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1.
J. bras. pneumol ; 44(1): 18-23, Jan.-Feb. 2018. tab, graf
Article in English | LILACS | ID: biblio-893891

ABSTRACT

ABSTRACT Objective: To investigate the diagnostic value of α-enolase (ENO1) and serum ENO1 autoantibody levels in lung cancer. Methods: Immunohistochemistry staining and ELISA were performed to detect ENO1 expression in lung tissue and serum ENO1 autoantibody levels, respectively. Results: The expression of ENO1 was higher in lung cancer tissues than in benign lung disease tissues (p < 0.001). The proportion of lung cancer samples expressing ENO1 was not significantly different among the various pathological classification groups. The proportion of samples expressing ENO1 was higher in lung cancer patients in stages I/II than in those in stages III/IV (χ2 = 5.445; p = 0.018). The expression of ENO1 in lung cancer tissues was not associated with age, gender, or smoking history. Serum ENO1 antibody levels were significantly higher in the lung cancer group than in the benign lung disease and control groups (p < 0.001). The differences among the pathological classification groups were not statistically significant. Serum ENO1 antibody levels were also in lung cancer patients in stages I/II than in those in stages III/IV (p < 0.01). Serum ENO1 antibody levels were not associated with age, gender, or smoking history in lung cancer patients. The ROC curve representing the diagnosis of lung cancer based on ENO1 antibody levels had an area under the curve of 0.806. Conclusions: Our results suggest that high levels of ENO1 are associated with the clinical stage of lung cancer and that ENO1 expression and its serum autoantibody levels show diagnostic value in lung cancer.


RESUMO Objetivo: Investigar o valor diagnóstico da α-enolase (ENO1) e dos níveis séricos de autoanticorpos contra ENO1 no câncer de pulmão. Métodos: Marcação imuno-histoquímica e ELISA foram realizados para detectar a expressão de ENO1 no tecido pulmonar e os níveis séricos de autoanticorpos contra ENO1, respectivamente. Resultados: A expressão de ENO1 foi maior nos tecidos de câncer de pulmão que nos tecidos de doença pulmonar benigna (p < 0,001). Não houve diferença significativa entre os diversos grupos de classificação patológica quanto à proporção de amostras de câncer de pulmão que expressaram ENO1. A proporção de amostras que expressaram ENO1 foi maior nos pacientes com câncer de pulmão nos estágios I/II que naqueles com câncer de pulmão nos estágios III/IV (χ2 = 5,445; p = 0,018). Não houve relação entre a expressão de ENO1 em tecidos de câncer de pulmão e idade, sexo ou histórico de tabagismo. Os níveis séricos de anticorpos contra ENO1 foram significativamente maiores no grupo câncer de pulmão que nos grupos doença pulmonar benigna e controle (p < 0,001). As diferenças entre os grupos de classificação patológica não foram estatisticamente significativas. Os níveis séricos de anticorpos contra ENO1 foram também significativamente maiores nos pacientes com câncer de pulmão nos estágios I/II que naqueles com câncer de pulmão nos estágios III/IV (p < 0,01). Nos pacientes com câncer de pulmão, não houve relação entre os níveis séricos de anticorpos contra ENO1 e idade, sexo ou histórico de tabagismo. A curva ROC do diagnóstico de câncer de pulmão baseado nos níveis de anticorpos contra ENO1 apresentou área sob a curva = 0,806. Conclusões: Nossos resultados sugerem que há relação entre níveis elevados de ENO1 e o estágio clínico do câncer de pulmão e que a expressão de ENO1 e os níveis séricos de autoanticorpos contra ENO1 têm valor diagnóstico no câncer de pulmão.


Subject(s)
Humans , Male , Female , Adult , Middle Aged , Aged , Aged, 80 and over , Phosphopyruvate Hydratase/analysis , Autoantibodies/blood , Carcinoma/enzymology , Carcinoma/pathology , Lung Neoplasms/enzymology , Lung Neoplasms/pathology , Reference Values , Enzyme-Linked Immunosorbent Assay , Immunohistochemistry , Carcinoma/diagnosis , Biomarkers, Tumor/analysis , Sensitivity and Specificity , Statistics, Nonparametric , Lung Neoplasms/diagnosis
2.
Clinics ; 70(4): 264-272, 04/2015. tab, graf
Article in English | LILACS | ID: lil-747111

