Revue française de transfusion et immuno-hématologie 

About: Revue française de transfusion et immuno-hématologie is an academic journal. The journal publishes majorly in the area(s): Monoclonal antibody & Antigen. It has an ISSN identifier of 0338-4535. Over the lifetime, 720 publications have been published receiving 2484 citations.

ABH and Lewis glycosyltransferases in human red cells, lymphocytes and platelets

Abstract: Summary The α-3-N-acetylgalactosaminyl-, α-3-D-galactosyl- and α-2-L-fucosyl-transferases, the direct products of the respective A, B and H blood group genes have been identified in red cells, lymphocytes and platelets homogenates from secretor and non-secretor individuals of appropriate ABO group. The H enzyme was not detectable in red cell membranes from Bombay individuals. Since the uptake of A antigen from the plasma has been shown at least for red cells [10] and lymphocytes [25] , the present results suggest that the ABH determinants of the blood cells may arise both from intrinsic and extrinsic origin, but the relative contribution of each mechanism is not known. In contrast, the Lewis enzyme was absent or inactive in all the investigated blood cell samples, which can be considered as an additional proof that the Lewis antigens of these cells are entirely derived from the plasma.

Structural and biological aspects of blood group I and i antigens on glycolipids and glycoproteins.

Abstract: Summary I and i oligosaccharide sequences are carried on a multiplicity of glycoproteins and glycosphingolipids They occur as accessible or as partially or totally masked antigens on the surface of diverse cell types and in certain secretions Changes in their expression may occur during differentiation, development, cell cycle and oncogenesis There is suggestive evidence that they may be coupled to receptor systems on lymphocyte membranes Monoclonal anti-I and i antibodies hold promise as reagents in biological chemistry

Serology, genetics and chemistry of the MNSs blood group system

Abstract: The MNSs blood group gene locus apparently corresponds to two adjacent and homologous genes which code for the amino acid sequences of two (MN and Ss) erythrocyte membrane sialoglycoproteins. The genes En, u and Mk represent alleles, silent at one or the other and at both loci, respectively. Amino acid polymorphisms at the first (Ser/Leu) and fifth (Gly/Glu) positions of the major (MN) glycoprotein account for the structural difference between the MN antigens. The N-terminal 26 residues of the Ss glycoprotein are completely identical with those of the blood group N-specific major glycoprotein, providing an explanation for the additional N receptor, denoted as 'N', on this molecule. A Met/Thr polymorphism at position 29 of the Ss glycoprotein represents the structural difference between the Ss antigens, as revealed by chemical modification experiments and sequence analysis. The Ux polymorphism, defined by a scarce serum (anti-Ux) directed against receptors within the homologous domains of the two glycoproteins, appears to be caused by differences in the Ss glycoprotein content between SS, Ss and ss red cells, rather than by an additional structural polymorphism on the Ss glycoprotein. The same explanation might also account for a further (Uz) polymorphism, defined by anti-Uz reacting with receptors which are located on a more interior portion of this molecule. Various factors such as the number of receptors per cell, their accessibility within the intact erythrocyte membrane as well as properties of the antibody (Uu genotype of the donor, method of absorption, the number of sites per antibody and its binding constant) contribute to the phenomenon that the capacity for reaction of the structurally identical N and 'N' antigens in intact red cells is different, thus enabling MN blood typing, despite the presence of 'N' receptors in MM erythrocytes.