O aumento de marcadores indicativos da presença de alterações na homeostase redox foi encontrado nos leucócitos e no plasma de pessoas com a mutação rs786205071 no gene BSCL2 em relação aos controles selvagens;
A existência de lesões nos lipídeos e no DNA decorrentes de mecanismos oxidativos foi observada em pessoas com mutação rs786205071 no gene BSCL2 em relação aos controles selvagens;
Foram encontradas relações entre os danos no DNA mitocondrial e disfunções funcionais nessa organela em pessoas com mutação rs786205071 no gene BSCL2;
O aumento de marcadores indicativos da presença de estresse do RE foi encontrado nos leucócitos de pessoas com mutação rs786205071 no gene BSCL2 em relação aos controles selvagens;
Embora a mutação rs786205071 no gene BSCL2 ainda conserve sítios de localização transmembranares para seipina, análises in silico demonstraram uma possível baixa probabilidade dessas sequências serem amiloidogênicas. Ademais, as análises transcricionais apontaram diminuição da presença intracelular do RNA que codifica para seipina;
O plasma de pessoas com a LGC do tipo 2 apresentou diminuição de moléculas antioxidantes, refletidas por distúrbios nas concentrações de adiponectina e baixo HDL-c, possíveis mecanismos elicitatórios das alterações estudadas nessa pesquisa.
REFERÊNCIAS
ABESO. Diretrizes brasileiras de obesidade 2009/2010. v. 3, p. 2009.
AGARWAL, A. K. et al. AGPAT2 is mutated in congenital generalized lipodystrophy linked to chromosome 9q34. Nature Genetics, v. 31, n. 1, p. 21–23, 2002.
AGARWAL, A. K. et al. Phenotypic and Genetic Heterogeneity in Congenital Generalized Lipodystrophy. The Journal of Clinical Endocrinology and Metabolism, v. 88, n. 10, p. 4840–4847, 2003.
AGARWAL, A. K. et al. Seipin: A mysterious protein. Trends in Molecular Medicine, v. 10, n. 9, p. 440–444, 2004.
AGARWAL, A. K. et al. Congenital generalized lipodystrophy: Significance of triglyceride biosynthetic pathways. Trends in Endocrinology and Metabolism, v. 14, n. 5, p. 214–221, 2003.
AL-AUBAIDY, H. A. et al. Oxidative stress and triglycerides as predictors of subclinical atherosclerosis in prediabetes. Redox Report, v. 19, n. 2, p. 87–91, 2014.
AL-BENNA, S. et al. Low-Density Lipoprotein Cholesterol Determines Oxidative Stress and Endothelial Dysfunction in Saphenous Veins From Patients With Coronary Artery Disease. Arteriosclerosis, Thrombosis, and Vascular Biology, v. 26, n. 1, p. 218– 223, 2006.
ANTUNA-PUENTE, B. et al. Higher adiponectin levels in patients with Berardinelli-Seip Congenital Lipodystrophy due to Seipin as compared with 1-Acylglycerol-3-Phosphate- O- Acyltransferase-2 Deficiency. Journal of Clinical Endocrinology and Metabolism, v. 95, n. 3, p. 1463–1468, 2010.
APPLIED BIOSYSTEMS. BigDyeTM Terminator v3.1 Cycle Sequencing Kit - User
Guide, 2016a.
APPLIED BIOSYSTEMS. High-Capacity cDNA Reverse Transcription Kits Protocol, 2016b.
APPLIED BIOSYSTEMS. ExoSAP-IT TM PCR Product Cleanup, 2017.
APWEILER, R. UniProt: the Universal Protein knowledgebase. Nucleic Acids Research, v. 32, p. 115–119, 2004.
ARMENTEROS, J. J. A. et al. DeepLoc: prediction of protein subcellular localization using deep learning. Bioinformatics, v. 18, p. 63–77, 2017.
ARTIMO, P. et al. ExPASy: SIB bioinformatics resource portal. Nucleic Acids Research, v. 40, p. 597–603, 2012.
AYALA, A. et al. Lipid peroxidation: Production, metabolism, and signaling mechanisms of malondialdehyde and 4-hydroxy-2-nonenal. Oxidative Medicine and Cellular Longevity, v. 2014, 2014.
