Man, apes, and Old World monkeys differ from other mammals in the expression of alpha-galactosyl epitopes on nucleated cells.

Galili, Uri; Shohet, Stephen B.; Kobrin, Eugenia; Stults, Cheryl L. M.; Macher, Bruce A.

doi:10.1016/s0021-9258(19)77900-9

Cited by 854 publications

(140 citation statements)

References 48 publications

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“…Both the enzyme activity and the α-galactosyl epitope exist in most mammals except for humans, apes, and Old World monkeys. 80 These species instead possess the antibody against the α-galactosyl epitope. Presence of this antibody is the primary reason for acute rejection of pig organ xenotransplanted to humans.…”

Section: Evolution Of Abo Gen Es An D R Elated Gen Esmentioning

confidence: 99%

Review: ABO blood group system—ABH oligosaccharide antigens, anti-A and anti-B, A and B glycosyltransferases, and ABO genes

Yamamoto

2004

Immunohematology

103

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Section: Evolution Of Abo Gen Es An D R Elated Gen Esmentioning

confidence: 99%

Review: ABO blood group system—ABH oligosaccharide antigens, anti-A and anti-B, A and B glycosyltransferases, and ABO genes

Yamamoto

2004

Immunohematology

103

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“…Choosing the right donor is difficult, but nowadays pigs are considered as the most suitable donors of tissues and organs for human patients with chronic or endstage organ failure. Pigs share a large amount of similarities in organ anatomy and physiology; moreover, they share approximately 96% of their genetic identity with humans [2][3][4][5]. Unfortunately, the large phylogenetic distance between pig and human is the cause of the immunological barrier including immune response leading to hyperacute rejection (HAR), which currently makes pig-to-human of xenotransplantation unsuccessful [6].…”

Section: Introductionmentioning

confidence: 99%

Trichostatin A-Assisted Epigenomic Modulation Affects the Expression Profiles of Not Only Recombinant Human α1,2-Fucosyltransferase and α-Galactosidase A Enzymes But Also Galα1→3Gal Epitopes in Porcine Bi-Transgenic Adult Cutaneous Fibroblast Cells

Wiater

Samiec

Skrzyszowska

et al. 2021

IJMS

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This study was conducted to explore whether trichostatin A-assisted epigenomic modulation (TSA-EM) can affect the expression of not only recombinant human α1,2-fucosyltransferase (rhα1,2-FT) and α-galactosidase A (rhα-Gal A) immune system enzymes but also Galα1→3Gal epitopes in ex vivo proliferating adult cutaneous fibroblast cells (ACFCs) derived from hFUT2×hGLA bi-transgenic pigs that had been produced for the needs of future xenotransplantation efforts. The ACFC lines were treated with 50 nM TSA for 24 h and then the expression profiles of rhα1,2-FT and rhα-Gal A enzymes were analyzed by Western blot and immunofluorescence. The expression profiles of the Galα1→3Gal epitope were determined by lectin blotting and lectin fluorescence. The ACFCs derived from non-transgenic (nTG) pigs were served as the negative (TSA−) and positive (TSA+) control groups. For both hFUT2×hGLA and nTG samples, the expression levels of α1,2-FT and α-Gal A proteins in TSA+ cells were more than twofold higher in comparison to TSA− cells. Moreover, a much lower expression of the Galα1→3Gal epitopes was shown in TSA− hFUT2×hGLA cells as compared to the TSA− nTG group. Interestingly, the levels of Galα1→3Gal expression in TSA-treated hFUT2×hGLA and nTG ACFCs were significantly higher than those noticed for their TSA-untreated counterparts. Summing up, ex vivo protection of effectively selected bi-transgenic ACFC lines, in which TSA-dependent epigenetic transformation triggered the enhancements in reprogrammability and subsequent expression of hFUT2 and hGLA transgenes and their corresponding transcripts, allows for cryopreservation of nuclear donor cells, nuclear-transferred female gametes, and resultant porcine cloned embryos. The latter can be used as a cryogenically conserved genetic resource of biological materials suitable for generation of bi-transgenic cloned offspring in pigs that is targeted at biomedical research in the field of cell/tissue xenotransplantation.

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“…The other members (Table 2) had been deemed nonfunctional. 30,[34][35][36][37] The number of GT6 genes varies from species to species, and even within phylogenetic groups, the type and number of genes can vary significantly. 39…”

Section: Gene Name Gbgt1mentioning

confidence: 99%

The FORS awakens: review of a blood group system reborn

Hult¹,

Olsson

2017

Immunohematology

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The presence of the FORS1 antigen on red blood cells was discovered relatively recently, and in 2012, the International Society of Blood Transfusion (ISBT) acknowledged FORS as blood group system number 031. This rare antigen is carried by a glycosphingolipid and formed by elongation of the P antigen. Most people have naturally occurring anti-FORS1 in their plasma. The clinical significance of these antibodies is unknown in the transfusion setting, but they can hemolyze FORS1+ erythrocytes in the presence of complement in vitro. First believed to be part of the ABO system, it was later shown that the gene encoding the glycosyltransferase giving rise to FORS1 expression is GBGT1. This gene had previously been deemed nonfunctional in humans, but a mutation, so far only detected in FORS1+ individuals, restores the enzymatic activity. Tissue distribution of the antigen in FORS1+ individuals has not been studied in detail, although the gene is expressed in several cell types. The antigen itself is known to be a receptor for various pathogens and toxins and has been detected in different forms of cancer, but the implications thereof are not fully understood. Immunohematology 2017;33:64–72.

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Man, apes, and Old World monkeys differ from other mammals in the expression of alpha-galactosyl epitopes on nucleated cells.

Cited by 854 publications

References 48 publications

Review: ABO blood group system—ABH oligosaccharide antigens, anti-A and anti-B, A and B glycosyltransferases, and ABO genes

Review: ABO blood group system—ABH oligosaccharide antigens, anti-A and anti-B, A and B glycosyltransferases, and ABO genes

Trichostatin A-Assisted Epigenomic Modulation Affects the Expression Profiles of Not Only Recombinant Human α1,2-Fucosyltransferase and α-Galactosidase A Enzymes But Also Galα1→3Gal Epitopes in Porcine Bi-Transgenic Adult Cutaneous Fibroblast Cells

The FORS awakens: review of a blood group system reborn

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