ABSTRACT

OBJECTIVE: Bone metastasis is frequently associated with nasopharyngeal carcinoma. The diagnosis and follow-up of bone metastatic patients usually relies on skeletal X-ray and bone scintigraphy, which are time-consuming and costly. This study aimed to evaluate whether serum alkaline phosphatase offers clinical value in predicting the clinical response and survival outcome for skeletal metastatic nasopharyngeal carcinoma. METHODS: Serum alkaline phosphatase was measured at baseline and then before each cycle of treatment in 416 nasopharyngeal carcinoma patients with bone metastasis. The correlations between the pre-treatment and post-treatment alkaline phosphatase levels and the treatment efficacy were analyzed using the chi-square test. Survival was analyzed using the Kaplan–Meier method and then compared using the log-rank test. RESULTS: Patients with elevated pre-treatment alkaline phosphatase (>110 IU/L) had significantly worse progression-free survival (P<0.001) and overall survival (P<0.001) than those with a normal level of this marker (≤110 IU/L). Patients with elevated post-treatment alkaline phosphatase had worse progression-free survival (P<0.001) and overall survival (P<0.001) compared with those with a normal level. Patients with normal pre-treatment and post-treatment alkaline phosphatase showed the most favorable prognosis. The Cox multivariate analysis revealed that only the pre-treatment and post-treatment alkaline phosphatase levels were independent prognostic factors for progression-free survival (HR ϝ 1.656, P<0.001; HR ϝ 2.226, P<0.001) and for overall survival (HR ϝ 1.794, P<0.001; HR ϝ 2.657, P<0.001). CONCLUSIONS: Serum alkaline phosphatase appears to be a significant independent prognostic index in patients with skeletal metastatic nasopharyngeal carcinoma, which could reflect the short-term treatment response ...


Subject(s)
Adolescent , Adult , Aged , Female , Humans , Male , Middle Aged , Young Adult , Alkaline Phosphatase/blood , Bone Neoplasms/enzymology , Bone Neoplasms/mortality , Carcinoma/enzymology , Carcinoma/mortality , Nasopharyngeal Neoplasms/enzymology , Nasopharyngeal Neoplasms/mortality , Biomarkers, Tumor/blood , Bone Neoplasms/blood , Bone Neoplasms/secondary , Carcinoma/blood , Carcinoma/pathology , Disease Progression , Disease-Free Survival , Kaplan-Meier Estimate , Nasopharyngeal Neoplasms/blood , Nasopharyngeal Neoplasms/pathology , Reference Values , Retrospective Studies , Time Factors , Treatment Outcome
3.
São Paulo med. j ; 133(1): 28-35, Jan-Fev/2015. tab, graf
Article in English | LILACS | ID: lil-733007

ABSTRACT

CONTEXT AND OBJECTIVE: Heparanase-1 degrades heparan sulfate and has been correlated with tumor progression. Although the isoform heparanase-2 has no catalytic activity, it seems to be important for modulating heparanase-1 activity. Cathepsin B is a proteinase involved in tumor metastasis. The aim of this study was to analyze heparanase isoform expression and cathepsin B activity in plasma samples from patients with gastrointestinal carcinomas, compared with healthy individuals (control group). DESIGN AND SETTING: This was an analytical cross-sectional study. Peripheral blood samples were collected at a Brazilian public hospital, from 21 patients with histopathological diagnoses of gastrointestinal carcinomas and from 43 healthy individuals. The analyses were performed in two Brazilian medical schools. METHODS: Heparanase isoforms were identified and quantified in plasma samples by means of Western blot. The enzymatic activities of heparanase-1 and cathepsin B were also measured. RESULTS: The results demonstrated that the expression of both heparanase isoforms was significantly greater in plasma samples from gastrointestinal carcinoma patients, compared with the control group. Logistic regression analysis showed that increased heparanase-1 and heparanase-2 expression was exclusively dependent on the ...


CONTEXTO E OBJETIVO: A heparanase-1 degrada heparam sulfato e está relacionada à progressão de tumor. Apesar de a isoforma heparanase-2 não possuir atividade catalítica, parece ser importante para modular a atividade da heparanase-1. A catepsina B é uma proteinase envolvida na metástase de tumores. O objetivo deste estudo foi analisar a expressão das isoformas de heparanase e atividade da catepsina B em amostras de plasma de pacientes com carcinomas gastrointestinais, comparando-se com indivíduos saudáveis (grupo controle). TIPO DE ESTUDO E LOCAL: Este é um estudo transversal analítico. Foram coletadas amostras de sangue periférico, em hospital público brasileiro, de 21 pacientes com diagnóstico histopatológico de carcinoma gastrointestinal e 43 indivíduos saudáveis. As análises foram realizadas em duas faculdades de medicina brasileiras. MÉTODOS: As isoformas da heparanase foram identificadas e quantificadas em amostras de plasma por Western blot. As atividades enzimáticas de heparanase-1 e catepsina B foram também mensuradas. RESULTADOS: Os resultados demonstraram que as expressões das isoformas de heparanase foram significativamente maiores nas amostras de plasma de pacientes com carcinoma gastrointestinal em comparação com ...


