Analysis of tumour necrosis factor alpha-specific, lactose-specific and mistletoe lectin-specific binding sites in human lung carcinomas by labelled ligands.
Receptor sites can be visualized by labelled ligands as an alternative to receptor-specific antibodies, as substantiated for two different receptor classes. Recombinant tumour necrosis factor alpha (TNF) was biotinylated via amino-groups and the resultant probe was applied to formalin-fixed, paraffin-embedded tissue sections of 94 primary bronchial carcinomas and to normal peripheral lung parenchyma. In addition, monoclonal antibodies specific for neuron-specific enolase (NSE) and TNF itself were used. The biotinylated beta-galactoside-specific mistletoe lectin, which exhibits dose-dependent immunomodulatory and toxic potency, and two probes that specifically detect certain types of sugar receptors were employed to illustrate further the feasibility of using ligands for receptor localisation. The tumours comprised 62 small cell lung carcinomas, 10 epidermoid carcinomas, 11 adenocarcinomas and 11 large cell anaplastic carcinomas. Expression of TNF-binding sites was found in 39 of the small cell lung carcinomas and in 13 of the non-small cell lung carcinomas. Binding capacity for the TNF-specific antibody was seen in similar proportions of small cell lung carcinomas and of non-small cell lung carcinomas. None of the normal lung parenchymas revealed significant staining. Binding capacities to mistletoe lectin were seen in all normal lung parenchymas and in nearly all cases of adenocarcinoma (10/11). A correlation between the expression of NSE and the binding capacities to TNF was detected. Endogenous lectins, specific for lactose or beta-GalNAc, were displayed in nearly one half of the small cell lung carcinoma cases (44% or 45% respectively) and in about 25% of the non-small cell lung carcinoma cases.
Kayser
K
K
Department of Pathology, Thoraxklinik, Heidelberg, Federal Republic of Germany.
Gabius
H J
HJ
Gabius
S
S
Hagemeyer
O
O
D000116:Acetylgalactosamine / Q000378:metabolism; D001665:Binding Sites; D018288:Carcinoma, Small Cell / Q000378:metabolism* / Q000473:pathology; D002294:Carcinoma, Squamous Cell / Q000378:metabolism* / Q000473:pathology; D006801:Humans; D007785:Lactose / Q000378:metabolism; D008024:Ligands; D008175:Lung Neoplasms / Q000378:metabolism* / Q000473:pathology; D010751:Phosphopyruvate Hydratase / Q000378:metabolism; D028321:Plant Preparations; D010940:Plant Proteins; D054790:Ribosome Inactivating Proteins, Type 2; D014118:Toxins, Biological / Q000378:metabolism*; D014409:Tumor Necrosis Factor-alpha / Q000378:metabolism*
D008024:Ligands; D028321:Plant Preparations; D010940:Plant Proteins; D054790:Ribosome Inactivating Proteins, Type 2; D014118:Toxins, Biological; D014409:Tumor Necrosis Factor-alpha; C009674:ribosome inactivating protein, Viscum; D010751:Phosphopyruvate Hydratase; D007785:Lactose; D000116:Acetylgalactosamine