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UDP-Gal:betaGlcNAc beta 1,4- galactosyltransferase, polypeptide 1

GalT, N-Acetyllactosamine Synthase, beta 1,4-galactosyltransferase
The protein encoded by this gene is a beta-1,3-glucosyltransferase that transfers glucose to O-linked fucosylglycans on thrombospondin type-1 repeats (TSRs) of several proteins. The encoded protein is a type II membrane protein. Defects in this gene are a cause of Peters-plus syndrome (PPS).[provided by RefSeq, Mar 2009] (from NCBI)
Top mentioned proteins: CAN, ACID, HAD, Alpha-1, CD45
Papers using GalT antibodies
The secretory membrane system in the Drosophila syncytial blastoderm embryo exists as functionally compartmentalized units around individual nuclei
Lippincott-Schwartz Jennifer et al., In The Journal of Cell Biology, 1997
... pUASp:Lys-GFP-KDEL and pUASp:GalT-GFP transgenic lines have been previously ...
Papers on GalT
Regulatory function of β1,4-galactosyltransferase I expression on Lewis-Y glycan and embryo implantation.
Kong et al., Dalian, China. In Gene, 15 Jun 2015
β1,4-Galactosyltransferase I (β1,4-GalT-I), a key enzyme in glycobiology, mediates several biological mechanisms.
Comparative N-linked glycan analysis of wild-type and α1,3-galactosyltransferase gene knock-out pig fibroblasts using mass spectrometry approaches.
Kim et al., Seoul, South Korea. In Mol Cells, 03 Mar 2015
Even after α1,3-galactosyltransferase gene knock-out (GalT-KO) pigs are generated, potential non-Gal antigens are still existed.
Bortezomib, C1-inhibitor and plasma exchange do not prolong the survival of multi-transgenic GalT-KO pig kidney xenografts in baboons.
Blancho et al., Nantes, France. In Am J Transplant, 28 Feb 2015
Galactosyl-transferase KO (GalT-KO) pigs represent a potential solution to xenograft rejection, particularly in the context of additional genetic modifications.
Transgenic expression of human CD47 markedly increases engraftment in a murine model of pig-to-human hematopoietic cell transplantation.
Hawley et al., Boston, United States. In Am J Transplant, Dec 2014
We report here the generation of hCD47 transgenic GalT-KO miniature swine that express hCD47 in all blood cell lineages.
Xylose phosphorylation functions as a molecular switch to regulate proteoglycan biosynthesis.
Dixon et al., San Diego, United States. In Proc Natl Acad Sci U S A, Dec 2014
We also show that the activity of galactosyl transferase II (GalT-II, B3GalT6), a key enzyme in the biosynthesis of the tetrasaccharide linkage region, is dramatically increased by Fam20B-dependent xylose phosphorylation.
The sweets standing at the borderline between allo- and xenotransplantation.
Kim et al., Seoul, South Korea. In Xenotransplantation, 2013
Although researchers have been able to develop α1,3-galactosyltransferase (GalT) gene knockout (KO) pigs, there remain unclarified non-Gal antigens that prevent xenotransplantation.
Two Tunisian patients with Peters plus syndrome harbouring a novel splice site mutation in the B3GALTL gene that modulates the mRNA secondary structure.
Fakhfakh et al., Sfax, Tunisia. In Gene, 2012
A novel homozygous c.597-2A>G mutation was identified in both patients with Peters plus syndrome harbouring a novel splice site mutation in the B3GALTL gene
Altered oligosaccharide structures reduce colitis induction in mice defective in β-1,4-galactosyltransferase.
Miyoshi et al., Ōsaka, Japan. In Gastroenterology, 2012
revealed increased expression of polylactosamines on B4galt1(+/-) B cells and macrophages, compared with B4galt1(+/+) cells
Carbohydrate antigens.
Fukuzawa et al., Ōsaka, Japan. In Curr Opin Organ Transplant, 2012
RECENT FINDINGS: Studies related to iGb3 and neoantigens after knocking out GalT (GGTA1) were reviewed.
[Regulation of human β-1,4-galactosyltransferase V gene expression in cancer cells].
Furukawa et al., Nagaoka, Japan. In Yakugaku Zasshi, 2011
β-1,4-Galactosyltransferase (β-1,4-GalT) V - whose human and mouse genes were cloned by us - has been suggested to be involved in the biosyntheses of N-glycans, O-glycans, and lactosylceramide by in vitro studies.
Vertebral defects in patients with Peters plus syndrome and mutations in B3GALTL.
Gasparini et al., In Ophthalmic Genet, 2011
Vertebral defects in a patient with Peters plus syndrome and mutations in B3GALTL.
Gal/non-Gal antigens in pig tissues and human non-Gal antibodies in the GalT-KO era.
Breimer, Göteborg, Sweden. In Xenotransplantation, 2011
Our knowledge regarding Gal and non-Gal antigens in GalT-KO pig tissues can be summarized as α3Galactosyl-tranferase gene knock out eliminates the Galα3Galβ4GlcNAc-R antigen expression in pig tissues as well as anti-Gal antibody binding.
Which anti-platelet therapies might be beneficial in xenotransplantation?
Robson et al., Boston, United States. In Xenotransplantation, 2011
The development of α-1,3-galactosyltransferase gene-knockout (GalT-KO) swine with the removal of a dominant xeno-antigen has been an important advance; however, delayed xenograft and acute vascular reaction in GalT-KO animals persist.
A novel nonsense B3GALTL mutation confirms Peters plus syndrome in a patient with multiple malformations and Peters anomaly.
Dollfus et al., Strasbourg, France. In Ophthalmic Genet, 2010
The present report confirms the wide clinical spectrum of Peters plus syndrome, underlines the major clinical criteria of the syndrome and the major implication of B3GALTL gene in this condition.
Novel B3GALTL mutation in Peters-plus Syndrome.
Chassaing et al., In Clin Genet, 2009
Novel B3GALTL mutation in Peters-plus Syndrome
Heart transplantation in baboons using alpha1,3-galactosyltransferase gene-knockout pigs as donors: initial experience.
Cooper et al., Boston, United States. In Nat Med, 2005
Hearts from alpha1,3-galactosyltransferase knockout pigs (GalT-KO, n = 8) were transplanted heterotopically into baboons using an anti-CD154 monoclonal antibody-based regimen.
Marked prolongation of porcine renal xenograft survival in baboons through the use of alpha1,3-galactosyltransferase gene-knockout donors and the cotransplantation of vascularized thymic tissue.
Sachs et al., Boston, United States. In Nat Med, 2005
Here we report our initial results using alpha-1,3-galactosyltransferase knockout (GalT-KO) donors and a tolerance induction approach.
Large-scale production of UDP-galactose and globotriose by coupling metabolically engineered bacteria.
Ozaki et al., Machida, Japan. In Nat Biotechnol, 1998
Recombinant E. coli that overexpress the UDP-Gal biosynthetic genes galT, galK, and galU were generated.
Translational coupling at an intercistronic boundary of the Escherichia coli galactose operon.
Rosenberg et al., In Cell, 1982
These results demonstrate that the galK gene is translationally coupled to the gene immediately preceding galK in the gal operon (that is, galT), and that the coupling effect depends primarily on the position at which upstream translation terminates relative to the galK start site.
IS1 insertion generates duplication of a nine base pair sequence at its target site.
Grindley, In Cell, 1978
DNA sequences of portions of the wild-type galT gene which act as the target sites for these insertions, as well as the corresponding gal/IS1 junctions, are reported.
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