Linked Life Data

20101026

Source:http://linkedlifedata.com/resource/pubmed/id/20101026

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2010-3-26
pubmed:abstractText
The cell-surface straight and branched repeats of N-acetyllactosamine (LacNAc) units, called poly-LacNAc chains, characterize the histo-blood group i and I antigens, respectively. The transition of straight to branched poly-LacNAc chain (i to I) is determined by the I locus, which expresses 3 IGnT transcripts, IGnTA, IGnTB, and IGnTC. Our previous investigation demonstrated that the i-to-I transition in erythroid differentiation is regulated by the transcription factor CCAAT/enhancer binding protein alpha (C/EBPalpha). In the present investigation, the K-562 cell line was used as a model to show that the i-to-I transition is determined by the phosphorylation status of the C/EBPalpha Ser-21 residue, with dephosphorylated C/EBPalpha Ser-21 stimulating the transcription of the IGnTC gene, consequently resulting in I branching. Results from studies using adult erythropoietic and granulopoietic progenitor cells agreed with those derived using the K-562 cell model, with lentiviral expression of C/EBPalpha in CD34(+) hematopoietic cells demonstrating that the dephosphorylated form of C/EBPalpha Ser-21 induced the expression of I antigen, granulocytic CD15, and also erythroid CD71 antigens. Taken together, these results demonstrate that the regulation of poly-LacNAc branching (I antigen) formation in erythropoiesis and granulopoiesis share a common mechanism, with dephosphorylation of the Ser-21 residue on C/EBPalpha playing the critical role.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1528-0020
pubmed:author
pubmed:issnType
Electronic
pubmed:day
25
pubmed:volume
115
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2491-9
pubmed:meshHeading
pubmed-meshheading:20101026-Antigens, CD34, pubmed-meshheading:20101026-CCAAT-Enhancer-Binding Protein-alpha, pubmed-meshheading:20101026-Carbohydrate Sequence, pubmed-meshheading:20101026-Cell Differentiation, pubmed-meshheading:20101026-Erythropoiesis, pubmed-meshheading:20101026-Granulocytes, pubmed-meshheading:20101026-Humans, pubmed-meshheading:20101026-I Blood-Group System, pubmed-meshheading:20101026-K562 Cells, pubmed-meshheading:20101026-Membrane Proteins, pubmed-meshheading:20101026-Molecular Sequence Data, pubmed-meshheading:20101026-Mutagenesis, Site-Directed, pubmed-meshheading:20101026-N-Acetylglucosaminyltransferases, pubmed-meshheading:20101026-Phosphorylation, pubmed-meshheading:20101026-Polysaccharides, pubmed-meshheading:20101026-Promoter Regions, Genetic, pubmed-meshheading:20101026-Serine
pubmed:year
2010
pubmed:articleTitle
Phosphorylation status of transcription factor C/EBPalpha determines cell-surface poly-LacNAc branching (I antigen) formation in erythropoiesis and granulopoiesis.
pubmed:affiliation
Institute of Biochemical Sciences, National Taiwan University, Taipei 106, Taiwan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't