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Artigo Antibrush border antibody disease: a case report and literature review(Elsevier, 2021) Almeida, Jose Bruno de; Brito, Laíse Pereira Arcoverde Fechine; Guedes, Felipe Leite; Vale, Pedro Henrique Cavalcante; Santos, Rivaldo Pereira; Martins, Sílvia Queiroz Santos; Dantas, Gleiko Yuri de Figueredo; Wanderley, David; Araújo, Stanley de Almeida; Silva, Gyl Eanes BarrosAnti-brush border antibody (ABBA) disease, also called anti–low-density lipoprotein receptor-related protein 2 (anti-LRP2) nephropathy, occurs due to the formation of antibodies against brush border antigens of the renal proximal convoluted tubule. We report a case of ABBA disease in a male farmer in his 30s who presented with 2 years of polyuria, dysuria, nocturia, and urinary urgency. He described a history of long-term occupational exposure to pesticides and silica, evolving into possible pneumoconiosis, and prior pulmonary tuberculosis. At presentation, he had reduced kidney function (serum creatinine 3.6 mg/dL) with hyponatremia, hypokalemia, hypophosphatemia, a normal anion gap, metabolic acidosis, and respiratory acidosis, and 2.2 g/day of urine proteinuria. The kidney biopsy was consistent with ABBA, showing amorphous immune-deposits in the tubular basement membrane and strong positivity on indirect immunofluorescence in the brush border of the proximal tubules. The trigger for production of ABBA is still unknown, but it may be associated with chronic conditions such as pulmonary tuberculosis and occupational exposures such as silica and pesticides, as seen in the patient in this report. Most cases do not respond to immunosuppression, and the prognosis is poor.Artigo Binding of the cytosolic p200 protein to Golgi membranes is regulated by heterotrimeric G proteins(Journal Of Cell Science, 1993) Almeida, Jose Bruno de; Doherty, Joanne; Ausiello, Dennis A.; Stow, Jennifer L.The formation of vesicles for protein trafficking requires the dynamic binding of cytosolic coat proteins onto Golgi membranes and this binding is regulated by a variety of GTPases, including heterotrimeric G proteins. We have previously shown the presence of the pertussis toxin-sensitive G i-3 protein on Golgi membranes and demonstrated a functional role for G i-3 in the trafficking of secretory proteins through the Golgi complex. We have also described a brefeldin A-sensitive phosphoprotein, p200, which is found in the cytoplasm and on Golgi membranes. The present study investigates the role of heterotrimeric G proteins in the regulation of p200 binding to Golgi membranes. An in vitro binding assay was used to measure the binding of cytosolic p200 to LLC-PK1 cell microsomal membranes and to purified rat liver Golgi membranes in the presence of specific activators of G proteins. The binding of p200 to Golgi membranes was compared to that of the coatomer protein -COP, for which G protein-dependent membrane binding has previously been established. Membrane binding of both p200 and -COP was induced maximally by activation of all G proteins in the presence of GTP S. More selective activation of the heterotrimeric G proteins, with AlFn or mastoparan, also induced membrane binding of p200 and -COP. Pertussis toxin pretreatment of Golgi membranes, to selectively inactivate G i-3, reduced the AlFn and mastoparan-induced binding of p200 to Golgi membranes, whereas no significant effect of pertussis toxin on -COP binding was found in this assay. The effect of pertussis toxin thus implicates G i-3, as one component of a regulatory pathway, in the binding of cytosolic p200 to Golgi membranes. The effects of AlFn and pertussis toxin on p200 membrane binding were also shown in intact cells by immunofluorescence staining. AlFn treatment of cells induced translocation of p200 from the cytoplasm onto the Golgi complex, resulting in a conformational change in some Golgi membranes. The translocation of p200 was blocked by pretreatment of intact NRK cells with pertussis toxin. The data presented here support the conclusion that the binding of the p200 protein to Golgi membranes involves regulation by the pertussis