BANERJEE, A. et al. Increased reactive oxygen species levels cause ER stress and cytotoxicity in andrographolide treated colon cancer cells. Oncotarget, v. 8, n. 16, p. 26142–26153, 2017.
factors. Atherosclerosis. Supplements, v. 3, n. 4, p. 39–47, 2002.
BARTER, P. J. The causes and consequences of low levels of high density lipoproteins in patients with diabetes. Diabetes & metabolism journal, v. 35, n. 2, p. 101–106, 2011.
BELLER, M. et al. Lipid droplets: A dynamic organelle moves into focus. FEBS Letters, v. 584, n. 11, p. 2176–2182, 2010.
BERMAN, H. et al. Announcing the worldwide Protein Data Bank. Nature Structural & Molecular Biology, v. 10, n. 12, p. 980–980, 2003.
BHAT, A. H. et al. Oxidative stress, mitochondrial dysfunction and neurodegenerative diseases: a mechanistic insight. Biomedicine & Pharmacotherapy, v. 74, p. 101– 110, 2015.
BHATTACHARYYA, A. et al. Oxidative stress: an essential factor in the pathogenesis of gastrointestinal mucosal diseases. Physiological reviews, v. 94, n. 2, p. 329–354, 2014.
BHATTACHARYYA, T. et al. Relationship of Paraoxonase 1 (PON1) Gene Polymorphisms and Functional Activity With Systemic Oxidative Stress and Cardiovascular Risk. JAMA, v. 299, n. 11, p. 1265, 2008.
BHAYANA, S. et al. Cardiomyopathy in congenital complete lipodystrophy. Clinical genetics, v. 61, n. 4, p. 283–287, 2002.
BI, J. et al. Seipin promotes adipose tissue fat storage through the ER Ca-ATPase SERCA. Cell Metabolism, v. 19, n. 5, p. 861–871, 2014.
BINNS, D. et al. Seipin is a discrete homooligomer. Biochemistry, v. 49, p. 10747– 10755, 2010.
BODDU, N. J. et al. Is the lack of adiponectin associated with increased ER/SR stress and inflammation in the heart? Adipocyte, v. 3, n. 1, p. 10–18, 2014.
BUCHAN, D. W. A. et al. Scalable web services for the PSIPRED Protein Analysis Workbench. Nucleic Acids Research, v. 41, p. 349–357, 2013.
CAMPS, J. et al. PPARs in Regulation of Paraoxonases: Control of Oxidative Stress and Inflammation Pathways. PPAR Research, v. 2012, p. 1–10, 2012.
CAMPS, J. et al. Paraoxonases, mitochondrial dysfunction and non-communicable diseases. Chemico-Biological Interactions, v. 259, p. 382–387, 2016.
CANDIDO DANTAS, V. K. et al. Nurses’ knowledge about Berardinelli-Seip Congenital Lipodystrophy. PLoS ONE, v. 13, n. 6, p. 1–14, 2018.
CANNIZZARO, L. et al. Regulatory landscape of AGE-RAGE-oxidative stress axis and its modulation by PPARγ activation in high fructose diet-induced metabolic syndrome. Nutrition & Metabolism, v. 14, n. 1, p. 5, 2017.
CHAN, J. L. et al. Clinical effects of long-term metreleptin treatment in patients with lipodystrophy. Endocrine Practice, v. 17, n. 6, p. 922–932, 2012.
CHEHAB, F. F. Minireview: Obesity and lipodystrophy - Where do the circles intersect? Endocrinology, v. 149, n. 3, p. 925–934, 2008.
Clinical & translational immunology, v. 7, n. 6, 2018.
CHEN, W. et al. The human lipodystrophy gene product Berardinelli-Seip congenital lipodystrophy 2/seipin plays a key role in adipocyte differentiation. Endocrinology, v. 150, n. 10, p. 4552–4561, 2008.
CHEN, W. et al. Berardinelli-Seip Congenital Lipodystrophy 2/Seipin Is a Cell- Autonomous Regulator of Lipolysis Essential for Adipocyte Differentiation. Molecular and Cellular Biology, v. 32, n. 6, p. 1099–1111, 2012.
