Your browser doesn't support javascript.
loading
Show: 20 | 50 | 100
Results 1 - 5 de 5
Filter
1.
Int. arch. otorhinolaryngol. (Impr.) ; 19(2): 112-115, Apr-Jun/2015. tab
Article in English | LILACS | ID: lil-747142

ABSTRACT

Introduction Parotid gland incidentalomas (PGIs) are unexpected hypermetabolic foci in the parotid region that can be found when scanning with whole-body positron emission/computed tomography (PET/CT). These deposits are most commonly due to benign lesions such as Warthin tumor. Objective The aim of this study was to determine the prevalence of PGIs identified in PET/CT scans and to assess the role of smoking in their etiology. Methods We retrospectively reviewed all PET/CT scans performed at our center in search of PGIs and identified smoking status and standardized uptake value (SUVmax) in each case. We also analyzed the database of parotidectomies performed in our department in the previous 10 years and focused on the pathologic diagnosis and the presence or absence of smoking in each case. Results Sixteen cases of PGIs were found in 4,250 PET/CT scans, accounting for 0.4% . The average SUVmax was 6.5 (range 2.8 to 16). Cytology was performed in five patients; it was benign in four cases and inconclusive in one case. Thirteen patients had a history of smoking. Of the parotidectomies performed in our center with a diagnosis of Warthin tumor, we identified a history of smoking in 93.8% of those patients. Conclusions The prevalence of PGIs on PET/CT was similar to that reported by other authors. Warthin tumor is frequently diagnosed among PGIs on PET/CT, and it has a strong relationship with smoking. We suggest that a diagnosis other than Warthin tumor should be considered for PGIs in nonsmokers. .


Subject(s)
Humans , ADAM Proteins/metabolism , Proteolysis , von Willebrand Factor/chemistry , von Willebrand Factor/metabolism , Binding Sites , Calcium/metabolism , Disulfides/chemistry , Disulfides/metabolism , Hydrogen Bonding , Models, Molecular , Mutagenesis, Site-Directed , Protein Binding , Protein Stability , Protein Structure, Tertiary , Protein Isoforms/chemistry , Protein Isoforms/metabolism , von Willebrand Factor/genetics
2.
Rev. saúde pública ; 49: 1-9, 27/02/2015. tab, graf
Article in English | LILACS | ID: lil-742296

ABSTRACT

OBJECTIVE To validate a screening instrument using self-reported assessment of frailty syndrome in older adults. METHODS This cross-sectional study used data from the Saúde, Bem-estar e Envelhecimento study conducted in Sao Paulo, SP, Southeastern Brazil. The sample consisted of 433 older adult individuals (≥ 75 years) assessed in 2009. The self-reported instrument can be applied to older adults or their proxy respondents and consists of dichotomous questions directly related to each component of the frailty phenotype, which is considered the gold standard model: unintentional weight loss, fatigue, low physical activity, decreased physical strength, and decreased walking speed. The same classification proposed in the phenotype was utilized: not frail (no component identified); pre-frail (presence of one or two components), and frail (presence of three or more components). Because this is a screening instrument, “process of frailty” was included as a category (pre-frail and frail). Cronbach’s α was used in psychometric analysis to evaluate the reliability and validity of the criterion, the sensitivity, the specificity, as well as positive and negative predictive values. Factor analysis was used to assess the suitability of the proposed number of components. RESULTS Decreased walking speed and decreased physical strength showed good internal consistency (α = 0.77 and 0.72, respectively); however, low physical activity was less satisfactory (α = 0.63). The sensitivity and specificity for identifying pre-frail individuals were 89.7% and 24.3%, respectively, while those for identifying frail individuals were 63.2% and 71.6%, respectively. In addition, 89.7% of the individuals from both the evaluations were identified in the “process of frailty” category. CONCLUSIONS The self-reported assessment of frailty can identify the syndrome among older adults and can be used as a screening tool. Its ...


