Biomaterial Database

Histochemical reactivities of lectins and surfactant apoprotein in pulmonary adenocarcinomas and their metastases. 1992

K Sugiyama, and T Kawai, and K Nakanishi, and M Suzuki

Department of Pathology, National Defense Medical College, Saitama, Japan.

In an attempt to better understand the biologic behavior of neoplastic cell metastasis, a histochemical study with the use of six different lectins and a monoclonal antibody against human pulmonary surfactant apoprotein (PE-10) was carried out on primary adenocarcinomas of the lungs and their regional (usually lymphatic to lymph nodes or contralateral lung) and distant (usually hematogenous to extrathoracic organs) metastatic lesions of 54 postmortem cases. Primary pulmonary adenocarcinomas were classified further into acinar, papillary, and solid types according to WHO histological typing. Acinar type primary adenocarcinoma of the lungs showed significantly higher (p less than 0.05) binding reactions to Ricinus communis-I (RCA-I) and Ulex europaeus-I (UEA-I) lectins than solid type adenocarcinoma. With six different lectins, concordantly positive reactions between primary pulmonary adenocarcinomas and their lymphatic and hematogenous metastases were seen in 67% or more cases, and with soybean agglutinin (SBA) and UEA-I the concordance rates between primary and lymphatic metastases (lymph nodes and contralateral lungs, respectively) were significantly higher (p less than 0.05) than those between primary and hematogenous metastases. With PE-10 immunohistochemistry, concordantly positive reactions between primary and metastases were low, especially in cases of distant hematogenous metastases (25%), but the statistical significance of differences was missed by narrow margins. With alcian blue PAS-stain, concordantly positive reactions of mucin production between primary adenocarcinomas and both lymphatic and hematogenous metastases were high (92%), but there was no evidence of correlation between lectin bindings and alcian blue-PAS reactions to either primary or metastatic lesions of pulmonary adenocarcinomas.

UI	MeSH Term	Description	Entries
D007150	Immunohistochemistry	Histochemical localization of immunoreactive substances using labeled antibodies as reagents.	Immunocytochemistry,Immunogold Techniques,Immunogold-Silver Techniques,Immunohistocytochemistry,Immunolabeling Techniques,Immunogold Technics,Immunogold-Silver Technics,Immunolabeling Technics,Immunogold Silver Technics,Immunogold Silver Techniques,Immunogold Technic,Immunogold Technique,Immunogold-Silver Technic,Immunogold-Silver Technique,Immunolabeling Technic,Immunolabeling Technique,Technic, Immunogold,Technic, Immunogold-Silver,Technic, Immunolabeling,Technics, Immunogold,Technics, Immunogold-Silver,Technics, Immunolabeling,Technique, Immunogold,Technique, Immunogold-Silver,Technique, Immunolabeling,Techniques, Immunogold,Techniques, Immunogold-Silver,Techniques, Immunolabeling
D008175	Lung Neoplasms	Tumors or cancer of the LUNG.	Cancer of Lung,Lung Cancer,Pulmonary Cancer,Pulmonary Neoplasms,Cancer of the Lung,Neoplasms, Lung,Neoplasms, Pulmonary,Cancer, Lung,Cancer, Pulmonary,Cancers, Lung,Cancers, Pulmonary,Lung Cancers,Lung Neoplasm,Neoplasm, Lung,Neoplasm, Pulmonary,Pulmonary Cancers,Pulmonary Neoplasm
D008207	Lymphatic Metastasis	Transfer of a neoplasm from its primary site to lymph nodes or to distant parts of the body by way of the lymphatic system.	Lymph Node Metastasis,Lymph Node Metastases,Lymphatic Metastases,Metastasis, Lymph Node
D011485	Protein Binding	The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.	Plasma Protein Binding Capacity,Binding, Protein
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000230	Adenocarcinoma	A malignant epithelial tumor with a glandular organization.	Adenocarcinoma, Basal Cell,Adenocarcinoma, Granular Cell,Adenocarcinoma, Oxyphilic,Adenocarcinoma, Tubular,Adenoma, Malignant,Carcinoma, Cribriform,Carcinoma, Granular Cell,Carcinoma, Tubular,Adenocarcinomas,Adenocarcinomas, Basal Cell,Adenocarcinomas, Granular Cell,Adenocarcinomas, Oxyphilic,Adenocarcinomas, Tubular,Adenomas, Malignant,Basal Cell Adenocarcinoma,Basal Cell Adenocarcinomas,Carcinomas, Cribriform,Carcinomas, Granular Cell,Carcinomas, Tubular,Cribriform Carcinoma,Cribriform Carcinomas,Granular Cell Adenocarcinoma,Granular Cell Adenocarcinomas,Granular Cell Carcinoma,Granular Cell Carcinomas,Malignant Adenoma,Malignant Adenomas,Oxyphilic Adenocarcinoma,Oxyphilic Adenocarcinomas,Tubular Adenocarcinoma,Tubular Adenocarcinomas,Tubular Carcinoma,Tubular Carcinomas
D000911	Antibodies, Monoclonal	Antibodies produced by a single clone of cells.	Monoclonal Antibodies,Monoclonal Antibody,Antibody, Monoclonal
D001059	Apoproteins	The protein components of a number of complexes, such as enzymes (APOENZYMES), ferritin (APOFERRITINS), or lipoproteins (APOLIPOPROTEINS).	Apoprotein
D037102	Lectins	Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition.	Animal Lectin,Animal Lectins,Isolectins,Lectin,Isolectin,Lectin, Animal,Lectins, Animal