title: Identification of a major poly-N-acetyllactosamine-containing cell-surface glycoprotein of mouse teratocarcinoma cells. Appearance on cells induced to primitive endoderm but not parietal endoderm differentiation.
abstract: Mouse teratocarcinoma F9 cells were induced to primitive endoderm differentiation with retinoic acid, and poly-N-acetyllactosamine-containing surface glycoproteins were identified by radiolabelling endo-beta-galactosidase-cleavable glycans with galactosyltransferase and radiolabelled UDP-galactose. One major radiolabelled band with an apparent size of 250-500 kDa was identified which differed from the known poly-N-acetyllactosamine-containing glycoproteins laminin, fibronectin, lysosome-associated membrane protein (LAMP)-1 and LAMP-2. This acidic glycoprotein, resistant to glycosaminoglycan-degrading enzymes and proteases, was purified by extraction and phase partition with Triton X-114, octyl Sepharose and Helix pomatia lectin chromatography. The purified glycoprotein could be digested by endo-beta-galactosidase and glycopeptide N-glycosidase F to an apparent size of 160-240 kDa. During retinoic-acid-induced differentiation into primitive endoderm cells, the glycoprotein showed a several-fold increase and a broadening to an apparent size of 200- > 700 kDa. The glycoprotein was no longer detected in retinoic-acid and dibutyryl-cAMP-treated cells which had undergone further differentiation to parietal endoderm cells, nor in the permanently differentiated parietal endoderm line F9-AC. The results suggest that the glycoprotein is a major carrier of poly-N-acetyllactosamine chains on differentiating teratocarcinoma F9 cells, and that its expression as revealed by the poly-N-acetyllactosamine labelling method is regulated by the stage of cellular differentiation.
authors.affiliation: Department of Medical Biochemistry, University of Turku, Finland.
authors.forename: D
authors.initials: D
authors.lastname: Spillmann
authors.forename: J
authors.initials: J
authors.lastname: Finne
mesh_terms: D000818:Animals; D003994:Bucladesine / Q000494:pharmacology; D002454:Cell Differentiation / Q000187:drug effects; D002460:Cell Line; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism; D002846:Chromatography, Affinity; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004707:Endoderm / Q000166:cytology* / Q000378:metabolism; D007700:Kinetics; D007797:Laminin / Q000096:biosynthesis / Q000302:isolation & purification; D037102:Lectins; D008562:Membrane Glycoproteins / Q000096:biosynthesis* / Q000737:chemistry / Q000302:isolation & purification; D051379:Mice; D011134:Polysaccharides / Q000032:analysis*; D018243:Teratocarcinoma / Q000378:metabolism* / Q000473:pathology; D014212:Tretinoin / Q000494:pharmacology; D014407:Tumor Cells, Cultured
chemical_list: D007797:Laminin; D037102:Lectins; D008562:Membrane Glycoproteins; D011134:Polysaccharides; D014212:Tretinoin; D003994:Bucladesine; C037199:poly-N-acetyllactosamine