Mouse ? 1,3-galactosyltransferase (GA1/GM1/GD1b synthase): Protein characterization, tissue expression, and developmental regulation in neural retina

Daniotti, José L.; Martina, José A.; Zurita, Adolfo R.; Maccioni, Hugo J. F.

doi:10.1002/(sici)1097-4547(19991015)58:2<318::aid-jnr12>3.0.co;2-u

Cited by 19 publications

(8 citation statements)

References 45 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…10 These antigens in our array set were listed in Table 2 along with reported biological relevance. 6,8,10,11,[29][30][31][32][33][34][35][36][37][38][39] We excluded Tn antigens from this analysis because we already observed high signals for these antigens in Figure 1 and GT2, also showed higher signals with broad distribution than Sd a antigen. The P1 antigen and blood group H type 2 antigens were 13.2 (1.0) and 10.9 (0.7) to 12.7 (1.3) in IgM, respectively, but the signal intensity toward high-mannose carbohydrates were negative.…”

Section: Antibody Signals Toward Non-α-gal Pig Antigens and Its Anamentioning

confidence: 99%

Profiling natural serum antibodies of non‐human primates with a carbohydrate antigen microarray

Nanno

Sterner

Gildersleeve

et al. 2019

Xenotransplantation

View full text Add to dashboard Cite

Background: Engineering of α-Galactosyltransferase gene-knockout pigs circumvented hyperacute rejection of pig organs after xenotransplantation in non-human primates. Overcoming this hurdle revealed the importance of non-α-Gal carbohydrate antigens in the immunobiology of acute humoral xenograft rejection. Methods: This study analyzed serum from seven naïve cynomolgus monkeys (blood type O/B/AB = 3/2/2) for the intensity of natural IgM and IgG signals using carbohydrate antigen microarray, which included historically reported α-Gal and non-α-Gal carbohydrate antigens with various modifications.Results: The median (range) of IgM and IgG signals were 12.71 (7.23-16.38) and 9.05 (7.23-15.90), respectively. The highest IgM and IgG signals with narrowest distribution were from mono-and disaccharides, followed by modified structures. Natural anti-α-Gal antibody signals were medium to high in IgM (11.2-15.9) and medium in IgG (8.5-11.6) spectra, and was highest with Lac core structure (Galα1-3Galβ1-4Glc, iGb3) and lowest with LacNAc core structure (Galα1-3Galβ1-4GlcNAc). Similar signal intensities (up to 15.8 in IgM and up to 11.8 in IgG) were observed for historically detected natural non-α-Gal antigens, which included Tn antigen, T antigen, GM2 glycolipid, and Sd a antigen. The hierarchical clustering analysis revealed the presence of clusters of anti-A antibodies and was capable of distinguishing between the blood group B and AB non-human primates. Conclusions:The results presented here provide the most comprehensive evaluation of natural antibodies present in cynomolgus monkeys. K E Y W O R D S carbohydrate antigen microarray, natural serum antibodies, non-human primates, xenotransplantation GM3(Gc)−Sp − 05 CT/Sda−Sp − 05

show abstract

Section: Antibody Signals Toward Non-α-gal Pig Antigens and Its Anamentioning

confidence: 99%

Profiling natural serum antibodies of non‐human primates with a carbohydrate antigen microarray

Nanno

Sterner

Gildersleeve

et al. 2019

Xenotransplantation

View full text Add to dashboard Cite

show abstract

“…The cDNA for Gal T-II has been cloned from rat [42], human [43], and mouse brains [44]. The Gal T-II gene has no significant homology with other galactosyltransferase genes and consists of a single exon, which is different from other GT genes.…”

Section: Galactosyltransferases (Ec 241x)mentioning

confidence: 99%

Cloning and Transcriptional Regulation of Genes Responsible for Synthesis of Gangliosides

