Expression of Abh, Lewis and Related Tissue Antigens in the Human Thymus

Pendu, Jacques Le; Dalix, A.M.; Mollicone, Rosella; Oriol, Rafaël

doi:10.1111/j.1744-313x.1989.tb00444.x

Cited by 9 publications

(4 citation statements)

References 29 publications

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“…Pendu et al (18) have previously investigated the human juvenile thymus (age range 1 day -12 years) showing that the Hassal's bodies display ABH and Lewis antigens. The distribution of the carbohydrates expressed by the epithelial cells of fetal thymic tissue in our investigation, is similar to what is described by Pendu et al(18): a strong expression of Le-y, Le-x and s-Le-x by the Hassal's bodies, a weaker expression by the medullary cells, and almost none by the cortical cells. Apparently, there seems to be no difference in expression of type 2 chain carbohydrates in fetal and juvenile thymus.…”

supporting

confidence: 91%

Histo‐blood group antigens in human fetal thymus and in thymomas

Engel¹,

Dabelsteen²,

Francis³

et al. 1996

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The glycosylation of epithelial cell surface antigens follows cellular differentiation, and changes in the pattern of expression are seen in various premalignant and malignant epithelial lesions. The distribution of type‐2 chain ABH‐carbohydrate structures (N‐acetyl‐lactosamine, H‐type 2 chain, Le‐y, Le‐x and sialyl‐Le‐x) of the ABO‐histo‐blood group system was investigated in 19 normal fetal thymuses (gestational age 16 to 39 weeks) and in 19 thymomas in order to study possible tumor‐associated changes in the glycosylation pattern. The material was investigated by immunochemical stainings of formalin‐fixed paraffin‐imbedded tissue using monoclonal antibodies with defined specificity. In fetal thymus the epithelial cells of the medulla and the Hassal's bodies strongly expressed elongated carbohydrate structures (Le‐y, Le‐x and sialyl‐Le‐x). In a few cases the cortical epithelial cells weakly expressed Le‐x and sialyl‐Le‐x. Compared with fetal thymus 16 of the thymomas showed a total loss, or a very much reduced expression of elongated carbohydrate structures. Three thymomas, which histologically had been reclassified according to Kirchner & Müller‐Hermelink (14) as high grade thymic carcinomas, revealed strong expression of Le‐y, moderate expression of Le‐x and weak expression of sialyl‐Le‐x. This is of interest as in other tumors Le‐y is correlated with increased cell motility and with poor prognosis.

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supporting

confidence: 91%

Histo‐blood group antigens in human fetal thymus and in thymomas

Engel¹,

Dabelsteen²,

Francis³

et al. 1996

APMIS

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“…ABH histo-blood group antigens and precursor structures are present mainly in the medulla of the human thymus (12, 156) ( Table 6). The type of ABH antigen structures has not been clearly defined, but studies indicate that both types I, 2, and 3 precursor structures are present in thymus from children between 1 month and 2 years (157). The strongest expression is seen in the Hassall's bodies, in which both histo-blood group antigen A and the precursor H antigen are expressed in a secretor-dependent way.…”

Section: A Thymusmentioning

confidence: 99%

Tissue distribution of histo‐blood group antigens.

Ravn

Dabelsteen

2000

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The introduction of immunohistochemical techniques and monoclonal antibodies to specific carbohydrate epitopes has made it possible to study in detail the tissue distribution of histo-blood group antigens and related carbohydrate structures. The present paper summarizes the available data concerning the histological distribution of histo-blood group antigens and their precursor structures in normal human tissues. Studies performed have concentrated on carbohydrate antigens related to the ABO, Lewis, and TTn blood group systems, i.e. histo-blood group antigens carried by type 1, 2, and 3 chain carrier carbohydrate chains. Histo-blood group antigens are found in most epithelial tissues. Meanwhile, several factors influence the type, the amount, and the histological distribution of histoblood group antigens, i.e. the ABO, Lewis, and saliva-secretor type of the individual, and the cell- and tissue type. Oligosaccharides with blood-group specificity are synthesized by the stepwise action of specific gene-encoded glycosyltransferases. In general, this stepwise synthesis of histo-blood group antigens correlates with cellular differentiation. The H and the Se genes both encode an al-2fucosyltransferase, which is responsible for the synthesis of blood group antigen H from precursor disaccharides. A new model for the participation of the Se/H-gene-encoded glycosyl transferases in synthesis of terminal histo-blood group antigens in human tissues is proposed; the type and degree of differentiation rather than the embryologic origin determines whether it is the H or the Se gene-encoded transferases that influence expression of terminal histo-blood group antigens in tissues.

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“…They have also been detected on the thymus epithelium, the skin and some neurons of the peripheral nervous system of a few mammalian species such as rat, rabbit, baboon and human. In contrast, they were never observed on connective tissues or muscles [2–5]. Their appearance on vascular endothelium is a rather recent event in evolutionary terms as endothelial expression is restricted to Old World monkeys and humans.…”

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Comparison of the three rat GDP‐L‐fucose:β‐D‐galactoside 2‐α‐L‐fucosyltransferases FTA, FTB and FTC

Bureau¹,

Marionneau²,

Cailleau-Thomas³

et al. 2001

European Journal of Biochemistry

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The complete coding sequences of three rat a1,2fucosyl-transferase genes were obtained. Sequence analysis revealed that these genes, called FTA, FTB and FTC, were homologous to human FUT1, FUT2 and Sec1, respectively. A distance analysis between all a1,2fucosyl-transferase sequences available showed that the two domains of the catalytic region evolved differently with little divergence between the FUT2 and Sec1 N-terminal domains, quite distant from that of FUT1. At variance, FUT1 and FUT2 C-terminal domains were less distant while a high evolutionary rate was noted for Sec1 C-terminal domain. Whereas FTA and FTB encode typical glycosyltransferases, FTC lacks the homologous start codon and encodes a protein devoid of intracellular and transmembrane domains. It is located on rat chromosome 1q34. Transfection experiments revealed that unlike FTA and FTB, FTC does not generate enzyme activity. Analysis by flow cytometry showed that H type 2 epitopes were synthesized in Chinese hamster ovary cells transfected by both FTA and FTB cDNA, but only FTB transfectants possessed H type 3 determinants. In REG rat carcinoma cells, both FTA and FTB allowed synthesis of H type 2 and H type 3 at the cell surface. Western blots showed that, in both cell types, FTA was able to synthesize H type 2 epitopes on a larger set of glycoproteins than FTB. Analysis of the kinetic parameters obtained using small oligosaccharides revealed only a slight preference of FTA for type 2 over other types of acceptor substrates, whereas FTB was barely able to fucosylate this substrate.

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Expression of Abh, Lewis and Related Tissue Antigens in the Human Thymus

Cited by 9 publications

References 29 publications

Histo‐blood group antigens in human fetal thymus and in thymomas

Histo‐blood group antigens in human fetal thymus and in thymomas

Tissue distribution of histo‐blood group antigens.

Comparison of the three rat GDP‐L‐fucose:β‐D‐galactoside 2‐α‐L‐fucosyltransferases FTA, FTB and FTC

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