Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1999-2-25
pubmed:abstractText
The expression of protein 4.2 in normal human erythroid cells was studied utilizing erythroblasts from bone marrow and erythroid cells cultured by the two-phase liquid culture method from burst-forming unit erythroid (BFU-E) in peripheral blood. As opposed to spectrin, which was expressed in erythroid progenitors or very early erythroblasts, protein 4.2 was first detected in late erythroblasts with a morphology nearly identical to orthochromatic erythroblasts. Among the various major membrane proteins, the expression of protein 4.2 was the latest. At the gene level, protein 4.2 gene mRNA was expressed in early erythroblasts. During normal erythroid maturation, the expression of seven different protein 4.2 gene products was observed by Southern blot analysis. These seven gene products appeared to be derived from protein 4.2 gene in the presence or absence of skipping of the 90 bp in exon 1, exon 3, and/or exon 5, as judged by deduction from the protein 4.2 sequence. Therefore, it can be speculated that protein 4.2 is expressed after the cytoskeletal network has been constructed and assembled with integral proteins in the membrane lipid bilayer.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0301-472X
pubmed:author
pubmed:issnType
Print
pubmed:volume
27
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
54-62
pubmed:dateRevised
2011-6-20
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Late expression of red cell membrane protein 4.2 in normal human erythroid maturation with seven isoforms of the protein 4.2 gene.
pubmed:affiliation
Department of Medicine, Kawasaki Medical School, Kurashiki City, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't