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1.
Indian J Pathol Microbiol ; 1995 Jul; 38(3): 261-5
Artigo em Inglês | IMSEAR | ID: sea-74310

RESUMO

The binding of biotinylated bauhinia purpurea (BPA) and pisum Sativum (PSA) lectins to paraffin-embedded tissue sections from 10 normal breast and 55 breast carcinoma has been investigated by applying avidin biotin peroxidase method (ABC). BPA showed very low affinity for normal breast epithelium and the binding was confined to the luminal surface. Eighty-seven percent carcinoma bound BPA, and the staining patterns varied depending on the histologic grade of tumors: luminal surface binding in grade 1 carcinomas; diffuse, granular cytoplasmic with para- or perinuclear deposits and staining along the plasma membrane in grade 2 and grade 3 carcinomas. PSA bound consistently to the luminal surface of all ducts and acinar cells of normal breast tissue. PSA was reactive with all carcinoma but the staining profiles were similar regardless of the tumor differentiation. It is concluded that the lectins used in this study have limited usefulness in routine diagnosis.


Assuntos
Mama/metabolismo , Neoplasias da Mama/diagnóstico , Carcinoma/diagnóstico , Diferenciação Celular , Feminino , Humanos , Lectinas/metabolismo , Lectinas de Plantas
2.
Indian J Pathol Microbiol ; 1994 Jan; 37(1): 21-8
Artigo em Inglês | IMSEAR | ID: sea-73368

RESUMO

The binding of biotinylated BPA to parraffin sections of 18 normal gastrointestinal tract mucosa, 5 nonneoplastic polyps (NNP), 12 adenomas, and 59 carcinomas was studied by using avidinbiotin peroxidase complex (ABC) technique. In normal mucosa BPA appeared to bind both mucus and nonmucus glycoproteins but goblet cell mucus showed a decrease in binding and increase in binding of nonmucus glycoproteins as the cells lose their differentiation. BPA showed characteristic binding patterns in adenoma and carcinoma that differed from the pattern in normal mucosa. In normal mucosa linear binding to the apical cytoplasm in the columnar cells of the surface epithelium was observed, whereas in adenomas and carcinomas, in addition to the linear binding to the apical cytoplasm, diffuse cytoplasmic and granular deposits in the supranuclear, paranuclear or infranuclear zones were seen. Our findings suggest that BPA binding patterns in normal and neoplastic mucosa are related to the degree of cellular differentiation. In the process of malignant transformation the carbohydrate distribution undergoes progressive changes through the adenoma carcinoma sequence. These changes are related to the degree of dysplasia in adenomas and to the degree of differentiation in carcinomas.


Assuntos
Adenocarcinoma/química , Adenoma/química , Carcinoma/química , Diferenciação Celular , Mucosa Gástrica/química , Neoplasias Gastrointestinais/química , Humanos , Técnicas Imunoenzimáticas , Mucosa Intestinal/química , Lectinas/metabolismo , Lectinas de Plantas , Pólipos/química , Receptores Mitogênicos/análise
3.
Indian J Pathol Microbiol ; 1994 Jan; 37(1): 29-38
Artigo em Inglês | IMSEAR | ID: sea-75815

RESUMO

Normal bronchopulmonary tissues and pulmonary carcinomas including three major types (squamous cell carcinoma, adenocarcinoma, and small-cell carcinoma) were studied using three biotinylated lectins (Bauhinia purpurea [BPA], Phaseolus vulgaris [PHA], and Maclura pomifera [MPA]) by avidin biotin peroxidase complex (ABC) method. The study demonstrated that BPA binds with macrophages and pneumocytes of normal tissue, and with adenocarcinoma and small-cell carcinoma, but nonreactive with squamous cell carcinoma. PHA and MPA bound to all the normal components of bronchopulmonary tree and carcinomas of all types. Adenocarcinoma showed the highest density of reacting sites for BPA and MPA, and squamous cell carcinoma showed the highest binding sites for PHA, while small-cell carcinoma were the lowest reacting variant for all lectins. Lectins used in this study have limited usefulness for the diagnosis of pulmonary neoplasms.


Assuntos
Adenocarcinoma/química , Carcinoma de Células Pequenas/química , Carcinoma de Células Escamosas/química , Humanos , Técnicas Imunoenzimáticas , Lectinas , Pulmão/química , Neoplasias Pulmonares/química , Fito-Hemaglutininas , Lectinas de Plantas , Sensibilidade e Especificidade
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