CHEN, W. et al. Molecular mechanisms underlying fasting modulated liver insulin sensitivity and metabolism in male lipodystrophic Bscl2/seipin-deficient mice. Endocrinology, v. 155, n. 11, p. 4215–4225, 2014.
CHIQUETTE, E. et al. Estimating the prevalence of generalized and partial lipodystrophy: Findings and challenges. Diabetes, Metabolic Syndrome and Obesity: Targets and Therapy, v. 10, p. 375–383, 2017.
CICHOZ-LACH, H. et al. Oxidative stress as a crucial factor in liver diseases. World Journal of Gastroenterology, v. 20, n. 25, p. 8082–8091, 2014.
CLAY, M. A. et al. Cholesteryl ester transfer protein and hepatic lipase activity promote shedding of apo A-I from HDL and subsequent formation of discoidal HDL. Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism, v. 1124, n. 1, p. 52–58, 1992.
CLÉMENT, S. et al. Role of seipin in lipid droplet morphology and hepatitis C virus life cycle. Journal of General Virology, v. 94, p. 2208–2214, 2013.
CNOP, M. et al. Endoplasmic reticulum stress, obesity and diabetes. Trends in Molecular Medicine, v. 18, n. 1, p. 59–68, 2012.
CONN, P. M. The unfolded protein response and cellular stress. Methods in Enzymology, v. 489, p. 384, 2011.
CRAVEIRO SARMENTO, A. S. et al. Exploring Seipin: From Biochemistry to Bioinformatics Predictions. International Journal of Cell Biology, v. 2018, p. 1–21, 2018.
CRAVEIRO SARMENTO, A. S. et al. The worldwide mutational landscape of Berardinelli-Seip congenital lipodystrophy. Mutation Research/Reviews in Mutation Research, v. 781, p. 30–52, 2019.
CUI, X. et al. Seipin ablation in mice results in severe generalized lipodystrophy. Human Molecular Genetics, v. 20, n. 15, p. 3022–3030, 2011.
CUI, X. et al. Overexpression of a short human seipin/BSCL2 isoform in mouse adipose tissue results in mild lipodystrophy. American Journal of Physiology: Endocrinology and Metabolism, v. 302, n. 6, p. 705–713, 2012.
CYBULSKY, A. V. Endoplasmic reticulum stress, the unfolded protein response and autophagy in kidney diseases. Nature Reviews Nephrology, v. 13, n. 11, p. 681–696, 2017.
DALLEAU, S. et al. Cell death and diseases related to oxidative stress:4- hydroxynonenal (HNE) in the balance. Cell Death & Differentiation, v. 20, n. 12, p. 1615–1630, 2013.
DAMASCENO, É. DE B. et al. Experiência de pessoas que vivem com a Síndrome de Berardinelli-Seip no Nordeste brasileiro. Ciência & Saúde Coletiva, v. 23, n. 2, p. 389–398, 2018.
DANTAS DE MEDEIROS, J. L. et al. Impairment of respiratory muscle strength in Berardinelli-Seip congenital lipodystrophy subjects. Respiratory Research, v. 19, n. 1, p. 1–11, 2018.
DE AZEVEDO MEDEIROS, L. B. et al. High prevalence of Berardinelli-Seip Congenital Lipodystrophy in Rio Grande do Norte State, Northeast Brazil. Diabetology & Metabolic Syndrome, v. 9, n. 1, p. 80, 2017.
DHALLA, N. S. et al. Role of oxidative stress in cardiovascular diseases. Journal of hypertension, v. 18, n. 6, p. 655–673, 2000.
DI MASO, V. et al. Subcellular localization of APE1/Ref-1 in human hepatocellular carcinoma: possible prognostic significance. Molecular medicine, v. 13, n. 1–2, p. 89– 96, 2007.
DI TOMMASO, P. et al. T-Coffee: A web server for the multiple sequence alignment of protein and RNA sequences using structural information and homology extension. Nucleic Acids Research, v. 39, p. 13–17, 2011.
DUDANI, S. et al. Rise in Plasma Triglycerides: An Early Marker of Oxidative Stress in Urban Indians. Journal of Clinical Lipidology, v. 4, n. 3, p. 202–203, 2010.
