Linked Life Data

1686414

Source:http://linkedlifedata.com/resource/pubmed/id/1686414

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1992-3-31
pubmed:abstractText
This chapter has reviewed the nature of antigens of the MNSs blood group system. The structures of the proteins and the molecular features and organization of glycophorin genes were described, emphasizing their domain arrangement and the extensive sequence homology that indicates that their common and variant alleles belong to a single gene family. Methods currently used to examine these antigens are immunoblotting and DNA typing. The majority of variant genes are hybrids of parent glycophorin genes in a variety of arrangements; they contain no other sequences but those of the parent genes. The structures of the hybrids are summarized in Figure 8. Several hybrids appear to have arisen by unequal homologous recombination but others appear to have occurred through gene conversion. In this system the molecular genetic basis for a single variant phenotype may differ, as documented by gene rearrangements that appear to have occurred, as separate events, at different sites in the same intron; this has resulted in protein structures (hence phenotypes) that are identical. For example, unequal homologous recombination occurring within intron 3 can have given rise to only a limited number of phenotypes, namely alpha M-delta S, alpha N-delta S, alpha M-delta S, alpha N-delta S and delta-alpha. In addition, different sites of an exon may have been involved in gene rearrangements through gene conversion leading to nearly identical protein structures, yet different serological phenotypes. Thus, gene conversion could be more significant for generation of antigenic diversification as the number of possible new alleles is quite large. The participation of the HGpE gene in these rearrangements would make this number even larger. New sites and the expressed pseudoexon have created the epitopes of the variant phenotypes, and sequences specific for several variant antisera have been identified. Thus, the molecular basis for several serological reactions involving this system is now better understood.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0950-3536
pubmed:author
pubmed:issnType
Print
pubmed:volume
4
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
821-48
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Biochemistry and molecular biology of MNSs blood group antigens.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review