Disease relevance of ST3GAL3

• Clinical relevance of sialyltransferases ST6GAL-I and ST3GAL-III in gastric cancer [1].
• In conclusion, high ST3Gal III and ST6Gal I expressions in human breast tumors are associated with poor prognosis markers [2].
• CONCLUSIONS: ST3Gal III gene is less expressed in pterygium than in normal conjunctiva [3].
• RESULTS: Among these five STs, the mRNA expressions of three STs, including ST3Gal III, ST3Gal IV, and ST3Gal VI, were significantly decreased in patients with ovarian cancers, compared to the normal controls (P<0.001) [4].
• RESULTS: Both ST6Gal I mRNA and ST3Gal III mRNA expressions were significantly increased in patients with lymph node metastases compared to those without lymph node metastases (P = 0.002 and P = 0.001, respectively, Mann-Whitney U test) [5].

High impact information on ST3GAL3

• And Galbeta1,3(4)GlcNAc alpha2,3-sialyltransferase (ST3Gal III) transfectants were made to increase further the expression of cell-surface, N-glycan, alpha2,3-linked sialic acids [6].
• Although ST3Gal III transfection resulted in increased invasivity when compared with parental U-373 MG and vector-transfected control cells in vitro, ST6Gal I transfection abolished invasion in vitro and induced alterations in both cell morphology, cell-spreading, and adhesion-mediated protein tyrosine phosphorylation [6].
• In contrast to ST3Gal III and ST3Gal IV, this enzyme exhibited restricted substrate specificity, i.e. it utilized Galbeta1,4GlcNAc on glycoproteins, and neolactotetraosylceramide and neolactohexaosylceramide, but not lactotetraosylceramide, lactosylceramide, or asialo-GM1 [7].
• All thymocytes bound M. amurensis agglutinin, demonstrating a direct correlation between the level of ST3N mRNA expression and cell-surface glycosylation [8].
• By in situ hybridization, mRNA encoding ST3N was detected uniformly throughout the thymus [8].

Biological context of ST3GAL3

• The coding sequences of the ST3Gal III gene stretch over a gene sequence of approximately 223 Kb comprised of 15 exons [9].
• Three isotranscripts, ST3Gal III C5, C12 and D5, were similar in the 3'-end coding for an identical amino acid sequence unrelated to the original enzyme [10].
• IL-1beta-induced sLeX expression on HuH-7 cells was suppressed by transfection of gene-specific small interference RNAs against FUT VI and ST3Gal IV but not against FUT IV and ST3Gal III [11].
• Using receiver operating characteristic curves of ST ratio index for accuracy comparison of lymph node metastases, ST3Gal III and ST6Gal I were observed to be fairly interchangeable (area under the curve (AUC) of 3Gal I = 0.810; AUC of 6Gal I = 0.786, significance of difference between AUC = 0.810) [5].

Anatomical context of ST3GAL3

• Significant correlations were found between the presence of signet ring cells and enhanced ST6GAL-I activity in the tumor tissue (p = 0.047) or in the mucosa (p = 0.024), and between signet ring cells and ST3GAL-III activity in the mucosa (p < 0.001) [1].
• Immunocytochemical localization of alpha2,3(N)-sialyltransferase (ST3Gal III) in cell lines and rat kidney tissue sections: evidence for golgi and post-golgi localization [12].
• However, an antibody fraction crossreactive with beta-galactosidase recognized natively expressed ST3Gal III which was found to be colocalized with beta1, 4-galactosyltransferase in the Golgi apparatus of several cultured cell lines [12].
• We have recently cloned and sequenced 19 human ST3Gal III gene isotranscripts from peripheral blood leukocytes and identified very complex patterns of isotranscripts of this gene in neuronal tissues [10].
• These ST3Gal III and ST3Gal IV clonal variants demonstrated increased adherence to IL-1beta-activated human umbilical vein endothelial cells (HUVEC) (up to 90% adherent cells compared with 63% for wild type cells) [13].

Associations of ST3GAL3 with chemical compounds

• Two of the C series isotranscripts, ST3Gal III C4 and C11 had both lost exons 12 and 13 containing the S-motif but had otherwise the L- and the VS-motifs intact [10].
• One of the STs, which exhibited the highest homology to ST3 Gal III, showed activity toward lactosylceramide (LacCer) and was termed ST3 Gal V according to the suggested nomenclature [1] [14].
• This phenomenon is reproducible by stable expression of ST6Gal I in parental CHO cells, but not upon transfection of the competing lactosamine-specific alpha2-3-sialyltransferase (Galbeta1-(3)4GlcNAc:alpha2-3-sialyltransferase; (ST6Gal III) formerly ST3N) into either cell type [15].

Other interactions of ST3GAL3

• We demonstrate that control and activated MSCs express ST3GAL3, a sialyltransferase necessary to produce the embryonic antigens SSEA-3 and -4 [16].
• GLUT1 was co-amplified with ST3N and Fuc-TVII genes, which are involved in the synthesis of sLe(x) (p < 0.01) [17].
• The mRNA steady-state level of sialyl- (ST3Gal III) and of fucosyl- (FUT3) transferases was moderately up-regulated by TNFalpha; a 52% increase of alpha2,3-sialyltransferase activity was also observed in TNFalpha-stimulated MM-39 cells [18].
• cDNAs, encoding human beta1,4-galactosyltransferase (hGalT I, EC 2.4.1.22), human Galbeta1,3(4)-GlcNAc alpha2,3-sialyltransferase (hST3GalIII, EC 2.4.99), and human Galbeta1,4-GlcNAc alpha2,6-sialyltransferase (hST6Gal I, EC 2.4.99.1), were cloned from human cell lines [19].

Analytical, diagnostic and therapeutic context of ST3GAL3

• These antibodies were used to localize ST3Gal III by immunofluorescence in various cell lines and rat kidney tissue sections [12].
• ST3Gal III sialyltransferase expression was also studied in 10 healthy conjunctiva and 10 pterygia by reverse transcriptase-polymerase chain reaction (RT-PCR) [3].

References