article, Colon Carcinogenesis, Colon Polyp, Colonoscopy, Controlled Study, Female, Gene Mutation, Genetic Association, Germ Line, Glucose Blood Level, Histopathology, Human, Human Cell, Human Tissue, Hypertension, In Vitro Study, In Vivo Study, Insulin Blood Level, Ligand Binding, Lipid Metabolism, Liver Metastasis, Loss Of Function Mutation, Non Insulin Dependent Diabetes Mellitus, Nucleotide Sequence, Obesity, Priority Journal, Protein Expression, Protein Function, Triacylglycerol Blood Level, Wild Type, Adenocarcinoma, Adolescent, 80 And Over, Animals, Base Sequence, Binding Sites, Cercopithecus Aethiops, Colonic Neoplasms, Cos Cells, Dna Primers, Germ-Line Mutation, Intestinal Polyps, Loss Of Heterozygosity, Middle Aged, Models, Molecular, Nih 3t3 Cells, Pedigree, Ppar Gamma, Recombinant Proteins, Transfection, Young Adult,
Affiliazioni:
*** IBB - CNR ***
Department of Biological and Environmental Sciences, University of Sannio, Via Port'Arsa, 11, 82100 Benevento, Italy
Institute of Genetics and Biophysics, A. Buzzati-Traverso CNR, Via P. Castellino, 113, 80131 Napoli, Italy
Department of Biochemistry and Medical Biotechnologies, University of Naples Federico II, Via S. Pansini, 5, 80131 Napoli, Italy
Fatebenefratelli Hospital, Division of Medical Oncology, Viale Principe di Napoli, 82100 Benevento, Italy
Department of Chemistry, University of Naples Federico II, Monte S. Angelo, 80100 Napoli, Italy
Riferimenti:
Francis, G.A., Fayard, E., Picard, F., Auwerx, J., Nuclear receptors and the control of metabolism (2003) Ann. Rev. Physiol., 65, pp. 261-31
Spiegelman, B.M., PPARγ: adipogenic regulator and thiazolidinedione receptor (1998) Diabetes, 47, pp. 507-514
Feige, J.N., Gelman, L., Michalik, L., Desvergne, B., Wahli, W., From molecular action to physiological outputs: peroxisome proliferator-activated receptors are nuclear receptors at the crossroads of key cellular functions (2006) Prog. Lipid Res., 45, pp. 120-159
Willson, T.M., Lambert, M.H., Kliewer, S.A., Peroxisome proliferator-activated receptor γ and metabolic disease (2001) Annu. Rev. Biochem., 70, pp. 341-367
Knouff, C., Auwerx, J., Peroxisome proliferator-activated receptor-γ calls for activation in moderation: lessons from genetics and pharmacology (2004) Endocr. Rev., 25, pp. 899-918
Sarraf, P., Mueller, E., Smith, W.M., Wright, H.M., Kum, J.B., Aaltonen, L.A., de la Chapelle, A., Eng, C., Loss-of-function mutations in PPARγ associated with human colon cancer (1999) Mol Cell, 3, pp. 799-804
Ristow, M., Muller-Wieland, D., Pfeiffer, A., Krone, W., Kahn, C.R., Obesity associated with a mutation in a genetic regulator of adipocyte differentiation (1998) N. Engl. J. Med., 339, pp. 953-959
Grommes, C., Landreth, G., Heneka, M.T., Antineoplastic effects of peroxisome proliferator activated receptor γ agonists (2004) Lancet Oncol., 7, pp. 419-429
Sabatino, L., Casamassimi, A., Peluso, G., Barone, M.V., Capaccio, D., Migliore, C., Monelli, P., Colantuoni, V., A novel peroxisome proliferator-activated receptor γ isoform with dominant negative activity generated by alternative splicing (2005) J. Biol. Chem., 280, pp. 26517-26525
Barroso, I., Gurnell, M., Crowley, V.E., Agostini, M., Schwabe, J.W., Soos, M.A., Maslen, G.L., O'Rahilly, S., Dominant negative mutations in human PPARγ associated with severe insulin resistance, diabetes mellitus and hypertension (1999) Nature, 402, pp. 880-883
Savage, D.B., Tan, G.D., Acerini, C.L., Jebb, S.A., Agostini, M., Gurnell, M., Williams, R.L., O'Rahilly, S., Human metabolic syndrome resulting from dominant-negative mutations in the nuclear receptor peroxisome proliferator-activated receptor γ (2003) Diabetes, 52, pp. 910-917
Peverali, F.A., Ramqvist, T., Saffrich, R., Pepperkok, R., Barone, M.V., Philipson, L., Regulation of G1 progression by E2A and Id helix-loop-helix proteins (1994) EMBO J., 13, pp. 4291-4301
Barone, M.V., Courtneidge, S.A., Myc but not Fos rescue of PDGF signaling block caused by kinase-inactive Src (1995) Nature, 378, pp. 509-512
