Molecular Cloning and Expression of Human ST6GalNAc III: Restricted Tissue Distribution and Substrate Specificity

Tsuchida, Akiko; Ogiso, Manabu; Nakamura, Yoko; Kiso, Makoto; Furukawa, Koichi

doi:10.1093/jb/mvi124

Cited by 30 publications

(16 citation statements)

References 14 publications

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“…Some of the data were essentially the same as reported in [21] and [23], but they were confirmed in this study using the identical conditions. Both enzymes showed activity toward fetuin, MSGG and sialyl Lc4 as well as GM1b.…”

Section: Hst6galnac III and Vi Synthesize Dsggsupporting

confidence: 86%

“…Isolation of cDNA clones was performed as described previously [23]. Briefly, RT (reverse transcription)-PCR using a human brain cDNA library as template was performed with the sense primer 5 -GAATGTGGGCTGGAGAGGTC-3 and the antisense primer 5 -GCAGAGTCACCATCCACATC-3 using TITANIUM TM Taq DNA Polymerase (Clontech) as follows; 95…”

Section: Isolation Of Human St6galnac IIImentioning

confidence: 99%

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Identification and expression of a sialyltransferase responsible for the synthesis of disialylgalactosylgloboside in normal and malignant kidney cells: downregulation of ST6GalNAc VI in renal cancers

Senda

Itoh

Tsuchida

et al. 2007

Biochemical Journal

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Although disialyl glycosphingolipids such as GD3 and GD2 have been considered to be associated with malignant tumours, whether branched-type disialyl glycosphingolipids show such an association is not well understood. We investigated the sialyltransferases responsible for the biosynthesis of DSGG (disialylgalactosylgloboside) from MSGG (monosialylgalactosylgloboside). Among six GalNAc:α2,6-sialyltransferases cloned to date, we focused on ST6GalNAc III, V and VI, which utilize sialylglycolipids as substrates. In vitro enzyme analyses revealed that ST6GalNAc III and VI generated DSGG from MSGG with V max /K m values of 1.91 and 4.16 respectively. Transfection of the cDNA expression vectors for these enzymes resulted in DSGG expression in a renal cancer cell line. Although both ST6GalNAc III and VI genes were expressed in normal kidney cells, the expression profiles of ST6GalNAc VI among 20 renal cancer cell lines correlated clearly with those of DSGG, suggesting that the sialyltransferase involved in the synthesis of DSGG in the kidney is ST6GalNAc-VI. ST6GalNAc-VI and DSGG were found in proximal tubule epithelial cells in normal kidney tissues, while they were downregulated in renal cancer cell lines and cancer tissues. All these findings indicated that DSGG was suppressed during the malignant transformation of the proximal tubules as a maturation arrest of glycosylation.

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Section: Hst6galnac III and Vi Synthesize Dsggsupporting

confidence: 86%

Section: Isolation Of Human St6galnac IIImentioning

confidence: 99%

Identification and expression of a sialyltransferase responsible for the synthesis of disialylgalactosylgloboside in normal and malignant kidney cells: downregulation of ST6GalNAc VI in renal cancers

Senda

Itoh

Tsuchida

et al. 2007

Biochemical Journal

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“…The sialyltransferase encoded by ST6GALNAC3 is expressed in human spleen, kidney, lung, and brain and catalyzes the synthesis of branched-type disialyl structures by transfer of a sialic acid onto a GalNAc residue (35,36). Others have shown that GC isoforms differ with respect to the degree of glycosylation (4,37).…”

Section: Discussionmentioning

confidence: 99%

Genome-wide association study of circulating vitamin D–binding protein

Moy¹,

Mondul²,

Zhang³

et al. 2014

The American Journal of Clinical Nutrition

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In this GWAS analysis, to our knowledge the first to examine this biochemical phenotype, 2 variants in GC--one exonic and one intronic--were associated with serum DBP concentrations at the genome-wide level of significance. Understanding the genetic contributions to circulating DBP may provide greater insights into the vitamin D binding, transport, and other functions of DBP and the effect of vitamin D status on health outcomes.

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“…While ST6GalNAc1 prefers Tn antigen as an acceptor, ST6GalNAc2 favors T antigen and sialyl-T antigen (Table 1). ST6GalNAc3 and ST6GalNAc4 both synthesize disialyl-T antigen from sialyl-T antigen and disialyl-lactotetraosyl-ceramide - G D1α from sialyl-lactotetraosyl-ceramide - G M1b (Table 1) (35, 36). Both ST6GalNAc5 and ST6GalNAc6 show restricted specificity towards G M1b to synthesize G D1α (Table 1) (37, 38).…”

Section: B α26 Siaylation Of O-glycans and Its Impact On Cancer Promentioning

confidence: 99%

Galectin-Binding O-Glycosylations as Regulators of Malignancy

Dimitroff

2015

Cancer Research

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Cancer cells commonly display aberrant surface glycans and related glycoconjugate scaffolds. Compared with their normal counterparts, cancer cell glycans are variably produced and often structurally distinct, serving as biomarkers of cancer progression or as functional entities to malignancy. The glycan signature of a cancer cell is created by the collaborative activities of glycosyltransferases, glycosidases, nucleotide-sugar transporters, sulfotransferases and glycan-bearing protein/lipid scaffolds. In a coordinated fashion, these factors regulate the synthesis of cancer cell glycans and thus are considered correlates of cancer cell behavior. Functionally, cancer cell glycans can serve as binding targets for endogenous lectin effectors, such as C-type selectins and S-type galectins. There has been a recent surge of important observations on the role of glycosytransferases, specifically α2,6 sialyltransferases, in regulating the length and lectin-binding features of serine/threonine (O)-glycans found on cancer cells. The capping activity of O-glycan-specific α2,6 sialyltransferases, in particular, has been found to regulate cancer growth and metastasis in a galectin-dependent manner. These findings highlight the functional importance of cancer cell O-glycans and related galectin-binding features in the virulent activity of cancer and raise the prospect of targeting cancer cell glycans as effective anti-cancer therapeutics.

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Molecular Cloning and Expression of Human ST6GalNAc III: Restricted Tissue Distribution and Substrate Specificity

Cited by 30 publications

References 14 publications

Identification and expression of a sialyltransferase responsible for the synthesis of disialylgalactosylgloboside in normal and malignant kidney cells: downregulation of ST6GalNAc VI in renal cancers

Identification and expression of a sialyltransferase responsible for the synthesis of disialylgalactosylgloboside in normal and malignant kidney cells: downregulation of ST6GalNAc VI in renal cancers

Genome-wide association study of circulating vitamin D–binding protein

Galectin-Binding O-Glycosylations as Regulators of Malignancy

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