Subject(s)
Aged , Aged, 80 and over , Female , Humans , Male , Middle Aged , Biomarkers, Tumor/blood , Carcinoma/enzymology , Cathepsin B/blood , Gastrointestinal Neoplasms/enzymology , Glucuronidase/blood , Blotting, Western/methods , Case-Control Studies , Cross-Sectional Studies , Immunoenzyme Techniques , Isoenzymes/blood
4.
Article in English | IMSEAR | ID: sea-135703

ABSTRACT

Background & objectives: Imbalances in compactly regulated DNA repair pathways in the form of single nucleotide polymorphisms (SNPs) within vital DNA repair genes may result in insufficient DNA repair and increase in DNA breaks thus rendering the human system vulnerable to the debilitatory effects of grave diseases like cancers. The present study involves investigation of association of the non-synonymous SNP rs1052133 (C8069G/Ser326Cys) located in the exonic region of the gene human 8-oxoguanine DNA glycosylase (hOGG1) with the risk of squamous cell carcinomas of the head and neck (SCCHN). Methods: Case-control based genetic association study was performed among 575 (250 SCCHN cases and 325 normal healthy controls) sub-population cluster-matched (Indo-Europeans linguistic subgroup + Caucasoid morphological subtype) samples from the north Indian States of Uttar Pradesh and Uttarakhand using polymerase chain reaction followed by restriction fragment length polymorphism (PCR-RFLP) and DNA sequencing analysis. Results: Our results demonstrated statistically significant protective association for the heterozygous CG [Odds Ratio (OR) 0.6587, 95% Confidence Interval (CI) 0.4615 to 0.9402, P=0.0238], homozygous mutant GG (OR 0.2570, 95% CI 0.1070 to 0.6175, P=0.0013) and combined mutant CG + GG (OR 0.6057, 95% CI 0.4272 to 0.8586, P=0.0059) genotypes. Interpretation & conclusions: The results indicate that the polymorphism rs1052133 is strongly associated with SCCHN susceptibility and the mutant (G) allele might be a protective factor for SCCHN among north Indian subpopulations.


Subject(s)
Carcinoma/enzymology , Carcinoma/genetics , Carcinoma/pathology , Carcinoma, Squamous Cell , Case-Control Studies , DNA Glycosylases/genetics , DNA Repair , Databases, Genetic , Genetic Predisposition to Disease , Genotype , Head and Neck Neoplasms/enzymology , Head and Neck Neoplasms/genetics , Head and Neck Neoplasms/pathology , Humans , India , Neoplasms, Squamous Cell/enzymology , Neoplasms, Squamous Cell/genetics , Neoplasms, Squamous Cell/pathology , Polymorphism, Single Nucleotide , Risk Factors
6.
Rev. Assoc. Med. Bras. (1992) ; 52(4): 275-280, jul.-ago. 2006. tab, graf
Article in Portuguese | LILACS | ID: lil-434400

ABSTRACT

OBJETIVOS: Correlacionar a presença de recidiva local de câncer de mama com a expressão de CD105 em carcinomas primários de mama, e a expressão da ciclooxigenase-2 nos carcinomas primários de mama e nos respectivos linfonodos axilares. MÉTODOS: Estudo com uma coorte histórica de 72 mulheres entre 29 e 67 anos com diagnóstico de carcinoma ductal infiltrante de mama, estadio II, tipo histológico não especial com seus linfonodos axilares respectivos, que tiveram diagnóstico e tratamento cirúrgico no Hospital Nossa Senhora da Conceição, no período de 2001 a 2002. Análise imunoistoquímica do CD105 e COX-2 no tumor primário, da COX-2 nos linfonodos axilares e da recidiva local. RESULTADOS: Das 72 mulheres analisadas com tumores primários, 40 tinham linfonodos axilares positivos e 32 eram negativos; para cada tumor primário, foi escolhido apenas um linfonodo axilar. O grau histológico dos tumores foi I (n=4), II (n=41) e III (n=27). Quinze pacientes apresentaram recidiva local em um período médio de 26 meses (IC 95 por cento 24-28). A presença da COX-2 nos tumores primários foi verificada em 52 casos, e a presença de CD105 em 34 casos, mas não foram considerados fatores prognósticos independentes para recidiva (p=0,203 e p=0,145, respectivamente). A sobrevida para pacientes com expressão da COX-2 em linfonodos axilares (metastáticos ou não metastáticos) foi de 19 meses, contra 28,3 meses para pacientes COX-2 negativa (p<0,0001). CONCLUSÃO: A expressão positiva da COX-2 em linfonodos axilares (positivos ou não) parece ser um fator prognóstico independente para sobrevida livre de doença.