EL ZOWALATY, A. E. et al. Seipin deficiency increases chromocenter fragmentation and disrupts acrosome formation leading to male infertility. Cell Death and Disease, v. 6, n. 7, p. 1–12, 2015.
FALUDI, A. et al. Atualização da diretriz brasileira de dislipidemias e prevenção da aterosclerose. Arquivos Brasileiros de Cardiologia, v. 109, p. 92, 2017.
FANG, H. et al. Adiponectin Regulation and Function. Comprehensive Physiology, v. 8, p. 1031–1063, 2018.
FEI, W. et al. Fld1p, a functional homologue of human seipin, regulates the size of lipid droplets in yeast. Journal of Cell Biology, v. 180, n. 3, p. 473–482, 2008.
FINN, R. D. et al. The Pfam protein families database: towards a more sustainable future. Nucleic Acids Research, v. 44, p. 279–285, 2016.
FRIEDWALD, W. et al. Estimation of the concentration of low density lipoprotein cholesterol in plasma, without use of the preparative ultracentrifuge. Chemical, v. 18, n. 6, p. 499–502, 1972.
FURDA, A. M. et al. Analysis of DNA Damage and Repair in Nuclear and Mitochondrial DNA of Animal Cells Using Quantitative PCR. Methods in Molecular Biology, v. 920, p. 111–132, 2012.
FURIHATA, C. An active alternative splicing isoform of human mitochondrial 8- oxoguanine DNA glycosylase (OGG1). Genes and environment, v. 37, p. 21, 2015. FURUKAWA, S. et al. Increased oxidative stress in obesity and its impact on metabolic syndrome. The journal of clinical investigation, v. 114, n. 12, p. 1752–1761, 2004. GARBUZYNSKIY, S. O. et al. FoldAmyloid: a method of prediction of amyloidogenic regions from protein sequence. Bioinformatics, v. 26, n. 3, p. 326–332, 2010.
GARG, A. et al. Skeletal muscle morphology and exercise response in congenital generalized lipodystrophy. Diabetes Care, v. 23, n. 10, p. 1545–1550, 2000.
GARG, A. Adipose Tissue Dysfunction in Obesity and Lipodystrophy. Abdominal Adiposity and Cardiometabolic Risk, v. 8, n. 4, p. 7–13, 2006.
GARG, A. Lipodystrophies: Genetic and acquired body fat disorders. Journal of Clinical Endocrinology and Metabolism, v. 96, n. 11, p. 3313–3325, 2011.
GE HEALTHCARE. illustra triplePrep Kit, 2009.
GLUCHOWSKI, N. L. et al. Lipid droplets and liver disease: from basic biology to clinical implications. Nature Reviews Gastroenterology & Hepatology, v. 14, n. 6, p. 343–355, 2017.
GOMES, K. B. et al. Mutations in the Seipin and AGPAT2 Genes Clustering in Consanguineous Families with Berardinelli-Seip Congenital Lipodystrophy from Two Separate Geographical Regions of Brazil. Journal of Clinical Endocrinology and Metabolism, v. 89, n. 1, p. 357–361, 2004.
GONZÁLEZ-MUNIESA, P. et al. Obesity. Nature Reviews Disease Primers, v. 3, p. 1–18, 2017.
GUGLIUCCI, A. et al. The Axis AGE-RAGE-Soluble RAGE and Oxidative Stress in Chronic Kidney Disease. Advances in experimental medicine and biology, v. 824, p. 191–208, 2014.
GUILLÉN-NAVARRO, E. et al. A new seipin-associated neurodegenerative syndrome. Journal of medical genetics, v. 50, n. 6, p. 401–409, 2013.
HABERZETTL, P. et al. Oxidized lipids activate autophagy in a JNK-dependent manner by stimulating the endoplasmic reticulum stress response. Redox biology, v. 1, n. 1, p. 56–64, 2013.
HANSEL, B. et al. Metabolic Syndrome Is Associated with Elevated Oxidative Stress and Dysfunctional Dense High-Density Lipoprotein Particles Displaying Impaired Antioxidative Activity. The Journal of Clinical Endocrinology & Metabolism, v. 89, n. 10, p. 4963–4971, 2004.
