RESUMO
BACKGROUND: Analysis of serum biomarkers for the assessment of atrophic gastritis (AG), a gastric precancerous lesion, is of growing interest for identification of patients at increased risk of gastric cancer. The aim was to analyze the diagnostic performance of serum pepsinogen testing using another method, chemiluminescent enzyme immunoassay (CLEIA), as well as of other new potential biomarkers. MATERIAL AND METHODS: The sera of patients considered at increased risk of gastric cancer and undergoing upper endoscopy collected in our previous prospective, multicenter study were tested for pepsinogen I (PGI) and II (PGII), interleukin-6 (IL-6), human epididymal protein 4 (HE-4), adiponectin, ferritin and Krebs von den Lungen (KL-6) using the CLEIA. The diagnostic performance for the detection of AG was calculated by taking histology as the reference. RESULTS: In total, 356 patients (162 men (46%); mean age 58.6 (±14.2) years), including 152 with AG, were included. For the detection of moderate to severe corpus AG, sensitivity and specificity of the pepsinogen I/II ratio were of 75.0% (95%CI 57.8-87.9) and 92.6% (88.2-95.8), respectively. For the detection of moderate to severe antrum AG, sensitivity of IL-6 was of 72.2% (95%CI 46.5-90.3). Combination of pepsinogen I/II ratio or HE-4 showed a sensitivity of 85.2% (95%CI 72.9-93.4) for the detection of moderate to severe AG at any location. CONCLUSION: This study shows that PG testing by CLEIA represents an accurate assay for the detection of corpus AG. Additionally, IL-6 and HE-4 may be of interest for the detection of antrum AG. MINI-ABSTRACT: Pepsinogens testing by chemiluminescent enzyme immunoassay is accurate for the detection of corpus atrophic gastritis. IL-6 and HE-4 maybe of interest for the detection of antrum atrophic gastritis.
RESUMO
Like all proteins, plasma albumin can undergo glycation to produce glycated albumin. This glycation will change the structure and therefore functionalities of albumin. Because of its accessibility, its high concentration and its half-life the glycation of albumin is greater than that of haemoglobin. Laboratory measurement of glycated albumin is possible. The value of glycated albumin reflects the glycaemic balance over a period of 3 weeks, and shows its interest in cases where the determination of HbA1c is impossible or deficient. It also seems that the glycated albumin has a prognostic interest in the chronic kidney disease patients dialyzed or not. In some patients, the assay of glycated albumin could replace measurement of fructosamines and provide additional information to HbA1c values.
Assuntos
Diabetes Mellitus Tipo 2/diagnóstico , Monitorização Fisiológica/métodos , Albumina Sérica/análise , Glicemia/metabolismo , Diabetes Mellitus Tipo 2/sangue , Diabetes Mellitus Tipo 2/complicações , Diabetes Mellitus Tipo 2/terapia , Nefropatias Diabéticas/sangue , Nefropatias Diabéticas/diagnóstico , Hemoglobinas Glicadas/análise , Hemoglobinas Glicadas/metabolismo , Produtos Finais de Glicação Avançada , Humanos , Valor Preditivo dos Testes , Prognóstico , Diálise Renal , Albumina Sérica/metabolismo , Albumina Sérica GlicadaRESUMO
Today, there is no reference method for the measurement of urinary proteins. The difficulties are that urine is a very complex biological fluid, and that there are a high intra-and inter-individual variability in the protein excretion rate. Progress has been made during the last thirty years, but high analytical variability persists among the colorimetric or turbidimetric methods used for urinary proteins measurement.
