Back to Search
Start Over
Evolution of glycophorin A in the hominoid primates studied with monoclonal antibodies, and description of a sialoglycoprotein analogous to human glycophorin B in chimpanzee.
- Source :
-
Journal of immunology (Baltimore, Md. : 1950) [J Immunol] 1986 Apr 01; Vol. 136 (7), pp. 2504-9. - Publication Year :
- 1986
-
Abstract
- Comparison of human and primate erythrocyte membrane sialoglycoproteins showed that common chimpanzee, dwarf chimpanzee, gorilla, orangutan, and gibbon have major periodic acid Schiff-positive proteins resembling human glycophorin A (GPA) monomer and dimer in electrophoretic mobility on sodium dodecyl sulfate-polyacrylamide gels. Immunoperoxidase staining of Western blots with monoclonal antibodies to human GPA showed that these primate bands express some GPA antigenic determinants. A new sialoglycoprotein analogous to human glycophorin B (GPB) was detected in common chimpanzee. Although human MN blood group phenotype results from an amino acid polymorphism of GPA, Western blots showed that in chimpanzee sialoglycoprotein (GPAch) always expresses the M blood group, whereas chimpanzee sialoglycoprotein (GPBch) expresses either the N blood group or a null phenotype. This result explains the detection of M and MN, but not of N, blood group phenotypes in chimpanzee. GPBch has higher apparent m.w. than human GPB, is present in the erythrocyte membrane in greater quantity than human GPB, and contains trypsin cleavage site(s) and the 10F7 determinant (both found on human GPA but not GPB). Expression of human GPA antigenic determinants was consistent with the phylogeny of the hominoid primates; common and dwarf chimpanzee expressed most of the determinants tested, gorilla and orangutan an intermediate number, and gibbon and siamang the least. Of the GPA antigenic determinants examined, the MN blood group determinants were most consistently expressed during evolution of the hominoid primates. The results suggested that variability in expression of GPA antigenic determinants between species was due to both differences in amino acid sequence and glycosylation.
- Subjects :
- Adult
Animals
Antigen-Antibody Reactions
Aotus trivirgatus
Blood Grouping and Crossmatching
Collodion
Electrophoresis, Polyacrylamide Gel
Erythrocyte Membrane analysis
Glycophorins immunology
Gorilla gorilla
Hemagglutination Tests
Humans
Hylobates
Membrane Proteins analysis
Paper
Pongo pygmaeus
Trypsin
Antibodies, Monoclonal
Biological Evolution
Glycophorins analysis
Pan troglodytes blood
Sialoglycoproteins analysis
Subjects
Details
- Language :
- English
- ISSN :
- 0022-1767
- Volume :
- 136
- Issue :
- 7
- Database :
- MEDLINE
- Journal :
- Journal of immunology (Baltimore, Md. : 1950)
- Publication Type :
- Academic Journal
- Accession number :
- 3950419