HOLLIE, N. I. et al. Micromolar changes in lysophosphatidylcholine concentration cause minor effects on mitochondrial permeability but major alterations in function. Biochimica et biophysica acta, v. 1841, n. 6, p. 888–895, 2014.
HONG, J. et al. The Role of Endoplasmic Reticulum Stress in Cardiovascular Disease and Exercise. International Journal of Vascular Medicine, v. 2017, p. 1–9, 2017. HOU, Y. et al. Adiponectin is protective against endoplasmic reticulum stress-induced apoptosis of endothelial cells in sepsis. Brazilian Journal of Medical and Biological Research, v. 51, n. 12, 2018.
HSIAO, C. T. et al. Clinical and molecular characterization of BSCL2 mutations in a taiwanese cohort with hereditary neuropathy. PLoS ONE, v. 11, n. 1, p. 1–12, 2016. HSU, C.-C. et al. Role of mitochondrial dysfunction in cancer progression. Experimental biology and medicine, v. 241, n. 12, p. 1281–95, 2016.
HUG, N. et al. Mechanism and regulation of the nonsense-mediated decay pathway. Nucleic acids research, v. 44, n. 4, p. 1483–1495, 2016.
IMAI, K. et al. Induction of OGG1 gene expression by HIV-1 Tat. Journal of Biological Chemistry, v. 280, n. 29, p. 26701–26713, 2005.
INVITROGEN. QubitTM Assay Kit, 2010.
ITO, D. et al. Characterization of seipin/BSCL2, a protein associated with spastic paraplegia 17. Neurobiology of Disease, v. 31, n. 2, p. 266–277, 2008.
ITO, D. et al. Molecular pathogenesis of Seipin/BSCL2-related motor neuron diseases. Annals of Neurology, v. 61, n. 3, p. 237–250, 2007.
ITO, D. et al. Seipinopathy: A novel endoplasmic reticulum stress-associated disease. Brain, v. 132, n. 1, p. 8–15, 2009.
IWABU, M. et al. Adiponectin and AdipoR1 regulate PGC-1α and mitochondria by Ca2+ and AMPK/SIRT1. Nature, v. 464, n. 7293, p. 1313–1319, 2010.
JENINGA, E. H. et al. A Patient with Congenital Generalized Lipodystrophy Due To a Novel Mutation in BSCL2: Indications for Secondary Mitochondrial Dysfunction. JIMD Reports, v. 4, p. 113–116, 2011.
JOHRI, A. et al. Mitochondrial Dysfunction in Neurodegenerative Diseases. Journal of Pharmacology and Experimental Therapeutics, v. 342, n. 3, p. 619–630, 2012. JOO, M. S. et al. AMPK Facilitates Nuclear Accumulation of Nrf2 by Phosphorylating at Serine 550. Molecular and Cellular Biology, v. 36, n. 14, p. 1931–1942, 2016. JOSHI, A. S. et al. Organelle biogenesis in the endoplasmic reticulum. Nature Cell Biology, v. 19, n. 8, p. 876–882, 2017.
KATSUKI, A. et al. Increased oxidative stress is associated with serum levels of triglyceride, insulin resistance, and hyperinsulinemia in Japanese metabolically obese, normal-weight men. Diabetes care, v. 27, n. 2, p. 631–632, 2004.
KHAN, M. M. et al. Endoplasmic Reticulum Stress in Sepsis. Shock, v. 44, n. 4, p. 294–304, 2015.
KIM, C. A. et al. Association of a homozygous nonsense caveolin-1 mutation with berardinelli-seip congenital lipodystrophy. Journal of Clinical Endocrinology and Metabolism, v. 93, n. 4, p. 1129–1134, 2008.
KIM, D.-S. et al. Effects of triglyceride on ER stress and insulin resistance. Biochemical and Biophysical Research Communications, v. 363, n. 1, p. 140–145, 2007.
KONTUSH, A. et al. A normotriglyceridemic, low HDL-cholesterol phenotype is characterised by elevated oxidative stress and HDL particles with attenuated antioxidative activity. Atherosclerosis, v. 182, n. 2, p. 277–285, 2005.