Subject(s)
Humans , Female , Adult , Middle Aged , Aged, 80 and over , Antigens, CD/analysis , Breast Neoplasms/enzymology , Carcinoma/enzymology , /metabolism , Receptors, Cell Surface/analysis , Biomarkers, Tumor , Breast Neoplasms/pathology , Breast Neoplasms/therapy , Cohort Studies , Carcinoma/pathology , Carcinoma/therapy , /analysis , Disease-Free Survival , Immunohistochemistry , Neoplasm Recurrence, Local , Retrospective Studies
7.
Article in English | IMSEAR | ID: sea-43807

ABSTRACT

BACKGROUND: Breast carcinoma is one of the most common tumors in female patients, and its metastasis is a major cause of death. An experimental model has recently found the association of CD44 with MMP-9 that facilitates tumor cell invasion and metastasis. MATERIAL AND METHOD: The CD44v4 and MMP-9 were performed on tissue in paraffin blocks of 50 cases of high-grade breast carcinoma with node positive and 50 cases with node negative. RESULTS: Increased expression of MMP-9(60%) significantly observed in high-grade breast carcinoma patients with node positive (p = 0. 004), whereas CD44v4 displays no significant difference between the two groups (p-value = 0.81). Significant co-expression of CD44v4+ / MMP-9+ (46%) was observed and correlated with node-positive patients whereas the CD44v4+ / MMP-9- (54%) express in node-negative patient (p-value = 0.01). CONCLUSION: The solely expression of CD44v4 does not associate with node status. MMP-9 plays an important role to enhance breast carcinoma cell invasion and associates with lymph node metastasis. The combined expression of CD44v4 (overexpression) and derangement of MMP-9 expression was significantly associated with nodal status.


Subject(s)
Hyaluronan Receptors/metabolism , Breast Neoplasms/enzymology , Carcinoma/enzymology , Female , Humans , Immunohistochemistry , Lymph Nodes/enzymology , Lymphatic Metastasis , Matrix Metalloproteinase 9/metabolism
8.
ABCD (São Paulo, Impr.) ; 17(1): 16-20, 2004. ilus, tab
Article in Portuguese | LILACS | ID: lil-390553

ABSTRACT

RAcional - A benzilamino-oxidase (BzAO) é uma enzima de substrato fisiológico ainda não totalmente conhecido, presente em todos os tecidos humanos e localiza-se nas células nusculares lisas dos vasos sanguíneos, especulando-se daí que a sua função esteja relacionada a angiogenese...


Subject(s)
Humans , Male , Female , Adult , Middle Aged , Benzylamine Oxidase/analysis , Carcinoma/enzymology , Esophageal Neoplasms/enzymology , Anticholesteremic Agents/pharmacology , Endoscopy , Esophagectomy/methods
9.
Rev. méd. Chile ; 123(2): 165-75, feb. 1995. tab, ilus
Article in Spanish | LILACS | ID: lil-151169

ABSTRACT

Tyrosine protein kinase (TPK) activity is associated to malignant cellular transformation. This work compares TPK activity in 27 surgical biopsy samples of mammary carcinoma, 10 samples of normal mammary tissue. TPK activity was determined in tissue homogenates using (Val5) angiotensin II as exogenous substrate. In samples of mammary carcinoma, TPK activity was 33.86 ñ 31.98 pmol P32/mg protein/30 min. This value was significantly higher that those observed in fibrocystic disease (3.92 ñ 2.35), fibroadenomas (13.86 ñ 10.9) and normal tissue (3.56 ñ 3.02)


Subject(s)
Humans , Female , Adult , Middle Aged , Protein-Tyrosine Kinases/biosynthesis , Breast Neoplasms/enzymology , Breast/enzymology , Breast Diseases/enzymology , Carcinoma/enzymology , Case-Control Studies , Fibroadenoma/enzymology
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