Pancione, M., Forte, N., Sabatino, L., Tomaselli, E., Parente, D., Febbraro, A., Colantuoni, V., Reduced γ-catenin and peroxisome proliferator-activated receptor γ expression levels are associated with colorectal cancer metastatic progression: correlation with tumor-associated macrophages, cyclooxygenase 2, and patient outcome (2009) Hum. Pathol., 40, pp. 714-725
Yeh, J.J., Marsh, D.J., Zedenius, J., Dwight, T., Delbridge, L., Robinson, B.G., Eng, C., Fine-structure deletion mapping of 10q22-24 identifies regions of loss of heterozygosity and suggests that sporadic follicular thyroid adenomas and follicular thyroid carcinomas develop along distinct neoplastic pathways (1999) Genes Chromosomes Cancer, 26, pp. 322-328
Kinzler, K.W., Vogelstein, B., Lessons from hereditary colorectal cancer (1996) Cell, 87, pp. 159-170
Gupta, R.A., Sarraf, P., Mueller, E., Brockman, J.A., Prusakiewicz, J.J., Eng, C., Willson, T.M., DuBois, R.N., Peroxisome proliferator-activated receptor γ mediated differentiation: a mutation in colon cancer cells reveals divergent and cell type-specific mechanisms (2003) J. Biol. Chem., 278, pp. 22669-22677
Girnun, G.D., Smith, W.M., Drori, S., Sarraf, P., Mueller, E., Eng, C., Nambiar, P., Spiegelman, B.M., APC-dependent suppression of colon carcinogenesis by PPARγ (2002) Proc. Natl. Acad. Sci. U.S.A., 99, pp. 13771-13776
Teresi, R.E., Shaiu, C.W., Chen, C.S., Chatterjee, V.K., Waite, K.A., Eng, C., Increased PTEN expression due to transcriptional activation of PPARγ by lovastatin and rosiglitazone (2006) Int. J. Cancer, 118, pp. 2390-2398
Annicotte, J.S., Iankova, I., Miard, S., Fritz, V., Sarruf, D., Abella, A., Berthe, M.L., Iborra, F., Peroxisome proliferator-activated receptor γ regulates E-cadherin expression and inhibits growth and invasion of prostate cancer (2006) Mol. Cell. Biol., 26, pp. 7561-7574
Wang, D., Dubois, R.N., Peroxisome proliferator-activated receptors and progression of colorectal cancer (2008) PPAR Res, p. 931074
Pascual, G., Fong, A.L., Ogawa, S., Gamliel, A., Li, A.C., Perissi, V., Rose, D.W., Glass, C.K., A SUMOylation-dependent pathway mediates transrepression of inflammatory response genes by PPARγ (2005) Nature, 437, pp. 759-763
Iatropoulos, M.J., Williams, G.M., Proliferation markers (1996) Exp. Toxicol. Pathol., 48, pp. 175-181
Platt, A.M., Mowat, A.M., Mucosal macrophages and the regulation of immune responses in the intestine (2008) Immunol. Lett., 119, pp. 22-31
Mori, M., Shimono, R., Adachi, Y., Matsuda, H., Kuwano, H., Sugimachi, K., Ikeda, M., Saku, M., Transitional mucosa in human colorectal lesions (1990) Dis. Colon Rectum, 33, pp. 498-501
Gampe, R.T., Montana, V.G., Lambert, M.H., Miller, A.B., Bledsoe, R.K., Milburn, M.V., Kliever, S.A., Xu, E.H., Asymmetry in the PPARγ /RXRγ crystal structure reveals the molecular basis of heterodimerization among nuclear receptors (2000) Mol. Cell, 5, pp. 545-555
Uppenberg, J., Svensson, C., Jaki, M., Bertilsson, G., Jendeberg, L., Berkenstam, A., Crystal structure of the ligand binding domain of the human nuclear receptor PPARγ (1998) J. Biol. Chem., 273, pp. 31108-31112
Petersen, M.T., Jonson, P.H., Petersen, S.B., Amino acid neighbours and detailed conformational analysis of cysteines in proteins (1999) Protein Eng., 12, pp. 535-548
Kraulis, P.J., MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures (1991) J. Appl. Crystallogr., 24, pp. 946-950
Rogler, G., Significance of anti-inflammatory effects of PPARγ agonists? (2006) Gut, 55, pp. 1067-1069
Alberici, P., Gaspar, C., Franken, P., Gorski, M.M., de Vries, I., Scott, R.J., Ristimäki, A., Fodde, R., Smad4 haploinsufficiency: a matter of dosage (2008) Pathogenetics, 1, pp. 2-12
Eng, C., Schneider, K., Fraumeni, J.F., Li, F.P., Third international workshop on collaborative interdisciplinary studies of p53 and other predisposing genes in Li-Fraumeni syndrome (1997) Cancer Epidemiol. Biomarkers Prev., 6, pp. 379-383
Russell-Swetek, A., West, A.N., Mintern, J.E., Jenkins, J., Rodriguez-Galindo, C., Ribeiro, R., Zambetti, G.P., Identification of a novel TP53 germline mutation E285V in a rare case of paediatric adrenocortical carcinoma and choroid plexus carcinoma (2008) J. Med. Genet., 45, pp. 603-606
