Malignant cells have increased levels of common glycoprotein ligands of the endogenous cerebellar soluble lectin CSL.
The glycoprotein composition of various transformed cells or malignant tumors was analyzed and compared to their respective non-malignant control cells or tissues of several species, including man, using an endogenous carbohydrate-binding protein, the cerebellar soluble lectin CSL (Zanetta et al., J. Neurochem. 49, 1250-1257 (1987). A large variety of transformed cells contain a much higher number and larger quantity of glycoprotein ligands of CSL than the control cells or normal tissues. The glycoprotein profiles were, in most cases, independent of the nature of the cell transformation of the degree of differentiation, of the tissue and species. Thus, it is suggested that many transformed cells have, as a common anomaly, the increased synthesis of the special type of glycan recognized by CSL, expressed on the same polypeptide chains.
Maschke
S
S
Laboratoire de Neurobiologie Moléculaire des Interactions Cellulaires-CNRS UPR 416, Strasbourg, France.
Robert
J
J
Coindre
J M
JM
Kuchler
S
S
Vincendon
G
G
Zanetta
J P
JP
D000818:Animals; D002461:Cell Line, Transformed / Q000737:chemistry*; D002478:Cells, Cultured; D003208:Concanavalin A / Q000378:metabolism; D006023:Glycoproteins / Q000032:analysis* / Q000378:metabolism; D006801:Humans; D037102:Lectins / Q000378:metabolism*; D008024:Ligands; D009363:Neoplasm Proteins / Q000032:analysis* / Q000378:metabolism; D014407:Tumor Cells, Cultured / Q000737:chemistry*
D006023:Glycoproteins; D037102:Lectins; D008024:Ligands; D009363:Neoplasm Proteins; C059525:cerebellar soluble lectin; D003208:Concanavalin A