toxinsensitive heterotrimeric G proteins, specifically the G i-3 proteinArtigo Collapsing glomerulopathy: a review by the collapsing brazilian consortium(Frontiers in medicine, 2022) Almeida, Jose Bruno de; Cutrim, Érico Murilo Monteiro; Neves, Precil Diego Miranda de Meneses; Campos, Marcos Adriano Garcia; Wanderley, Davi Campos; Teixeira Júnior, Antonio Augusto Lima; Muniz, Monique Pereira Rêgo; Ladchumananandasivam, Francisco Rasiah; Gomes, Orlando Vieira; Vasco, Rafael Fernandes Vanderlei; Brito, Dyego José de Araújo; Lages, Joyce Santos; Salgado-Filho, Natalino; Guedes, Felipe Leite; Magalhães, Marcelo; Araújo, Stanley de Almeida; Silva, Gyl Eanes BarrosCollapsing glomerulopathy (CG) is a clinicopathologic entity characterized by segmentar or global collapse of the glomerulus and hypertrophy and hyperplasia of podocytes. The Columbia classification of 2004 classified CG as a histological subtype of focal segmental glomerulosclerosis (FSGS). A growing number of studies have demonstrated a high prevalence of CG in many countries, especially among populations with a higher proportion of people with African descent. The present study is a narrative review of articles extracted from PubMed, Medline, and Scielo databases from September 1, 2020 to December 31, 2021. We have focused on populational studies (specially cross-sectional and cohort articles). CG is defined as a podocytopathy with a distinct pathogenesis characterized by strong podocyte proliferative activity. The most significant risk factors for CG include APOL1 gene mutations and infections with human immunodeficiency virus and severe acute respiratory syndrome coronavirus 2. CG typically presents with more severe symptoms and greater renal damage. The prognosis is notably worse than that of other FSGS subtypesArtigo Distribution and role of heterotrimeric G proteins in the secretory pathway of polarized epithelial cells(Journal Of Cell Science, 1993) Almeida, Jose Bruno de; Stow, Jennifer L.The movement of newly synthesized proteins in the constitutive secretory pathway, from their site of synthesis in the endoplasmic reticulum to the cell surface or to intracellular destinations, requires an orderly sequence of transport steps between membrane-bound compartments. Until recently, the trafficking and secretion of proteins through this pathway was thought to occur as a relatively automatic, unregulated series of events. Recent studies show that protein trafficking in the constitutive secretory pathway requires G T P hydrolysis by families of GTP-binding proteins (G proteins), which at multiple steps potentially provide regulation and specificity for protein trafficking. M any monomeric G proteins are known to be localized and functional on membrane compartments in the constitutive secretory pathway. Now, members of the heterotrimeric G protein family have also been localized on intracellular membranes and compartments such as the Golgi complex. We have studied the localization and targeting of G a subunits to distinct membrane domains in polarized epithelial cells. The distribution of different G a subunits on very specific membrane domains in cultured epithelial cells and in epithelial cells of the kidney cortex, is highly suggestive of roles for these G proteins in intracellular trafficking pathways. One of these G protein subunits, Gai-3, was localized on Golgi membranes. Studies on L L C -P K i cells overexpressing Gcti.3 provided evidence for its functional role in regulating the transport o f a constitutively secreted heparan sulfate proteoglycan through the Golgi complex. Inhibition or activation of heterotrimeric G proteins by pertussis toxin or by aluminium fluoride respectively, have provided further evidence for regulation of intracellular transport by pertussis toxin-sensitive G proteins. Although the functions of Golgi-associated G proteins are not yet understood at the molecular level, heterotrimeric G proteins have been implicated in the binding of cytosolic coat proteins and vesicle formation on Golgi membranes. Future studies will elucidate how multiple G proteins, of both the heterotrimeric and monomeric families, are