Identification and biochemical characterization of secreted Wnt-1 protein from P19 embryonal carcinoma cells induced to differentiate along the neuroectodermal lineage.
Previous studies have described Wnt-1 protein synthesized by cell lines transfected with Wnt-1 cDNA. This report presents the first identification and biochemical characterization of native Wnt-1 protein, from P19 embryonal carcinoma cells undergoing neuroectodermal differentiation. The data demonstrate that P19 cells efficiently process and secrete glycosylated Wnt-1 protein species of 40 kD and 42 kD. Similar to recombinant Wnt-1 proteins, native Wnt-1 proteins are associated with the cell surface upon secretion and can be released by suramin treatment of the cells. Non-reducing gel analysis showed that Wnt-1 proteins are secreted as monomers.
Papkoff
J
J
SUGEN Inc., Redwood City, Ca 94063.
D000818:Animals; D002460:Cell Line; D054278:Embryonal Carcinoma Stem Cells; D006031:Glycosylation; D051379:Mice; D008970:Molecular Weight; D014411:Neoplastic Stem Cells / Q000737:chemistry*; D011518:Proto-Oncogene Proteins / Q000032:analysis* / Q000378:metabolism; D011994:Recombinant Proteins / Q000378:metabolism; D051153:Wnt Proteins; D051155:Wnt1 Protein; D029961:Zebrafish Proteins
D011518:Proto-Oncogene Proteins; D011994:Recombinant Proteins; D051153:Wnt Proteins; D051155:Wnt1 Protein; C495246:Wnt1 protein, mouse; D029961:Zebrafish Proteins