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  • 1
    ISSN: 1432-1211
    Keywords: Key words Membrane protein ; Lu homologue ; Gene structure ; Laminin receptor ; Cell adhesion
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  The human Lutheran (Lu) blood group antigens are carried by two glycoproteins (gps) that belong to the immunoglobulin (Ig) superfamily. These gps represent adhesion molecules that function as the unique erythroid receptors for laminin. We report here the cloning and functional expression of the orthologous mouse Lu mRNA as well as the genomic organization of the mouse Lu gene. The deduced human and mouse Lu gps share 72.5% identity and similar organization of the Ig-like domains. As in the human, the mouse Lu gene is organized in 15 exons. The proximal promoter showed consensus CACC-binding sites whereas the distal promoter exhibits a GATA-1-binding site and multiple E boxes. Like the human gene, the mouse Lu gene is also widely expressed among tissues but is transcribed as a unique 2.4-kb mRNA species. Expression of the mouse Lu mRNA is upregulated upon dimethyl sulfoxide-induced erythroid differentiation of murine erythroleukemia cells (MEL). During mouse embryonic development, the Lu transcript is detected as early as day 7 of gestation. Analysis of transfected human erythroleukemia K562 cells indicated that the adhesive properties of the Lu gps to laminin are conserved between human and mouse.
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1432-1203
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary A cDNA clone, RhIXb (1384 bp), encoding the entire protein sequence of a human blood group Rh polypeptide has been used to map the Rh locus, by in situ hybridization, to the region p34.3–p36.1 of chromosome 1. Two other unrelated cDNA clones, pUCA2 (750bp) and pUCIII (1600 bp), isolated during the cloning procedure of the Rh cDNA were investigated simultaneously, and assigned to chromosome 3p21.1–3p22 (clone pUCA2) and to chromosome 22q12.1–22q13.1 (clone pUCIII).
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-1211
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Rh-related transcripts present in bone marrow samples from several species of nonhuman primates (chimpanzee, gorilla, gibbon, crab-eating macaque) have been amplified by RT-polymerase chain reaction using primers deduced from the sequence of human RH genes. Nucleotide sequence analysis of the nonhuman transcripts revealed a high degree of similarity to human blood group Rh sequences, suggesting a great conservation of the RH genes throughout evolution. Full-length transcripts, potentially encoding 417 amino acid long proteins homologous to Rh polypeptides, were characterized, as well as mRNA isoforms which harbored nucleotide deletions or insertions and potentially encode truncated proteins. Proteins of 30–40 000 M r, immunologically related to human Rh proteins, were detected by western blot analysis with antipeptide antibodies, indicating that Rh-like transcripts are translated into membrane proteins. Comparison of human and nonhuman protein sequences was pivotal in clarifying the molecular basis of the blood group C/c polymorphism, showing that only the Pro103Ser substitution was correlated with C/c polymorphism. In addition, it was shown that a proline residue at position 102 was critical in the expression of C and c epitopes, most likely by providing an appropriate conformation of Rh polypeptides. From these data a phylogenetic reconstruction of the RH locus evolution has been calculated from which an unrooted phylogenetic tree could be proposed, indicating that African ape Rh-like genes would be closer to the human RhD gene than to the human RhCE gene.