involved in the regulation of Golgi function and protein trafficking in the secretory pathwayArtigo Effects of an individualized nutritional intervention on kidney function, body composition, and quality of life in kidney transplant recipients: study protocol for a randomized clinical trial(Plos One, 2022) Almeida, Jose Bruno de; Morais, Tassia Louise Sousa Augusto de; Souza, Karla Simone Costa de; Lima, Mabelle Alves Ferreira de; Pereira, Maurıcio Galvão; Oliveira, Antonio Manuel Gouveia de; Evangelista, Karine Cavalcanti Mauricio Sena; Rezende, Adriana Augusto deBackground: Proteinuria after kidney transplantation (KTx) has been a frequent problem due to several factors, high protein intake being one of them. Individualized nutritional intervention in the late post-KTx period can promote the improvement or the reduction of risks associated with the parameters of evaluation of kidney function, body composition, and quality of life in individuals submitted to KTx. Methods: This is a single-center, randomized and stratified clinical trial. The study will be conducted in a university hospital in northeastern Brazil with 174 individuals aged ≥19 years submitted to KTx and followed up for 12 months. Assessments will take place at 3-month intervals (T0, T3, T6, T9, and T12). The patients will be allocated to intervention and control groups by random allocation. The intervention group will receive individualized nutritional interventions with normoproteic diets (1.0 g/kg) after 60 days of KTx whereas the controls will receive the standard nutritional guidance for the post-KTx period. The primary efficacy variable is the change from baseline in log proteinuria assessed with the urinary albumin/creatinine ratio. Secondary efficacy variables include body composition, anthropometry, quality of life assessment and physical activity, lipid profile and glycemic control. Ninety-two subjects per group will afford 70% power to detect a difference of 25% between groups in log proteinuria. Primary efficacy analysis will be on the modified intention-to-treat population with between-groups comparison of the change from baseline in log proteinuria by analysis of covariance. Discussion: The study will assess the effects of an individualized nutritional intervention on proteinuria 12 months after KTxArtigo Entry of cholera toxin into polarized human intestinal epithelial cells. Identification of an early brefeldin a sensitive event required for A1-peptide generation(American Society for Clinical Investigation, 1993) Almeida, Jose Bruno de; Lencer, W. I.; Moe, S.; Stow, Jennifer L.; Ausiello, Dennis A.; Madara, J. L.The effect of brefeldin-A (BFA), a reversible inhibitor of vesicular transport, on cholera toxin (CT)-induced Cl- secretion (Isc) was examined in the polarized human intestinal cell line, T84. Pretreatment of T84 monolayers with 5 microM BFA reversibly inhibited Isc in response to apical or basolateral addition of 120 nM CT (2.4 +/- 0.5 vs. 68 +/- 3 microA/cm2, n = 5). In contrast, BFA did not inhibit Isc responses to the cAMP agonist VIP (63 +/- 7 microA/cm2). BFA had no effect on cell surface binding and endocytosis of a functional fluorescent CT analog or on the dose dependency of CT induced 32P-NAD ribosylation of Gs alpha in vitro. In contrast, BFA completely inhibited (> 95%) the ability of T84 cells to reduce CT to the enzymatically active A1-peptide. BFA had to be added within the first 10 min of CT exposure to inhibit CT-elicited Isc. The early BFA-sensitive step occurred before a temperature-sensitive step essential for apical CT action. These studies show that sequential steps are required for a biological response to apical CT: (a) binding to cell surfaces and rapid endocytosis; (b) early, BFA-sensitive vesicular transport essential for reduction of the A1-peptide; and (c) subsequent temperature-sensitive translocation of a signal (the A1-peptide or possibly ADP-ribose-Gs alpha) to the basolateral domainTese Estudo da associação dos genes TLR2, TLR4, MYD88 e de citocinas pró-inflamatórias com a nefropatia diabética em pacientes com diabetes tipo 1.