KONTUSH, A. et al. Antiatherogenic function of HDL particle subpopulations: focus on antioxidative activities. Current Opinion in Lipidology, v. 21, n. 4, p. 312–318, 2010. KROKAN, H. E. et al. Base Excision Repair. Cold Spring Harbor Perspectives in Biology, n. 5, p. 1–22, 2013.
KYRIAKAKIS, E.; CHARMPILAS, N.; TAVERNARAKIS, N. Differential adiponectin signalling couples ER stress with lipid metabolism to modulate ageing in C. Elegans. Scientific Reports, v. 7, n. 1, p. 1–13, 2017.
Labtest Diagnóstica S.A. Disponível em: <https://labtest.com.br/>. Acesso em: 9 ago. 2018.
LARA-GUZMÁN, O. J. et al. Oxidized LDL triggers changes in oxidative stress and inflammatory biomarkers in human macrophages. Redox Biology, v. 15, p. 1–11, 2018.
LAURENT, V. et al. Periprostatic adipocytes act as a driving force for prostate cancer progression in obesity. Nature Communications, v. 7, p. 1–15, 2016.
LEI, T. et al. Stress kinases, endoplasmic reticulum stress, and Alzheimer’s disease related markers in peripheral blood mononuclear cells from subjects with increased body weight. Nature Publishing Group, v. 6, p. 1–9, 2016.
LEUNG, D. W. The structure and functions of human lysophosphatidic acid acyltransferases. Frontiers in Bioscience, v. 6, p. 944–953, 2001.
LI, H. et al. Adiponectin ameliorates hyperglycemia-induced cardiac hypertrophy and dysfunction by concomitantly activating Nrf2 and Brg1. Free Radical Biology and Medicine, v. 84, p. 311–321, 2015.
LIA, D. et al. Mitochondrial maintenance under oxidative stress depends on mitochondrially localised α-OGG1. Journal of Cell Science, v. 131, n. 12, 2018. LIGUORI, I. et al. Oxidative stress, aging, and diseases. Clinical Interventions in Aging, p. 757–772, 2018.
LIMA, J. G. et al. Clinical and laboratory data of a large series of patients with congenital generalized lipodystrophy. Diabetology & Metabolic Syndrome, v. 8, n. 23, p. 1–7, 2016.
LIMA, J. G. et al. Causes of death in patients with Berardinelli- Seip congenital generalized lipodystrophy. PLoS ONE, v. 13, n. 6, p. 1–10, 2018.
LIN, Z. et al. Adiponectin protects against acetaminophen-induced mitochondrial dysfunction and acute liver injury by promoting autophagy in mice. Journal of hepatology, v. 61, n. 4, p. 825–831, 2014.
LIU, L. et al. Deletion of Cavin/PTRF causes global loss of caveolae, dyslipidemia and glucose intolerance. Cell Metabolism, v. 8, n. 4, p. 310–317, 2008.
LIU, L. et al. Adipose-specific knockout of Seipin/Bscl2 results in progressive lipodystrophy. Diabetes, v. 63, n. 7, p. 2320–2331, 2014.
LIU, Z. et al. Adiponectin reduces ER stress-induced apoptosis through PPARα transcriptional regulation of ATF2 in mouse adipose. Cell death & disease, v. 7, n. 11, 2016.
LOUNIS, M. A. et al. Hepatic BSCL2 (Seipin) Deficiency Disrupts Lipid Droplet Homeostasis and Increases Lipid Metabolism via SCD1 Activity. Lipids, v. 52, n. 2, p. 129–150, 2017.
LUNDIN, C. et al. Membrane topology of the human seipin protein. FEBS Letters, v. 580, n. 9, p. 2281–2284, 2006.
MAGRÉ, J. et al. Identification of the gene altered in Berardinelli-Seip congenital lipodystrophy on chromosome 11q13. Nature Genetics, v. 28, n. 4, p. 365–370, 2001. MALDERGEM, L. VAN et al. Genotype-phenotype relationships in Berardinelli-Seip
congenital lipodystrophy. Journal of medical genetics, v. 39, n. 10, p. 722–733, 2002. MALHI, H. et al. Endoplasmic reticulum stress in liver disease. Journal of Hepatology, v. 54, n. 4, p. 795–809, 2011.
