ABSTRACT
The S100 proteins have been extensively used as cancer biomarkers. The objectives of the present work were to immobilize the antibody anti-protein S100 to a net of semi-interpenetrated of polysiloxane and polyvinyl alcohol (POS-PVA discs), to investigate its capacity to capture S100 protein from serum and to quantify it by ELISA in sera from patients with prostatic adenocarcinoma (n = 15) and healthy individuals (n = 10). Also these values were compared to the S100 protein expression in the prostatic tissue through immunohistochemistry. The POS-PVA discs fixed about 92.8% of the offered antibody (7.75 microg of antibody per disc). The best values of the immobilized no-marked antibody anti-S100 and serum dilution were found to be 10 microg and 1:400, respectively. Optical density (OD) values for the sera of patients (0.425 +/- 0.042) with prostatic adenocarcinoma were significantly lower (P < 0.05) compared to those established for the healthy individuals (1.034 +/- 0.124). In the immunohistochemistry study no significant variations were observed in the number of positive S100 cells between prostatic adenocarcinoma (153.45 +/- 16.82) and normal prostate (147.04 +/- 18.98). These results showed a clear difference between S100 proteins expressed in tissue and presented in serum during the prostatic tissue neoplasic transformation. Sera analysis was more sensitive than immunohistochemistry S100 protein detection in the prostate tissue besides the advantage to be less invasive method.
Subject(s)
Biomarkers, Tumor/blood , Enzyme-Linked Immunosorbent Assay/methods , Neoplasm Proteins/blood , Prostatic Neoplasms/blood , Prostatic Neoplasms/diagnosis , S100 Proteins/blood , Biomarkers, Tumor/immunology , Humans , Male , Neoplasm Proteins/immunology , Prostatic Neoplasms/immunology , Reproducibility of Results , S100 Proteins/immunology , Sensitivity and SpecificityABSTRACT
The present study aims to evaluate, through lectin histochemistry, the alterations in the expression of cell surface carbohydrate between benign and malignant lesions of skin using computer image analysis. Skin fragments were obtained through biopsies and diagnosed as basal cell carcinoma (BCC), epidermoid carcinoma (EpC), trichoepithelioma (TE), keratoacanthoma (KA), seborrheic keratosis (SK) and actinic keratosis (AK). Lectins Con A, WGA, PNA, UEA-I and LTA were used in histochemistry study. Image analysis was carried out in a workstation using OPTIMAS TM software system. PNA strong binding pattern to studied tumours evidenced the high expression of D-galactose residues in the epidermal neoplasms when compared to other sugars recognized by the other lectins. Among benign neoplasms, KA presented a high expression of glucose/mannose, alpha-fucose and D-galactose residues evidenced by the intense staining of Con A (94.7 percent), LTA (84.2 percent) and PNA (89.4 percent), respectively. Malignant tumours showed distinct binding patterns. EpC presented significant binding only by PNA lectin. BCC was differentially stained in comparison to the staining pattern observed in benign lesions such as TE. Qualitative (lectin histochemistry) and quantitative (digital image analysis) data obtained in this study evidenced those lectins are potential markers to biochemical alterations in skin neoplasms.
O presente estudo objetivou avaliar, através da histoquímica com lectinas, as alterações na expressão dos carboidratos da superfície celular entre lesões benignas e malignas da pele usando análise de imagens computadorizadas. Fragmentos de pele foram obtidos através de biópsias e diagnosticados como carcinoma basocelular (CBC), carcinoma epidermóide (EpC), tricoepitelioma (TE), cerato acantoma (KA), ceratose seborreica (CS) e ceratose actínica (CA). As lectinas Con A, WGA, PNA, UEA-I e LTA foram usadas no estudo histoquímico. A análise de imagens foi realizada numa estação de análise usando o sistema OPTIMAS TM de análises. A PNA tem sido largamente utilizada no estudo de tumores, evidenciando a expressão de D-galactose nas neoplasias epidérmicas; esse açúcar apresenta alta expressão quando comparado com os outros reconhecidos pelas demais lectinas. Entre as neoplasias benignas, KA apresentou alta expressão glucose/manose; resíduos de alfa-fucose e D-galactose apresentaram intensa marcação com ConA (94,7%) LTA (84,2%) e PNA (89,4 %), respectivamente. Os tumores malignos mostraram marcações distintas: EpC apresentou marcaçã significativa somente com a lectina PNA; CBC apresentou diferente padrão de marcação quando comparado ao observado nas lesõs benignas assim como no TE. Os resultados qualitativos (análise de imagens) e quantitativos (histoquímica com lectinas) desse estudo evidenciaram que as lectinas têm grande potencial como marcadores de alterações bioquímicas nas neoplasias da pele.