    Type of Medium: Electronic Resource
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  • 4
    ISSN: 1432-1076
    Keywords: Neonatal neutropenia ; Iso-immune neutropenia ; Anti-neutrophil antibody ; CD16 molecule
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract We report a case of transient neonatal neutropenia due to a maternal iso-immunization against a non polymorphic region of the glycosylphosphatidylinositollinked Fc receptor type III (CD16) on granulocytes. The mother's granulocytes were typed NA1-negative, NA2-negative and CD16-negative with human and monoclonal antibodies whereas her lymphocytes express the CD16 molecule. Expression of other markers were comparable to the controls. Flow cytometric analysis showed that maternal antibody recognized the granulocytes but not the lymphocytes from blood bank donors and that its binding was decreased on normal, phospholipase C-treated, granulocytes. The binding of commercial CD16 monoclonal antibodies was also dramatically decreased on normal granulocytes pre-incubated with maternal serum. The CD16 specificity of the antibody was confirmed by negative reactions with another CD16-deficient granulocytes. This observation leads us to conclude that celllineage specific differences of CD16 molecules are recognized by the patient's antibody. Moreover, we confirm that the absence of the FcRIII (CD16) on granulocytes is not associated with any pathology or susceptibility to infections and that, in the children, the blockade of this receptor by the maternal antibody only led to moderate neutropenia.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1279-8509
    Keywords: Autoimmune neutropenia ; IgM anti-i antibody ; VH4-21 gene ; B-cell lymphoma ; Monoclonal IgM-(kappa)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract A sixty-year old female was referred to the Internal Medicine Department for the treatment of a diffuse high-grade non Hodgkin’s lymphoma. She presented episodes of fever in a context of neutropenia (neutrophils 0.35 × 109/l from 1.6 × 109/l white blood cells). Hemoglobin level was 8.2 g/dl and platelets 132 × 1012/l. A monoclonal IgM-(kappa) protein (48 g/l) was detected in her serum. A direct antiglobulin test on the red cells proved positive with anti-C3d but not with anti-IgG antiglobulin, due to the presence of an IgM cold antibody with a serological anti-i specificity. The IgM antibody was found on the patient’s neutrophils as well as in her serum. This antibody recognized all neutrophils tested in conventional serological tests whatever the neutrophil phenotypes in systems NA, NB, and 5. It was demonstrated that it recognized the i antigen expressed on the neutrophils. These results suggest that a cold agglutinin anti-i might be responsible for neutropenia in some patients.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 9 (1982), S. 0 
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: A group AB mother (Mrs P.D.) gave birth to a group O female baby (C.D.). Extensive study of the blood group genetic markers in both the parents and the child, carried out on several occasions, showed nothing unusual outside the ABO system. Mrs P.D. then, gave birth to a second female baby who was also group O. Mrs P.D. had normal amounts of A, B, H and Lewis antigens in her saliva. The H, A and B agglutinability of her red cells was in the range of normal A2B group. This A2B blood group was characterized by very low A gene-specified glycosyltransferase activity in serum. Moreover this activity was undettable in red blood cell membranes. These results are discussed in the light of various hypotheses in order to explain this unusual transmission of ABO blood group.
    Type of Medium: Electronic Resource
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  • 7
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 5 (1978), S. 0 
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The product of the A blood group gene in the erythrocyte membrane and serum from ‘weak A’ variants was investigated using low and high molecular weight acceptors and compared with common A1 and A2 blood samples. A reduced enzyme activity was detected, but only in some of the A variants, namely the A3 (eight out of eleven), Am or Ay samples. Other sera from A3 (three out of eleven), Ax, Aend or Ael individuals were apparently devoid of enzyme activity.A kinetic study by temperature inactivation of A blood group sera also showed that A enzymes are more labile than B enzymes from BI or BII sera. Moreover, in one case (A3 sample Del.), a very fast inactivation of the A enzyme was observed, suggesting the occurrence of a variant enzyme qualitatively different from the others so far studied.The erythrocyte membrane preparations from all A variants contained no detectable A enzyme activity except for the A1 and A2 samples, the former being three to five times more active than the latter. The B enzyme activities from four samples of B RBC tested were comparatively stronger than the A enzyme activity of A1 RBC.The results were discussed and it was suggested that the synthesis and/or the secretion of the A enzyme in the organism is not uniform from one tissue to another, but could depend on which of the ‘weak A’ alleles or modifier genes is involved.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 3 (1976), S. 0 
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: From the variations of α-N-acetylgalactosaminyltransferases activities with the pH, evidence was obtained for the recognition of A1A2 heterozygotes in normal A blood group sera.Besides, unusual transferase properties associated with two A2 sera from individuals out of AAm1 siblings, lead to the identification of the very infrequent A2AAm1 genotypes. These results strongly support the simultaneous coexistence of both A1 and A2 transferases in heterozygotes' sera, and bring some new information on the genetical background of the Am phenotype.The meaning of transferase properties directly determined on whole sera is briefly discussed.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Amsterdam : Elsevier
    Archives of Biochemistry and Biophysics 222 (1983), S. 231-244 
    ISSN: 0003-9861
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
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  • 10
    ISSN: 0378-1119
    Keywords: Cap site ; blood-group antigens ; cis-acting sequences ; erythroid-specific regulation ; recombinant DNA ; sialoglycoproteins
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology
    Type of Medium: Electronic Resource
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