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1.
Clin Chem Lab Med ; 56(8): 1328-1335, 2018 07 26.
Artigo em Inglês | MEDLINE | ID: mdl-29648993

RESUMO

BACKGROUND: Carbohydrate sulfotransferases (CHST) were shown to be involved in carcinogenesis. The aim of the study was to assess the diagnostic value of serum CHST7 concentration in differentiation between lung cancer and non-malignant pulmonary inflammations. METHODS: Clinical case-control study involving 125 participants was conducted: the control group containing cases of pneumonia and chronic obstructive pulmonary disease was compared to the lung cancer group composed of primary and metastatic cancers. Serum concentrations of CHST7 and routinely used markers including carcinoembryonic antigen (CEA), cytokeratin fragment 21-1 (CYFRA 21-1) and neuron-specific enolase (NSE) were determined for each participant using immunochemical methods. Statistical association, receiver operating characteristic (ROC) analysis and cross-validation were used for the evaluation of CHST7 either as a standalone biomarker or as a part of a biomarker panel. RESULTS: In comparison to the control group, serum CHST7 was elevated in lung cancer (p<0.001), but no differences between the overall stages of primary cancers were detected (p=0.828). The differentiation performance in terms of ROC area under curve (AUC) was 0.848 making CHST7 superior biomarker to the NSE (p=0.031). In comparison to CEA and CYFRA 21-1, the performance differences were not detected. CHST7 was not correlated to other biomarkers, and its addition to the routine biomarker panel significantly improved the cross-validated accuracy (85.6% vs. 75.2%) and ROC AUC (p=0.004) of the differentiation using a machine learning approach. CONCLUSIONS: Serum CHST7 is a promising biomarker for the differentiation between lung cancer and non-malignant pulmonary inflammations.


Assuntos
Biomarcadores Tumorais/sangue , Neoplasias Pulmonares/diagnóstico , Pneumonia/diagnóstico , Sulfotransferases/sangue , Adulto , Idoso , Idoso de 80 Anos ou mais , Antígenos de Neoplasias/sangue , Antígeno Carcinoembrionário/sangue , Estudos de Casos e Controles , Diagnóstico Diferencial , Feminino , Humanos , Queratina-19/sangue , Neoplasias Pulmonares/sangue , Masculino , Pessoa de Meia-Idade , Fosfopiruvato Hidratase/sangue , Pneumonia/sangue , Curva ROC , Adulto Jovem , Carboidrato Sulfotransferases
2.
Coll Antropol ; 31(1): 247-51, 2007 Mar.
Artigo em Inglês | MEDLINE | ID: mdl-17598409

RESUMO

Although the majority of eukaryotic proteins are glycosylated, there is a dearth of knowledge regarding protein sugar moieties and their changes in disease. Most multiple myeloma cases are characterized by production of monoclonal immunoglobulins (Ig). We studied galactosylation and sialylation of IgG heavy chains in 16 patients with IgG myeloma using lectin blotting and densitometry. In comparison to age and sex matched controls, galactosylation was reduced in multiple myeloma (median 317 vs. 362, range 153-410 vs. 309-447 relative units, p = 0.015, Student's t-test). Sialylation was stage dependent; samples from patients with stage IIA had lowest amounts of sialic acid, IIIA intermediate and IIIB highest (142.6 vs. 185.9 vs. 248.5 relative units, correlation coefficient r = 0.55). Both galactosylation and sialylation levels were independent of age, sex, treatment type, response to treatment, disease duration and IgG and b2 microglobulin concentration. These data indicate that multiple myeloma is characterized by aberrant immunoglobulin glycosylation.


Assuntos
Imunoglobulina G/metabolismo , Cadeias Pesadas de Imunoglobulinas/metabolismo , Mieloma Múltiplo/imunologia , Adulto , Idoso , Feminino , Galactose/metabolismo , Glicosilação , Humanos , Masculino , Pessoa de Meia-Idade , Ácido N-Acetilneuramínico/metabolismo
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