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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 08 Dec 2016.

ST3 beta-galactoside alpha-2,3-sialyltransferase 5

GM3 synthase, ST3Gal5, ganglioside GM3 synthase
Ganglioside GM3 is known to participate in the induction of cell differentiation, modulation of cell proliferation, maintenance of fibroblast morphology, signal transduction, and integrin-mediated cell adhesion. The protein encoded by this gene is a type II membrane protein which catalyzes the formation of GM3 using lactosylceramide as the substrate. The encoded protein is a member of glycosyltransferase family 29 and may be localized to the Golgi apparatus. Mutation in this gene has been associated with Amish infantile epilepsy syndrome. Transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, sialyltransferase, HAD, CAN, glycosyltransferase
Papers on GM3 synthase
Early growth and development impairment in patients with ganglioside GM3 synthase deficiency.
New
Xin et al., Cleveland, United States. In Clin Genet, Jan 2016
UNASSIGNED: Ganglioside GM3 synthase is a key enzyme involved in the biosynthesis of gangliosides.
Serum Deprivation-Induced Human GM3 Synthase (hST3Gal V) Gene Expression Is Mediated by Runx2 in Human Osteoblastic MG-63 Cells.
New
Lee et al., Pusan, South Korea. In Int J Mol Sci, Dec 2015
In parallel, gene expression of human GM3 synthase (hST3Gal V) catalyzing ganglioside GM3 biosynthesis was upregulated by SD in MG-63 cells.
Loss of ancestral N-glycosylation sites in conserved proteins during human evolution.
New
Hahn et al., Seoul, South Korea. In Int J Mol Med, Dec 2015
The results showed that each of the human proteins, CELSR1, ST3GAL5 and VSIG10, lost an ancestrally conserved N-glycosylation site following human-chimpanzee divergence.
The regulation of ER export and Golgi retention of ST3Gal5 (GM3/GM4 synthase) and B4GalNAcT1 (GM2/GD2/GA2 synthase) by arginine/lysine-based motif adjacent to the transmembrane domain.
New
Inokuchi et al., Sendai, Japan. In Glycobiology, Dec 2015
We investigated two glycosyltransferases, ST3Gal5 (ST3G5) and B4GalNAcT1 (B4GN1), involved in ganglioside synthesis and examined their signal sequences for ER export and Golgi retention.
GM3 ganglioside and phosphatidylethanolamine-containing lipids are adipose tissue markers of insulin resistance in obese women.
New
Harrison et al., Australia. In Int J Obes (lond), Nov 2015
RESULTS: In omental adipose tissue of obese, insulin-resistant women, adipocyte hypertrophy and macrophage infiltration were accompanied by an increase in GM3 ganglioside and its synthesis enzyme ST3GAL5; in addition, phosphatidylethanolamine (PE) lipids were increased and their degradation enzyme, phosphatidylethanolamine methyl transferase (PEMT), decreased.
Synthesis and biological evaluation of several dephosphonated analogues of CMP-Neu5Ac as inhibitors of GM3-synthase.
New
Anastasia et al., Milano, Italy. In Chemistry, Nov 2015
Herein, the synthesis of several dephosphonated CMP-Neu5Ac congeners and their anti-GM3-synthase activity is reported.
miRNA proxy approach reveals hidden functions of glycosylation.
New
Mahal et al., New York City, United States. In Proc Natl Acad Sci U S A, Jul 2015
We focus on three enzymes, beta-1,3-glucosyltransferase (B3GLCT), beta-galactoside alpha-2,3-sialyltransferase 5 (ST3GAL5), and (alpha-N-acetyl-neuraminyl-2,3-beta-galactosyl-1,3)-N-acetylgalactosaminide alpha-2,6-sialyltransferase 5 (ST6GALNAC5), encoding glycans that are difficult to analyze by traditional methods.
siRNA-based spherical nucleic acids reverse impaired wound healing in diabetic mice by ganglioside GM3 synthase knockdown.
New
Paller et al., Chicago, United States. In Proc Natl Acad Sci U S A, Jun 2015
Spherical nucleic acid (SNA) gold nanoparticle conjugates (13-nm-diameter gold cores functionalized with densely packed and highly oriented nucleic acids) dispersed in Aquaphor have been shown to penetrate the epidermal barrier of both intact mouse and human skin, enter keratinocytes, and efficiently down-regulate gene targets.