(2014-02-17) Ururahy, Marcela Abbott Galvão; Rezende, Adriana Augusto de; ; http://lattes.cnpq.br/4245215108740331; ; http://lattes.cnpq.br/8016222352823817; http://lattes.cnpq.br/8016222352823817; Sousa, Andre Gustavo Pires de; ; http://lattes.cnpq.br/7508340761996478; Almeida, Jose Bruno de; ; http://lattes.cnpq.br/1398736458693233; Lima Neto, Lidio Goncalves; ; http://lattes.cnpq.br/1932060521693591; Canani, Luís Henrique Santos; ; http://lattes.cnpq.br/7510654864567417Os objetivos do presente trabalho foram estudar a associação de polimorfismos e da expressão do mRNA dos genes TLR2, TLR4, MYD88, IL1B, IL6 e TNFA com a nefropatia diabética em crianças e adolescentes com Diabetes mellitus tipo 1 (DM1), assim como investigar o potencial papel do WT-1 nos exossomos urinários como um biomarcador sensível e não invasivo de dano glomerular nestes pacientes. No total, foram incluídos no estudo 144 crianças e adolescentes com DM1 e 173 indivíduos normoglicêmicos (NG) da mesma faixa etária. Foram pesquisados os polimorfismos dos genes IL6 (-634C>G e -174G>C), IL1B (3954C>T e -511C>T), TNFA (-308G>A) e TLR2 (1350T>C), determinadas as expressões gênicas de IL6, IL1B, TNFA, MYD88, TLR2 e TLR4, e quantificado o WT-1 em exossomos urinários. Além disso, foram avaliados o controle glicêmico, os lipídios séricos e parâmetros laboratoriais de função renal. Os indivíduos com DM1 apresentaram um controle glicêmico insatisfatório e valores aumentados de colesterol total, LDL-colesterol e da relação albumina:creatinina (RAC), quando comparados com os NG (p<0,05). O polimorfismo IL6 -174G>C foi associado com susceptibilidade ao DM1 (p<0,05). Estudando apenas os indivíduos com DM1, foi observado que os carreadores do genótipo IL6 -174CC apresentaram maiores concentrações de RAC, colesterol total e LDL-colesterol, no modelo recessivo (p<0,05); já os carreadores do genótipo TNFA -308AA apresentaram um aumento nas concentrações séricas de HDL-colesterol, também no modelo recessivo (p<0,05). A relação WT-1:creatinina apresentou-se significativamente aumentada nos indivíduos com DM1 e microalbuminúria quando comparados com ambos os grupos DM1 sem microalbuminúria e NG (p<0,05). Esses resultados sugerem que o polimorfismo IL6 -174G>C pode contribuir para o desenvolvimento do DM1 e da nefropatia diabética, que o TNFA -308G>A pode conferir proteção contra a doença renal induzida pelo DM1 e que o WT-1 nos exossomos urinários seria um indicador precoce de dano em podócitos.Artigo A heterotrimeric GProtein, G«i-3 , on Golgi membranes regulates the secretion of a heparan sulfate proteoglycan in LLC-PKI epithelial cells(The Journal Of Cell Biology, 1991) Almeida, Jose Bruno de; Stow, Jennifer L.; Narula, Navneet; Holtzman, Eliezer J.; Ercolani, Louis; Ausiello, Dennis A.A heterotrimeric Gai subunit, «i- 3 , is localized on Golgi membranes in LLC-PKI and NRK epithelial cells where it colocalizes with mannosidase II by immunofluorescence . The M-3 was found to be localized on the cytoplasmic face of Golgi cisternae and it was distributed across the whole Golgi stack. The a;_3 subunit is found on isolated rat liver Golgi membranes by Western blotting and Gai -3 on the Golgi apparatus is ADP ribosylated by pertussis toxin. LLCPKI cells were stably transfected with GO;-3 on an MT1, inducible promoter in order to overexpress ai-3 on Golgi membranes. The intracellular processing and constitutive secretion of the basement membrane heparan sulfate proteoglycan (HSPG) was measured in LLC-PK, cells. Overexpression of ai-3 on Golgi membranes in transfected cells retarded the secretion of HSPG and accumulated precursors in the medial-trans-Golgi . This effect was reversed by treatment of cells with pertussis toxin which results in ADP-ribosylation and functional uncoupling of Gai-3 on Golgi membranes. These results provide evidence for a novel role for the pertussis toxin sensitive Gai-3 protein in Golgi trafficking of a constitutively secreted protein in epithelial cellsArtigo Infecção por polioma vírus após transplante renal: relato de caso(Brazilian Journal Of Transplantation, 2010) Almeida, Jose Bruno de; Costa, Kellen Micheline Alves Henrique; Félix, Ricardo Humberto de Miranda; Silva