OBJETIVO Validar instrumento de rastreamento por avaliação autorreferida da síndrome de fragilidade entre idosos. MÉTODOS Estudo transversal com dados do estudo Saúde, Bem-estar e Envelhecimento, realizado em São Paulo, SP. A amostra probabilística foi constituída por 433 idosos (idade ≥ 75 anos) avaliados em 2009. O instrumento autorreferido utilizado pode ser aplicado a idosos ou proxi-informantes e foi composto por questões dicotômicas relacionadas diretamente a cada componente do fenótipo de fragilidade considerado padrão-ouro: perda de peso não intencional, fadiga, baixa atividade física, redução de força e de velocidade de marcha. Manteve-se a classificação proposta no fenótipo: não frágil (nenhum componente identificado); pré-frágil (presença de um ou dois componentes) e frágil (presença de três ou mais componentes). Por tratar-se de instrumento de rastreamento, incluiu-se a categoria processo de fragilização (pré-frágil e frágil). Utilizou-se o coeficiente α de Cronbach na análise psicométrica para avaliar confiabilidade e validade de critério, sensibilidade, especificidade e valores preditivos positivo e negativo. Para verificar a adequação do número de componentes propostos, utilizou-se a análise fatorial. RESULTADOS Os componentes “redução de velocidade de caminhada” e “redução de força” apresentaram boa consistência interna (α = 0,77 e α = 0,72, respectivamente) e a “baixa atividade física” (α = 0,63) foi um pouco menos satisfatória. A sensibilidade e a especificidade para identificação dos pré-frágeis foram de 89,7% e 24,3% e dos frágeis, 63,2% e 71,6%, respectivamente. A categoria “processo de fragilização” identificou, igualmente, 89,7% das pessoas em ambas as avaliações. CONCLUSÕES O instrumento de avaliação de fragilidade autorreferida é capaz de identificar a síndrome entre as pessoas idosas, podendo ser utilizado como instrumento de rastreamento, ...


Subject(s)
Animals , Humans , ADAM Proteins/metabolism , Carrier Proteins/metabolism , Hemarthrosis/etiology , Hemarthrosis/metabolism , Hemophilia A/complications , Signal Transduction , Tumor Necrosis Factor-alpha/metabolism , Synovitis/etiology , Synovitis/metabolism
3.
Biol. Res ; 47: 1-12, 2014. ilus, graf
Article in English | LILACS | ID: biblio-950727

ABSTRACT

BACKGROUND: Extracellular metolloproteases have been implied in different process such as cell death, differentiation and migration. Membrane-bound metalloproteases of the ADAM family shed the extracellular domain of many cytokines and receptor controlling auto and para/juxtacrine cell signaling in different tissues. ADAM17 and ADAM10 are two members of this family surface metalloproteases involved in germ cell apoptosis during the first wave of spermatogenesis in the rat, but they have other signaling functions in somatic tissues. RESULTS: In an attempt to further study these two enzymes, we describe the presence and localization in adult male rats. Results showed that both enzymes are detected in germ and Sertoli cells during all the stages of spermatogenesis. Interestingly their protein levels and cell surface localization in adult rats were stage-specific, suggesting activation of these enzymes at particular events of rat spermatogenesis. CONCLUSIONS: Therefore, these results show that ADAM10 and ADAM17 protein levels and subcellular (cell surface) localization are regulated during rat spermatogenesis.


Subject(s)
Animals , Male , Rats , Spermatogenesis/physiology , Spermatozoa/metabolism , ADAM Proteins/metabolism , Seminiferous Tubules/chemistry , Sertoli Cells/cytology , Sertoli Cells/metabolism , Spermatids/cytology , Spermatids/metabolism , Testis/anatomy & histology , RNA, Messenger/analysis , Immunohistochemistry , Cell Differentiation/physiology , Rats, Sprague-Dawley , Apoptosis/physiology , fas Receptor/analysis , Reverse Transcriptase Polymerase Chain Reaction , ADAM Proteins/analysis , ADAM10 Protein , ADAM17 Protein
4.
Experimental & Molecular Medicine ; : e89-2014.
Article in English | WPRIM | ID: wpr-17801

