Blood-group-I activity associated with band 3, the major intrinsic membrane protein of human erythrocytes

Childs, Robert A.; Feizi, Ten; Fukuda, Minoru; Hakomori, S

doi:10.1042/bj1730333

Cited by 73 publications

(10 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In addition to a major role in anion transport (Low 1986), it has been implicated in transmembrane moveOffprint requests to: M. Palatnik ments of water (cf. Low 1986), urea (Toon and Solomon 1986) and glucose (Langdon and Holman 1988), and is associated with several blood-group antigens: Ii (Childs et al 1978) and ABH (Moore and Green 1987), but not Rh (Moore and Green 1987) or KeN (Redman 1988). Apparently, it participates in the process of invasion of human erythrocytes by Plasmodiurn falciparum (Okoye and Bennett 1985).…”

Section: Introductionmentioning

confidence: 99%

The 60 and 63 kDa proteolytic peptides of the red cell membrane band-3 protein: their prevalence in human and non-human primates

et al. 1990

View full text Add to dashboard Cite

Three phenotypes based on the polymorphism of band-3 protein from human red cells are described. Limited proteolysis of intact red cells from most individuals (homozygotes) yields a peptide of 60 kDa, but in some cases (heterozygotes), there is also a 63-kDa peptide, and rarely only the single peptide of 63 kDa is found. This is the first description of the 63-kDa homozygote. The interpretation that the three phenotypes are controlled by two alleles of a single autosomal locus, with no dominance, is supported by population and family studies. The frequencies of the allele, which we designate as p63, is 0.041 +/- 0.0068 in Caucasoids and 0.125 +/- 0.0121 in Negroids. The electrophoretic profiles and molecular weights of the peptides obtained with several commercial proteases from Streptomyces griseus are similar to those obtained with chymotrypsin. Whereas band-3 protein in two New-World monkeys (Saimiri and Cebus) resisted pronase attack, an Old-World monkey (Macaca mulatta) was monomorphic for a 63-kDa fragment, and in an ape (Pan troglodytes), a doublet of 62 kDa and 64 kDa was found. Band-3 protein polymorphism appears to be a good marker for genetic differentiation in human populations.

show abstract

Section: Introductionmentioning

confidence: 99%

The 60 and 63 kDa proteolytic peptides of the red cell membrane band-3 protein: their prevalence in human and non-human primates

et al. 1990

View full text Add to dashboard Cite

show abstract

“…The zonal pattern of the whole sera (slot 1) showed a typical serum profile but with an elevated IgM component, while the nonbound fraction (slot 2) was de void of this band. The homogeneity, purity and specificity of the warm-eluted material (slots [3][4][5] 3. Zonal electrophoresis analysis of the starting serum (WS), pooled nonbound (NB) and warm eluted fractions (WE) from a serum sample (anti-i PE) run on the desialated orosomucoid affinity column.…”

Section: Resultsmentioning

confidence: 99%

Rapid Purification of Anti-I and Anti-i Cold Antibodies by Affinity Chromatography

Glick¹,

Oppenheim²

1985

Vox Sanguinis

View full text Add to dashboard Cite

A method is described for the rapid purification of serologically active high titer anti-I and anti-i cold antibodies from the sera of patients with chronic cold agglutinin disease (CCAD). The purification procedure is based on thermal affinity chromatography, using desialated orosomucoid (α(1)-acid glycoprotein)-Sepharose 4B conjugated beads. The nature of the interaction between the cold agglutinins (CA) and the desialated orosomucoid is unknown. Inhibition studies, however, revealed that the cold hemagglutinating activities of all the anti-i sera were inhibited by desialated orosomucoid while only 1 out of 4 of the anti-I sera was similarly affected. Anti-I or anti-i antibodies were separated from whole sera in 7 out of 7 samples with a recovery in most cases of 100% of the cold hemagglutinating activity. The resultant products were purified monoclonal IgM fractions which could react with anti-χ and anti-µ but not with anti-λ, sera. The homogeneity, purity and specificity of all preparations were confirmed by immunodiffusion analysis against purified I and i blood group antigens isolated from human erythrocyte membranes, zonal and right-angle electrophoresis and hemagglutination or hemagglutination inhibition studies.

show abstract

“…In addition, structural studies of glycopeptides of bovine thymus plasma membranes (26) (17). Moreover, polyglycosyl peptides have recently been isolated from Pronase-digested erythrocyte membranes (27) (8).…”

Section: Discussionmentioning

confidence: 99%

I and i antigens of human peripheral blood lymphocytes cocap with receptors for concanavalin A.

Feizi

Kapadia

Yount³

1980

Proc. Natl. Acad. Sci. U.S.A.

Self Cite

View full text Add to dashboard Cite

Surface immunofluorescence experiments using a human anti-i and two anti-I antisera have been performed on human peripheral blood lymphocytes. These are known to contain cold-reactive monoclonal IgM antibodies against the carbohydrate sequence:Galfl -4GlcNAc#1 -3Galjfl 4GlcNAc/31 -3Gal-(anti-i Den) and the 1 --4, 1 -6 domain (anti-I Ma) and the 1 --4, 1 3 domain (anti-I Step) of the branched I-active structure:Galf1l 4GlcNAcfll \6G lfli -4GIcNAcfl -3Gal-A high proportion of B-and T-type lymphocytes express these I and i determinants. In the presence of anti-human immunoglobulin, the cold-reactive membrane-associated complexes of I-anti-I and i-anti-i become stabilized, and redistribution (with patching and capping) can be elicited at 370C. Dual fluorescence experiments have shown striking concordant staining of I or i (fluorescein) caps and patches with concanavalin A (rhodamine) reactive sites on normal and leukemic cells, suggesting that a proportion of I and i active structures of lymphocyte membranes are structurally associated or physiologically coupled with glycoproteins carrying oligosaccharides with branched mannosyl cores.

show abstract

Blood-group-I activity associated with band 3, the major intrinsic membrane protein of human erythrocytes

Cited by 73 publications

References 19 publications

The 60 and 63 kDa proteolytic peptides of the red cell membrane band-3 protein: their prevalence in human and non-human primates

The 60 and 63 kDa proteolytic peptides of the red cell membrane band-3 protein: their prevalence in human and non-human primates

Rapid Purification of Anti-I and Anti-i Cold Antibodies by Affinity Chromatography

I and i antigens of human peripheral blood lymphocytes cocap with receptors for concanavalin A.

Contact Info

Product

Resources

About