MALHOTRA, J. D. et al. Endoplasmic Reticulum Stress and Oxidative Stress: A Vicious Cycle or a Double-Edged Sword? Antioxidants & Redox Signaling, v. 9, n. 12, p. 2277–2294, 2007.
MARCHLER-BAUER, A. et al. CDD: NCBI’s conserved domain database. Nucleic Acids Research, v. 43, p. 222–226, 2015.
MARSEGLIA, L. et al. Oxidative stress in obesity: a critical component in human diseases. International journal of molecular sciences, v. 16, n. 1, p. 378–400, 2014. MATHEBULA, S. D. Polyol pathway: A possible mechanism of diabetes complications in the eye. African Vision and Eye Health, v. 74, n. 1, 2015.
MATSUDA, M. et al. Roles of adiponectin and oxidative stress in obesity-associated metabolic and cardiovascular diseases. Reviews in Endocrine and Metabolic Disorders, v. 15, n. 1, p. 1–10, 2014.
MAZIÈRE, C. et al. Oxidized LDL Induces an Oxidative Stress and Activates the Tumor Suppressor p53 in MRC5 Human Fibroblasts. Biochemical and Biophysical Research Communications, v. 276, n. 2, p. 718–723, 2000.
MEEHAN, C. A. et al. Metreleptin for injection to treat the complications of leptin deficiency in patients with congenital or acquired generalized lipodystrophy. Expert Review of Clinical Pharmacology, v. 9, n. 1, p. 59–68, 2016.
MILECH, A. Diretrizes da Sociedade Brasileira de Diabetes. Sociedade Brasileira de Diabetes, p. 1–383, 2017.
MODARESI, A. et al. Oxidative stress in chronic kidney disease. Iranian journal of kidney diseases, v. 9, n. 3, p. 165–179, 2015.
MONDAL, A. K. et al. Effect of Endoplasmic Reticulum Stress on Inflammation and Adiponectin Regulation in Human Adipocytes. Metabolic Syndrome and Related Disorders, v. 10, n. 4, p. 297–306, 2012.
MULLER, C. et al. HDLs inhibit endoplasmic reticulum stress and autophagic response induced by oxidized LDLs. Cell Death & Differentiation, v. 18, n. 5, p. 817–828, 2011a.
MULLER, C. et al. Oxidized LDLs trigger endoplasmic reticulum stress and autophagy: Prevention by HDLs. Autophagy, v. 7, n. 5, p. 541–543, 2011b.
MULLER, C. et al. Protein Disulfide Isomerase Modification and Inhibition Contribute to ER Stress and Apoptosis Induced by Oxidized Low Density Lipoproteins. Antioxidants & Redox Signaling, v. 18, n. 7, p. 731–742, 2013.
NCBI RESOURCE COORDINATORS. Database Resources of the National Center for Biotechnology Information. Nucleic Acids Research, v. 45, p. 8–20, 2013.
NICULESCU, L. S. et al. HDL inhibit endoplasmic reticulum stress by stimulating apoE and CETP secretion from lipid-loaded macrophages. Biochemical and Biophysical Research Communications, v. 434, n. 1, p. 173–178, 2013.
Singapore, v. 997, p. 111–120, 2017.
OSWIECIMSKA, J. et al. Berardinelli-Seip syndrome patient with novel AGPAT2 splicesite mutation and concomitant development of non-diabetic polyneuropathy. Journal of Clinical Research in Pediatric Endocrinology, 2018.
OZCAN, L. et al. Role of Endoplasmic Reticulum Stress in Metabolic Disease and Other Disorders. Annual Review of Medicine, v. 63, n. 1, p. 317–328, 2012.
OZCAN, U. et al. Endoplasmic Reticulum Stress Links Obesity, Insulin Action, and Type 2 Diabetes. Science, v. 299, p. 1033–1036, 2003.
PAGAC, M. et al. SEIPIN Regulates Lipid Droplet Expansion and Adipocyte Development by Modulating the Activity of Glycerol-3-phosphate Acyltransferase. Cell Reports, v. 17, n. 6, p. 1546–1559, 2016.
PATNI, N. et al. Congenital generalized lipodystrophies - New insights into metabolic dysfunction. Nature Reviews Endocrinology, v. 11, n. 9, p. 522–534, 2015.
