Lectin binding in murine tumour lines with different malignant characteristics. Effect of enzyme (pronase, neuraminidase) treatment on lectin labelling.
We used 5 syngeneic murine tumour systems for studying quantitative lectin surface binding of intact viable tumour cells. We also investigated, for 3 of the tumours, whether the lectin binding sites were susceptible to proteolytic enzyme (pronase) or neuraminidase treatment. There were significant differences between two of the tumour lines in the binding of wheat germ agglutinin (WGA), concanavalin A (ConA). peanut agglutinin (PNA), soybean agglutinin (SBA) and Ulex europeus agglutinin (UEA). There were also variations in lectin binding between the other tumor lines, but these differences were not statistically significant. Lectin binding showed no evident relationship to the malignancy or the metastasis-forming capacity of the respective tumour cell line. Proteolytic treatment, which drastically affects intravenously induced experimental metastasis formation by one of the tumours, caused a decreased binding of SBA, ConA and WGA. Neuraminidase treatment increased both PNA and SBA binding in three different cell lines, presumably by removing sialic acid masking D-galactose and N-acetyl-D-galactose-amine groups.
Hagmar
B
B
Department of Pathology, Faculty of Medicine, Kuwait.
Erkell
L J
LJ
Burns
G
G
Ryd
W
W
D000818:Animals; D015295:Antigens, Tumor-Associated, Carbohydrate / Q000378:metabolism; D050260:Carbohydrate Metabolism; D037102:Lectins / Q000378:metabolism*; D051379:Mice; D008808:Mice, Inbred CBA; D009361:Neoplasm Invasiveness; D009362:Neoplasm Metastasis; D009368:Neoplasm Transplantation; D009374:Neoplasms, Experimental / Q000378:metabolism* / Q000473:pathology; D009439:Neuraminidase / Q000378:metabolism; D011402:Pronase / Q000378:metabolism; D014407:Tumor Cells, Cultured
D015295:Antigens, Tumor-Associated, Carbohydrate; D037102:Lectins; D009439:Neuraminidase; D011402:Pronase