EXPRESSION OF Xg AND THE 12E7 ANTIGEN IN PRIMATES

Shaw, Marie; Tippett, Patricia; Delhanty, Joy D. A.; Andrews, M.; Goodfellow, Peter N.

doi:10.1111/j.1744-313x.1985.tb00837.x

Cited by 6 publications

(3 citation statements)

References 9 publications

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“…This is interesting, since previous studies have shown that the Xga antigen is also a protease-sensitive component of the red cell membrane (Habibi et al, 1979). Recent investigations of the expression of Xga and 12E7 on primate red cells have indicated that both Xg(a +) and Xg(a -) gibbon erythrocytes failed to express high levels of 12E7 antigen, suggesting that Xga and 12E7 are different epitopes, but it is not established whether these antigens are present on the same molecule (Shaw et al, 1985).…”

Section: Discussionmentioning

confidence: 99%

Immunochemical characterization of the human blood cell membrane glycoprotein recognized by the monoclonal antibody 12E7

Latron

Blanchard

Cartron

1987

Biochemical Journal

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The 12E7 murine monoclonal antibody recognizes a protease-sensitive component of human red cells, platelets and lymphocytes which could not be detected on granulocytes. Scatchard analyses indicated that the 125I-labelled antibody binds to 1000, 4000 and 27,000 antigen sites on each red cell, platelet and lymphocyte respectively, with a binding constant ranging from 4 x 10(7) to 9 x 10(7) M-1. The membrane components recognized by the monoclonal antibody were characterized by immunostaining on nitrocellulose sheets. A 28 kDa sialoglycoprotein was visualized following electrophoretic transfer of the red cell and lymphocyte membrane proteins separated by SDS/polyacrylamide-gel electrophoresis. Another component of 25 kDa was also clearly identified in the lymphocyte and platelet lysates, but was barely detectable in the red cell membrane preparations. Enzyme treatment of intact platelets, as well as analysis of the membrane and cytosolic preparations from these cells, have shown that the 25 kDa component was of cytoplasmic origin. The mobility of the 28 kDa membrane component is decreased following neuraminidase treatment of intact blood cells, but these cells still react normally with the monoclonal antibody, indicating that sialic acids are not required for binding. The 28 kDa component is present on red cell membranes prepared from S-s-U-, En(a-) and Gerbich(-) individuals, demonstrating that it is a new sialoglycoprotein not derived from glycophorins A, B, C or D. The 28 kDa component was totally solubilized with 0.1% Triton X-100 from red cell membranes and behaves like the other red cell membrane sialoglycoproteins since it was extracted in the aqueous phase following chloroform/methanol/water or butanol/water partitionings. The 28 kDa component could be partially purified by h.p.l.c. gel permeation chromatography and preparative SDS/polyacrylamide-gel electrophoresis. The material finally obtained strongly inhibits the 12E7 monoclonal as well as human anti-Xga antibodies, suggesting either that the 28 kDa glycoprotein carries both antigens or that the 12E7 and Xga-active molecules copurified.

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Section: Discussionmentioning

confidence: 99%

Immunochemical characterization of the human blood cell membrane glycoprotein recognized by the monoclonal antibody 12E7

Latron

Blanchard

Cartron

1987

Biochemical Journal

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“…CD99 was detected on red cells and fi broblasts of chimpanzees and gorillas, but not of orangutans or any of the other mammals tested [21,98,99] . Other great apes (67 chimpanzees, two gorillas, 20 orangutans, and fi ve gibbons of the species Hylobates pileatus ) as well as various monkeys (including 60 baboons), and a few non -primates, were all Xg(a -).…”

Section: Xg a And Cd99 In Animalsmentioning

confidence: 99%

Xg Blood Group System

Daniels

2013

Human Blood Groups

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“…CD99 was detected on RBCs and fibroblasts of chimpanzees and gorillas, but not of orangutans or any of the other mammals tested. 23…”

Section: Biochemistrymentioning

confidence: 99%

XG: the forgotten blood group system

Johnson¹

2011

Immunohematology

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The XG blood group system is best known for its contributions to the fields of genetics and chromosome mapping. This system comprises two antigens, Xg a and CD99, that are not antithetical but that demonstrate a unique phenotypic relationship. XG is located on the tip of the short arm of the X chromosome with exons 1 to 3 present in the pseudoautosomal region of the X (and Y) chromosome(s) and exons 4 to 10 located only on the X chromosome. Xg a demonstrates a clear X-linked pattern of inheritance. MIC2, the gene encoding the CD99 antigen, is found in the pseudoautosomal region of both the X and Y chromosomes. Anti-Xg a is comparatively rare, and only two examples of anti-CD99 have ever been identified. Alloanti-Xg a is considered clinically insignificant; only one example of autoanti-Xg a has been reported, but it resulted in severe hemolytic anemia. Insufficient data exist to determine the clinical significance of anti-CD99. Linkage of XG to several X-borne genes encoding inherited disorders has been demonstrated. CD99 is an adhesion molecule, and high levels are associated with some types of cancer.

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EXPRESSION OF Xg AND THE 12E7 ANTIGEN IN PRIMATES

Cited by 6 publications

References 9 publications

Immunochemical characterization of the human blood cell membrane glycoprotein recognized by the monoclonal antibody 12E7

Immunochemical characterization of the human blood cell membrane glycoprotein recognized by the monoclonal antibody 12E7

Xg Blood Group System

XG: the forgotten blood group system

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