PAYNE, V. A. et al. The human lipodystrophy gene BSCL2/Seipin may be essential for normal adipocyte differentiation. Diabetes, v. 57, n. 8, p. 2055–2060, 2008.
PIPERI, C. et al. Crosstalk between Advanced Glycation and Endoplasmic Reticulum Stress: Emerging Therapeutic Targeting for Metabolic Diseases. The Journal of Clinical Endocrinology & Metabolism, v. 97, n. 7, p. 2231–2242, 2012.
PLAISANCE, V. et al. Endoplasmic Reticulum Stress Links Oxidative Stress to Impaired Pancreatic Beta-Cell Function Caused by Human Oxidized LDL. PLOS ONE, v. 11, n. 9, 2016.
PNCQ – Programa Nacional de Controle de Qualidade. Valores Normais de Hemograma.
QIU, W. et al. Suppression of Adipogenesis by Pathogenic Seipin Mutant Is Associated with Inflammatory Response. PLoS ONE, v. 8, n. 3, 2013.
RAKOCEVIC-STOJANOVIC, V. et al. N88S mutation in the BSCL2 gene in a Serbian family with distal hereditary motor neuropathy type V or Silver syndrome. Journal of the Neurological Sciences, v. 296, n. 1–2, p. 107–109, 2010.
RAN, C. et al. Genetic Variations and mRNA Expression of NRF2 in Parkinson’s Disease. Parkinson’s Disease, v. 2017, p. 1–7, 2017.
REN, Y. et al. Adiponectin modulates oxidative stress-induced mitophagy and protects C2C12 myoblasts against apoptosis. Scientific Reports, v. 7, n. 1, p. 1–12, 2017. ROBBESYN, F. et al. HDL counterbalance the proinflammatory effect of oxidized LDL by inhibiting intracellular reactive oxygen species rise, proteasome activation, and subsequent NF-κB activation in smooth muscle cells. The FASEB Journal, v. 17, n. 6, p. 743–745, 2003.
ROBERTS, C. K. et al. Oxidative stress and metabolic syndrome. Life Sciences, v. 84, n. 21–22, p. 705–712, 2009.
ROBERTSON, R. P. et al. Chronic oxidative stress as a mechanism for glucose toxicity of the beta cell in Type 2 diabetes. Cell Biochemistry and Biophysics, v. 48, n. 2–3, p. 139–146, 2007.
macrophage oxidative stress: studies in PON1-knockout mice. Free Radical Biology and Medicine, v. 34, n. 6, p. 774–784, 2003.
RUIZ-RIQUELME, A. et al. Larger aggregates of mutant seipin in Celia’s Encephalopathy, a new protein misfolding neurodegenerative disease. Neurobiology of Disease, v. 83, p. 44–53, 2015.
RUSCICA, M. et al. High Density Lipoproteins Inhibit Oxidative Stress-Induced Prostate Cancer Cell Proliferation. Scientific Reports, v. 8, n. 1, p. 1–12, 2018. SAH, R. P. et al. Endoplasmic reticulum stress is chronically activated in chronic pancreatitis. Journal of Biological Chemistry, v. 289, n. 40, p. 27551–27561, 2014. SÁNCHEZ-IGLESIAS, S. et al. Does Seipin Play a Role in Oxidative Stress Protection and Peroxisome Biogenesis? New Insights from Human Brain Autopsies. Neuroscience, v. 396, p. 119–137, 2018.
SANGER, F. et al. DNA sequencing with chain-terminating inhibitors. Proceedings of the National Academy of Sciences of the United States of America, v. 74, n. 12, p. 5463–5467, 1977.
SCHEIBYE-KNUDSEN, M. et al. A novel diagnostic tool reveals mitochondrial pathology in human diseases and aging. Aging, v. 5, n. 3, p. 192–208, 2013.
SCHULZE, P. C. et al. Hyperglycemia Promotes Oxidative Stress through Inhibition of Thioredoxin Function by Thioredoxin-interacting Protein. Journal of Biological Chemistry, v. 279, n. 29, p. 30369–30374, 2004.
SEIP, M.; et al. Generalized Lipodystrophy. Archives of Disease in Childhood, v. 38,