Zeng¹,

2008

CDT

View full text Add to dashboard Cite

Ganglioside synthases are glycosyltransferases involved in the biosynthesis of glycoconjugates. A number of ganglioside synthase genes have been cloned and characterized. They are classified into different families of glycosyltransferases based on similarities of their amino acid sequences. Tissue-specific expression of these genes has been analyzed by hybridization using cDNA fragments. Enzymatic characterization with the expressed recombinant enzymes showed these enzymes differ in their donor and acceptor substrate specificities and other biochemical parameters. In vitro enzymatic analysis also showed that one linkage can be synthesized by multiple enzymes and one enzyme may be responsible for synthesis of multiple gangliosides. Following the cloning of the ganglioside synthase genes, the promoters of the key synthase genes in the ganglioside biosynthetic pathway have been cloned and analyzed. All of the promoters are TATA-less, lacking a CCAAT box but containing GC-rich boxes, characteristic of the housekeeping genes, although transcription of ganglioside synthase genes is subject to complex developmental and tissue-specific regulation. A set of cis-acting elements and transcription factors, including Sp1, AP2, and CREB, function in the proximal promoters. Negative-regulatory regions have also been defined in most of the promoters. We present here an overview of these genes and their transcriptional regulation. Keywords glycosyltransferase; ganglioside; ganglioside synthase; gene cloning; transcription regulation; transcription factors Cloning of the Ganglioside Synthase (Glycosyltransferase) GenesGanglioside synthases are glycosyltransferases (GTs) that transfer sugar residues from an activated donor substrate, usually a nucleotide-sugar, to a specific acceptor, which may be a lipid, protein, or growing oligosaccharide. GTs are typically grouped into families based on the type of sugar they transfer (i.e., galactosyltransferases, sialyltransferases, and like). Many GT genes have been identified by molecular cloning or homology search of the available genomic databases and have been classified into families by amino-acid-sequence similarities [1,2] (available at http://afmb.crns-mrs.fr/CAZY and http:// glycob.oupjournals.org). Despite the fact that many GTs recognize identical donor or acceptor substrates, surprisingly limited sequence homology exists among different families [2]. However, common structural features are found among mammalian transferases: they are almost all classified as type II integral membrane proteins, with a short amino-terminal cytoplasmic tail, a membrane-anchoring domain, a short proteolytically sensitive stem region, and a large catalytic domain that includes the carboxyl terminus [3]. In addition, analysis of crystal structures of GTs shows that structural folds appear to be more conserved than sequence similarities since only a few topologies exists for most of the GT families NIH Public Access although there is a large variability in the acceptor-binding domain [4]. The c...

show abstract

“…Mouse Gal-T2 is coded by one gene contained into a single exon located in chromosome 17 [6], 500 bp downstream the polyadenylation signal of the S18 ribosomal protein gene (RPS18 gene). The locus contains a number of genes conserved and synthenic in human, rat and mouse genome.…”

Section: Introductionmentioning

confidence: 99%

“…The locus contains a number of genes conserved and synthenic in human, rat and mouse genome. Gal-T2 activity and mRNA levels are developmentally regulated in the rat CNS [6,7]. Gal-T2 mRNA is also highly expressed in adult extraneural tissues, particularly testis, which also showed elevated Gal-T2 activity [6].…”

Section: Introductionmentioning

confidence: 99%

“…Gal-T2 activity and mRNA levels are developmentally regulated in the rat CNS [6,7]. Gal-T2 mRNA is also highly expressed in adult extraneural tissues, particularly testis, which also showed elevated Gal-T2 activity [6]. Altogether, these results strongly suggest that Gal-T2 is under transcriptional control both in neural and extraneural tissues.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

ETS‐1 transcription factor activates the expression of mouse UDP‐Gal:GA2/GM2/GD2/GT2 galactosyltransferase gene

2004

Self Cite

View full text Add to dashboard Cite

UDP-Gal:GA2/GM2/GD2/GT2 galactosyltransferase (Gal-T2) transfers galactose to the terminal N-acetylgalactosamine of either the neutral glycolipid GA2 or of the gangliosides GM2, GD2 and GT2. Previous studies revealed a tight regulation of Gal-T2 activity and mRNA expression during development of the rat CNS. Here, we study in PC12 cells the cis-acting elements involved in the activation of a fragment of 211 bp around the transcription initiation site of the mouse Gal-T2 promoter. Mutagenesis, competition experiments and functional assays showed that the Ets-1 transcription factor is involved in the activation of the Gal-T2 promoter.

show abstract

Mouse ? 1,3-galactosyltransferase (GA1/GM1/GD1b synthase): Protein characterization, tissue expression, and developmental regulation in neural retina

Cited by 19 publications

References 45 publications

Profiling natural serum antibodies of non‐human primates with a carbohydrate antigen microarray

Profiling natural serum antibodies of non‐human primates with a carbohydrate antigen microarray

Cloning and Transcriptional Regulation of Genes Responsible for Synthesis of Gangliosides

ETS‐1 transcription factor activates the expression of mouse UDP‐Gal:GA2/GM2/GD2/GT2 galactosyltransferase gene

Contact Info

Product

Resources

About