Júnior, Maurício Ferreira da; Franco, Marcelo Fabiano deA nefropatia por poliomavírus ocorre em 1,1% a 9,3% dos pacientes transplantados renais, causando perda do enxerto em mais de 40% dos casos. A infecção primária ocorre durante a infância e o vírus se mantém latente no organismo, sendo reativado em estados de imunossupressão. Relatamos o caso de uma mulher de 45 anos transplantada renal há três anos, em uso crônico de tacrolimo e micofenolato mofetil, que apresentou perda progressiva da função renal durante episódio diarréico, mesmo com tratamento adequado. Biópsia do enxerto renal revelou presença de células com inclusões por poliomavírus, sendo iniciado sirolimo e imunoglobulina humana. Com a terapêutica instituída, houve melhora da função renal e nova biópsia realizada após a internação não demonstrou alterações histológicas de poliomavírusArtigo Measuring eosinophiluria, urinary eosinophil cationic protein and urinary interleukin-5 in patients with Lupus Nephritis(Allergy, Asthma & Clinical Immunology, 2014) Almeida, Jose Bruno de; Brito, Tereza Neuma Souza; Vilar, Maria José; Faria, Ana Luiza Souza Brito; Medeiros, Sarah Dantas Viana; Medeiros, Maria Carmo Cardoso; Silva, Edna Marques Araújo; Silva, Vanessa Marques Araújo; Souza, Luanda Bárbara Ferreira Canário; Arruda, Luisa Karla P; Costa, Tatiana Xavier; Cavalcanti Junior, Geraldo Barroso; Oliveira, Antonio Gouveia; Sales, Valéria Soraya FariasBackground: Urine is increasingly becoming an attractive biological fluid in clinical practice due to being an easily obtained, non-invasive sampling method, containing proteins and peptides. The aim of this study was to investigate eosinophiluria, urinary eosinophil cationic protein (uECP) and urinary IL-5 (uIL-5) in patients with Lupus Nephritis. Methods: Seventy-four patients with SLE—20 with clinical and laboratory evidence of lupus nephritis (LN group) and 54 without evidence of renal involvement (non-LN group)—were analyzed regarding eosinophiluria, uECP and uIL-5. Eosinophiluria was observed by Hansel's stain, ECP by fluoroenzymeimmunoassay and uIL-5 by quantitative sandwich enzyme immunoassay. Both uECP and urinary IL-5 (uIL-5) were corrected by urinary creatinine. Eosinophiluria and uECP were compared with glomerular erythrocyturia, protein/creatinine ratio (Pr/Cr ratio), serum creatinine, estimated glomerular filtration rate (eGFR), anti-double-stranded DNA (anti-dsDNA), serum levels of complement (C3 and C4), uIL-5/Cr ratio, and SLE disease activity index. Results: Patients of the LN group had higher eosinophiluria, uECP, uECP/Cr ratio levels, and uIL-5 than patients of the non-LN group (p<0.001 for all). These variables showed a statistically significant correlation with glomerular erythrocyturia, casts, Pr/Cr ratio, serum creatinine, eGFR, anti-dsDNA, uIL-5/Cr, and SLE disease activity index (all p<0.05). Conclusion: These results provide evidence of increased urinary eosinophils, ECP and IL-5 in patients with SLE and LN; uECP/Cr ratio showed better correlation with markers of renal function and SLE disease activityArtigo Pseudotumor cerebral associado ao uso de ciclosporina após transplante renal(Jornal Brasileiro de Nefrologia, 2010) Almeida, Jose Bruno de; Costa, Kellen Micheline Alves Henrique; Félix, Ricardo Humberto de Miranda; Silva Júnior, Maurício Ferreira daPseudotumor cerebral (PC) é uma síndrome, caracterizada pela presença de hipertensão intracraniana (HIC) e sistema ventricular normal. Pacientes submetidos a transplante renal parecem ser mais suscetíveis a desenvolvê-la, devido à terapia com imunossupressores. Ciclosporina (CsA) é uma causa rara de PC, pouco descrita na literatura e que deve ser lembrada no diagnóstico diferencial de HIC e papiledema nesses pacientes. Relatamos um caso de um menino de 10 anos, há três anos com enxerto renal, em uso crônico de micofenolato mofetil (MMF), CsA e baixas doses de prednisona que apresentou quadro de cefaleia, vômitos, diplopia e fotofobia. Fundoscopia revelou edema de papila bilateral. Exame do líquor (LCR) e de imagem foram normais. Após exclusão de causas secundárias, foi feito diagnóstico de PC devido ao uso