title: Disialoganglioside GD3 synthase expression recruits membrane transglutaminase 2 during erythroid differentiation of the human chronic myelogenous leukemia K562 cells.
abstract: By employing proteomics analysis tool, we examined the effects of GD3 synthase expression on the differentiation properties of chronic myelogenous leukemia (CML)-derived leukemia cells K562. Forced expression of GD3 synthase induced erythroid differentiation as determined by an increase in glycophorin A expression and synthesis of hemoglobins. The proteomic analysis revealed that 15 proteins were increased by GD3 synthase. In contrast, we observed three protein gel spots decreased in contents in the cell membranes of GD3 synthase-transfected K562 cells. Among the increased proteins, membrane transglutaminase 2 (TG2) was specifically increased in the cell membrane of GD3 synthase-transfected K562 cells. Then, we generated the GD3 synthase-transfected cells in the K562 cells. Interestingly, the TG2 level was increased in GD3 synthase-transfected cells compared with vector- and plasma membrane-associated ganglioside sialidase (Neu3)-transfected cells. In addition, its ability to be photoaffinity-labeled with [alpha-(32)P]GTP was also increased in the GD3 synthase- and TG2-transfected cells. Moreover, small interfering RNA (siRNA) analysis for the GD3 synthase showed the decrease or abolishment of the membrane TG2. Finally, GD3 synthase-transfected cells accelerated the erythroid differentiation. Therefore, we propose that the recruitment of TG2 into membranes by GD3 might play an important role in the erythroid differentiation in K562 cells.
authors.affiliation: Molecular and Cellular Glycobiology Unit, Department of Biological Science, SungKyunKwan University, Suwon, Kyunggi-Do, Korea.
authors.forename: Sung-Koo
authors.initials: SK
authors.lastname: Kang
authors.forename: Yong-Sam
authors.initials: YS
authors.lastname: Kim
authors.forename: Yun-Jeong
authors.initials: YJ
authors.lastname: Kong
authors.forename: Kwon-Ho
authors.initials: KH
authors.lastname: Song
authors.forename: Young-Chae
authors.initials: YC
authors.lastname: Chang
authors.forename: Young-Guk
authors.initials: YG
authors.lastname: Park
authors.forename: Jeong-Heon
authors.initials: JH
authors.lastname: Ko
authors.forename: Young-Choon
authors.initials: YC
authors.lastname: Lee
authors.forename: Cheorl-Ho
authors.initials: CH
authors.lastname: Kim
mesh_terms: D015152:Blotting, Northern; D015153:Blotting, Western; D054337:Cell Dedifferentiation; D015180:Electrophoresis, Gel, Two-Dimensional; D041905:Erythroid Cells / Q000166:cytology / Q000378:metabolism*; D005434:Flow Cytometry; D019204:GTP-Binding Proteins / Q000378:metabolism*; D006801:Humans; D047468:Immunoprecipitation; D020014:K562 Cells; D015464:Leukemia, Myelogenous, Chronic, BCR-ABL Positive / Q000235:genetics / Q000378:metabolism / Q000473:pathology; D008565:Membrane Proteins / Q000378:metabolism*; D048052:Mitogen-Activated Protein Kinase 3 / Q000235:genetics / Q000378:metabolism; D009439:Neuraminidase / Q000235:genetics / Q000378:metabolism; D051058:Oncogene Protein v-akt / Q000235:genetics / Q000378:metabolism; D010766:Phosphorylation; D000091345:Protein Glutamine gamma Glutamyltransferase 2; D034741:RNA, Small Interfering / Q000235:genetics; D020133:Reverse Transcriptase Polymerase Chain Reaction; D012799:Sialyltransferases / Q000235:genetics / Q000378:metabolism*; D011503:Transglutaminases / Q000378:metabolism*
chemical_list: D008565:Membrane Proteins; D034741:RNA, Small Interfering; D000091345:Protein Glutamine gamma Glutamyltransferase 2; D011503:Transglutaminases; D012799:Sialyltransferases; C043662:alpha-N-acetylneuraminate alpha-2,8-sialyltransferase; D051058:Oncogene Protein v-akt; D048052:Mitogen-Activated Protein Kinase 3; C465436:Neu3 protein, human; D009439:Neuraminidase; D019204:GTP-Binding Proteins