ABSTRACT

LR11, also known as SorLA or SORL1, is a type-I membrane protein from which a large extracellular part, soluble LR11 (sLR11), is released by proteolytic shedding on cleavage with a disintegrin and metalloproteinase 17 (ADAM17). A shedding mechanism is presumed to have a key role in the functions of LR11, but the evidence for this has not yet been demonstrated. Tetraspanin CD9 has been recently shown to regulate the ADAM17-mediated shedding of tumor necrosis factor-alpha and intercellular adhesion molecule-1 on the cell surface. Here, we investigated the role of CD9 on the shedding of LR11 in leukocytes. LR11 was not expressed in THP-1 monocytes, but it was expressed and released in phorbol 12-myristate 13-acetate (PMA)-induced THP-1 macrophages (PMA/THP-1). Confocal microscopy showed colocalization of LR11 and CD9 proteins on the cell surface of PMA/THP-1. Ectopic neo-expression of CD9 in CCRF-SB cells, which are LR11-positive and CD9-negative, reduced the amount of sLR11 released from the cells. In contrast, incubation of LR11-transfected THP-1 cells with neutralizing anti-CD9 monoclonal antibodies increased the amount of sLR11 released from the cells. Likewise, the PMA-stimulated release of sLR11 increased in THP-1 cells transfected with CD9-targeted shRNAs, which was negated by treatment with the metalloproteinase inhibitor GM6001. These results suggest that the tetraspanin CD9 modulates the ADAM17-mediated shedding of LR11 in various leukemia cell lines and that the association between LR11 and CD9 on the cell surface has an important role in the ADAM17-mediated shedding mechanism.


Subject(s)
Humans , ADAM Proteins/metabolism , Tetraspanin 29/genetics , Cell Line, Tumor , LDL-Receptor Related Proteins/genetics , Leukocytes/metabolism , Macrophages/metabolism , Membrane Transport Proteins/genetics , Proteolysis
5.
Rev. méd. Chile ; 133(11): 1349-1354, nov. 2005. graf
Article in Spanish | LILACS | ID: lil-419939

ABSTRACT

We report a 23 years old female who presented a second episode of thrombotic thrombocytopenic purpura (TTP). She was treated with fresh frozen plasma infusions and 14 plasma exchange (PE) sessions without response. Therefore a second-line therapy was started, associating a weekly cycle administration of vindesine (Vds) 2 mg/m2 and rituximab (R) 375 mg/m2. Five cycles of this association plus one cycle of R exclusively, were administered. After the third course, biological signs of improvement were observed and complete normalization of blood cell counts and other specific parameters was seen after 8 weeks. From the beginning of her second relapse we detected a severe deficit (<5%) in von Willebrand-cleaving factor (ADAMTS13) associated to the presence of ADAMTS13 inhibitors. The combined treatment induced an improvement in ADAMTS13 values without detectable inhibitors. After 21 months of follow-up the patient was well, without signs of relapse but ADAMTS13 values were still under normal, which may be an unfavorable prognostic factor. PE is the treatment of choice for acquired idiopathic TTP, but for refractory cases or TTP cases with severe ADAMTS13 values/high inhibitor titers, PE associated to an immunosuppressive treatment should be considered.


Subject(s)
Adult , Female , Humans , Antibodies, Monoclonal/therapeutic use , Antineoplastic Agents, Phytogenic/therapeutic use , Immunologic Factors/therapeutic use , Purpura, Thrombocytopenic, Idiopathic/drug therapy , Purpura, Thrombotic Thrombocytopenic/drug therapy , Vindesine/therapeutic use , ADAM Proteins/antagonists & inhibitors , ADAM Proteins/chemistry , ADAM Proteins/metabolism , Drug Therapy, Combination , Platelet Transfusion , Purpura, Thrombocytopenic, Idiopathic/blood , Purpura, Thrombocytopenic, Idiopathic/immunology , Purpura, Thrombotic Thrombocytopenic/blood , Purpura, Thrombotic Thrombocytopenic/immunology , Recurrence , Treatment Outcome , von Willebrand Factor/analysis
SELECTION OF CITATIONS
SEARCH DETAIL