crônico de CsA, que, portanto, foi substituída por Sirolimus. O paciente apresentou melhora clínica progressiva, com resolução do papiledema após três mesesArtigo Severe hypertension induces disturbances of renal autoregulation(Hypertension, 1992) Almeida, Jose Bruno de; Saragoca, Manoel A.; Tavares, Agostinho; Cezareti, Mário L.; Draibe, Sérgio A.; Ramos, Oswaldo L.To study if the severity of hypertension could be associated with disturbances of the autoregulation of renal blood flow and glomerular filtration, we compared the renal hemodynamic and functional responses to acute blood pressure reductions of a group of patients with moderate essential hypertension (n = 10) with those of a group of patients with severe hypertension (n = 10). Blood pressure was reduced to normal levels by a stepwise infusion of sodium nitroprusside, and effective renal blood flow (by 131I-hippuran), glomerular filtration rate (by endogenous creatinine clearance), and filtration fraction were determined. After acute blood pressure normalization, effective renal blood flow and glomerular filtration rate were significantly reduced in patients with severe hypertension (-41.6 +/- 8.3% and -44.7 +/- 6.8%, respectively; p less than 0.01 for both) but not in those with moderate hypertension (+4.9 +/- 9.1% and +6.2 +/- 13.3%, respectively; NS). Filtration fraction remained unchanged in both groups. These results show that severe but not moderate essential hypertensive patients have a displacement to the right of the lower limit of the renal autoregulation curve due to impaired vasodilation to maintain adequate renal blood flow during acute reductions of blood pressure. This impairment may be due to anatomic or functional defects of preglomerular vessels, or to both. Furthermore, the inability to maintain adequate glomerular filtration in these circumstances shows that patients with severe hypertension also have an impaired ability to adjust postglomerular vasomotor tone in the face of reductions in glomerular blood flow.Artigo Targeting of chimeric Gαi proteins to specific membrane domains(Journal of Cell Science, 1994) Almeida, Jose Bruno de; Holtzman, Eliezer J.; Peters, Philip; Ercolani, Louis; Ausiello, Dennis A.; Stow, Jennifer L.Heterotrimeric guanine nucleotide-regulatory (G) proteins are associated with a variety of intracellular membranes and specific plasma membrane domains. In polarized epithelial LLC-PK1 cells we have shown previously that endogenous Gαi-2 is localized on the basolateral plasma membrane, whereas Gαi-3 is localized on Golgi membranes. The targeting of these highly homologous Gαi proteins to distinct membrane domains was studied by the transfection and expression of chimeric Gαi proteins in LLC-PK1 cells. Chimeric cDNAs were constructed from the cDNAs for Gαi-3 and Gαi-2 and introduced into a pMXX eukaryotic expression vector containing a mouse metallothioneinI promotor. Stably transfected cell lines were produced that expressed either Gαi-2/3 or Gαi-3/2 chimeric proteins. Chimeric and endogenous Gαi proteins were detected in cells using specific carboxy-terminal peptide antibodies. Immunofluorescence staining was used to localize endogenous and chimeric Gαi proteins in LLC-PK1 cells. The staining of chimeric proteins was detected as an increased intensity of staining on membranes containing endogenous Gαi proteins. Using confocal microscopy and image analysis we localized Gαi-2 to a specific sub-domain of the lateral membrane of polarized cells, the chimeric Gαi-3/2 protein was then shown to colocalize with endognenous Gαi-2 in the same lateral plasma membrane domain. The chimeric Gαi-2/3 protein colocalized with endogenous Gαi-3 on Golgi membranes in LLC-PK1 cells. These results show that chimeric Gαi proteins were targeted to the same membrane domains as endogenous Gαi proteins and the specificity of their membrane targeting was conferred by the carboxy-terminal end of the proteins. These data provide the first evidence for specific targeting information contained in the carboxy termini of Gαi proteins, which appears to be independent of amino-terminal membrane attachment sites in these proteins