Studies on 6C3HED murine ascites tumor cell receptors for mannosyl-binding lectins.

Abstract

We have investigated the receptor site activity present on 6C3HED tumor cells for concanavalin A, fava, lentil and pea lectins. The binding of the tritiated lectins to the tumor cells was inhibited by methyl-alpha-D-mannoside but not by D-galactose. The number of binding sites for the lectins was 3.5-10(6)/cell for concanavalin A, 3.3-10(6)/cell for fava, 3.6-10(6)/cell for lentil and 4.8-10(6)/cell for pea. The apparent association constants were 3.6 and 1.3 muM-1 for concanavalin A, 3.9 muM-1 for fava, 4.2 muM-1 for lentil and 4.6 and 0.6 muM-1 for pea. Competitive inhibition studies showed that lentil was a good inhibitor of pea binding; concanavalin A was a poor inhibitor of pea binding; and fava was a better inhibitor than concanavalin A but not as good as lentil. Reciprocal inhibition experiments indicated that concanavalin A and pea may bind to different receptors as well as to common receptors. This was also indicated by the observation that trypsin or protease treatment of the cells decreased the binding of pea lectin by 20-40 percent whereas concanavalin A binding was unaffected.

• Authors: H J Allen, E A Johnson
• Journal: Biochimica et biophysica acta (Biochim Biophys Acta) Vol. 436 Issue 3 Pg. 557-66 (Jul 01 1976) ISSN: 0006-3002 [Print] Netherlands
• PMID: 952911 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Lectins
• Methylglycosides
• Methylmannosides
• Concanavalin A
• Peptide Hydrolases
• Trypsin

Topics

• Animals
• Binding Sites
• Binding, Competitive
• Concanavalin A (metabolism)
• Kinetics
• Lectins (metabolism)
• Male
• Methylglycosides (pharmacology)
• Methylmannosides (pharmacology)
• Mice
• Neoplasms, Experimental (metabolism)
• Peptide Hydrolases (pharmacology)
• Protein Binding
• Species Specificity
• Trypsin (pharmacology)