Microarray analysis of differentially expressed genes regulating lipid metabolism during melanoma progression.
New
Sudhakar et al., In Indian J Biochem Biophys, Apr 2015
Genes for synthesis of pro-tumorigenic GM3 and GD3 gangliosides (UGCG, HEXA, ST3GAL5 and ST8SIA1) were also upregulated in melanoma.
GM3 and cancer.
Review
New
Handa et al., Seattle, United States. In Glycoconj J, Feb 2015
Levels of mRNA for GM3 synthase were reduced in avian and mammalian cells transformed by oncoprotein "v-Jun", and overexpression of GM3 synthase in the transformed cells caused reversion from transformed to normal cell-like phenotype.
Heterogeneity of gangliosides among T cell subsets.
Review
Suzuki et al., Sendai, Japan. In Cell Mol Life Sci, 2013
Ganglioside GM3 synthase-deficient mice lacking a-series gangliosides neither exhibited the TCR-dependent activation of CD4(+) T nor developed ovalbumin-induced allergic airway inflammation.
[The regulation of ganglioside GM3 synthesis].
Review
Uemura, Sendai, Japan. In Yakugaku Zasshi, 2011
Nevertheless, we have succeeded in detecting endogenous mouse GM3 synthase (GM3S), the primary glycosyltransferase responsible for the biosynthesis of ganglio-series gangliosides.
Regulation of human EGF receptor by lipids.
GeneRIF
Simons et al., Dresden, Germany. In Proc Natl Acad Sci U S A, 2011
GM3 exhibits the potential to regulate the allosteric structural transition from inactive to a signaling EGFR dimer, by preventing the autophosphorylation of the intracellular kinase domain in response to ligand binding
Transcriptional activation of human GM3 synthase (hST3Gal V) gene by valproic acid in ARPE-19 human retinal pigment epithelial cells.
GeneRIF
Lee et al., Pusan, South Korea. In Bmb Rep, 2011
Data demonstrate that valproic acid (VPA) transcriptionally regulates human GM3 synthase (hST3Gal V), which catalyzes ganglioside GM3 biosynthesis in ARPE-19 human retinal pigment epithelial cells.
Physiopathological function of hematoside (GM3 ganglioside).
Review
Inokuchi, Japan. In Proc Jpn Acad Ser B Phys Biol Sci, 2010
Since I was involved in the molecular cloning of GM3 synthase (SAT-I), which is the primary enzyme for the biosynthesis of gangliosides in 1998, my research group has been concentrating on our efforts to explore the physiological and pathological implications of gangliosides especially for GM3.
Two active and differently N-glycosylated isoforms of human ST3Gal-V are produced from the placental mRNA variant by a leaky scanning mechanism.
GeneRIF
Colombo et al., Milano, Italy. In Febs Lett, 2010
In vivo expression of the transcript gives rise to two human ST3Gal-V isoforms with distinct characteristics.
Elevated mRNA level of hST6Gal I and hST3Gal V positively correlates with the high risk of pediatric acute leukemia.
GeneRIF
Mandal et al., Calcutta, India. In Leuk Res, 2010
ST6Gal I and ST3Gal V were positively correlated with the high risk of pediatric acute leukemia.
GM3 synthase overexpression results in reduced cell motility and in caveolin-1 upregulation in human ovarian carcinoma cells.
GeneRIF
Sonnino et al., Milano, Italy. In Glycobiology, 2010
GM3 synthase overexpression results in reduced cell motility and in caveolin-1 upregulation in human ovarian carcinoma cells
Insulin resistance as a membrane microdomain disorder.
Review
Inokuchi, Sendai, Japan. In Yakugaku Zasshi, 2007
We were able to extend these in vitro observations to living animals using obese Zucker fa/fa rats and ob/ob mice, in which the GM3 synthase mRNA levels in the white adipose tissues are significantly higher than in their lean controls.
Infantile-onset symptomatic epilepsy syndrome caused by a homozygous loss-of-function mutation of GM3 synthase.
Impact
GeneRIF
Crosby et al., London, United Kingdom. In Nat Genet, 2004
). We sequenced genes in the region and identified a nonsense mutation in SIAT9, which is predicted to result in the premature termination of the GM3 synthase enzyme (also called lactosylceramide alpha-2,3 sialyltransferase).
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