Ikezoe, T., Miller, C.W., Kawano, S., Heaney, A., Williamson, E.A., Hisatake, J., Green, E., Koeffler, H.P., Mutational analysis of the peroxisome proliferator-activated receptor gamma gene in human malignancies (2001) Cancer Res., 61, pp. 5307-5310
Tsai, Y.S., Kim, H.J., Takahashi, N., Kim, H.S., Hagaman, J.R., Kim, J.K., Maeda, N., Hypertension and abnormal fat distribution but not insulin resistance in mice with P465L PPARγ (2004) J. Clin. Invest, 114, pp. 163-175
Meredith, D., Panchatcharam, M., Miriyala, S., Tsai, Y.S., Morris, A.J., Maeda, N., Stouffer, G.A., Smyth, S.S., Dominant-negative loss of PPARγ function enhances smooth muscle cell proliferation, migration, and vascular remodeling (2009) Arterioscler. Thromb. Vasc. Biol., 29, pp. 465-471
Francis, G. A., Fayard, E., Picard, F., Auwerx, J., Nuclear receptors and the control of metabolism (2003) Ann. Rev. Physiol., 65, pp. 261-31
Spiegelman, B. M., PPAR: adipogenic regulator and thiazolidinedione receptor (1998) Diabetes, 47, pp. 507-514
Feige, J. N., Gelman, L., Michalik, L., Desvergne, B., Wahli, W., From molecular action to physiological outputs: peroxisome proliferator-activated receptors are nuclear receptors at the crossroads of key cellular functions (2006) Prog. Lipid Res., 45, pp. 120-159
Willson, T. M., Lambert, M. H., Kliewer, S. A., Peroxisome proliferator-activated receptor and metabolic disease (2001) Annu. Rev. Biochem., 70, pp. 341-367
Savage, D. B., Tan, G. D., Acerini, C. L., Jebb, S. A., Agostini, M., Gurnell, M., Williams, R. L., O'Rahilly, S., Human metabolic syndrome resulting from dominant-negative mutations in the nuclear receptor peroxisome proliferator-activated receptor (2003) Diabetes, 52, pp. 910-917
Peverali, F. A., Ramqvist, T., Saffrich, R., Pepperkok, R., Barone, M. V., Philipson, L., Regulation of G1 progression by E2A and Id helix-loop-helix proteins (1994) EMBO J., 13, pp. 4291-4301
Barone, M. V., Courtneidge, S. A., Myc but not Fos rescue of PDGF signaling block caused by kinase-inactive Src (1995) Nature, 378, pp. 509-512
Yeh, J. J., Marsh, D. J., Zedenius, J., Dwight, T., Delbridge, L., Robinson, B. G., Eng, C., Fine-structure deletion mapping of 10q22-24 identifies regions of loss of heterozygosity and suggests that sporadic follicular thyroid adenomas and follicular thyroid carcinomas develop along distinct neoplastic pathways (1999) Genes Chromosomes Cancer, 26, pp. 322-328
Kinzler, K. W., Vogelstein, B., Lessons from hereditary colorectal cancer (1996) Cell, 87, pp. 159-170
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We report a novel PPARG germline mutation in a patient affected by colorectal cancer that replaces serine 289 with cysteine in the mature protein (S289C). The mutant has impaired transactivation potential and acts as dominant negative to the wild type receptor. In addition, it no longer restrains cell proliferation both in vitro and in vivo. Interestingly, the S289C mutant poorly activates target genes and interferes with the inflammatory pathway in tumor tissues and proximal normal mucosa. Consistently, only mutation carriers exhibit colonic lesions that can evolve to dysplastic polyps. The proband presented also dyslipidemia, hypertension and overweight, not associated to type 2 diabetes; of note, family members tested positive for the mutation and display only a dyslipidemic profile at variable penetrance with other biochemical parameters in the normal range. Finally, superimposing the mutation to the crystal structure of the ligand binding domain, the new Cys289 becomes so closely positioned to Cys285 to form an S-S bridge. This would reduce the depth of the ligand binding pocket and impede agonist positioning, explaining the biological effects and subcellular distribution of the mutant protein. This is the first PPARG germline mutation associated with dyslipidemia and colonic polyp formation that can progress to full-blown adenocarcinoma. © 2010 Elsevier B.V.
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41 Records (37 escludendo Abstract e Conferenze).
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Impact factor a 5 anni totale: 150.995 (132.65 escludendo Abstract e Conferenze).
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