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Information on EC 2.8.2.29 - [heparan sulfate]-glucosamine 3-sulfotransferase 2
for references in articles please use BRENDA:EC2.8.2.29
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EC Tree 2 Transferases
2.8 Transferring sulfur-containing groups
2.8.2 Sulfotransferases
2.8.2.29 [heparan sulfate]-glucosamine 3-sulfotransferase 2
IUBMB Comments
This enzyme sulfates the residues marked with an asterisk in sequences containing at least → IdoA2S→ GlcN*→ or → GlcA2S→ GlcN*→ (symbols as in 2-Carb-38). Preference for GlcN2S vs. unmodified GlcN has not yet been established. Additional structural features are presumably required for substrate recognition, since the 3-O-sulfated residue is of low abundance, whereas the above IdoA-containing sequence is quite abundant. This enzyme differs from the other [heparan sulfate]-glucosamine 3-sulfotransferases by modifying selected glucosamine residues preceded by GlcA2S; EC 2.8.2.23 ([heparan sulfate]-glucosamine 3-sulfotransferase 1) prefers GlcA or IdoA, whereas EC 2.8.2.30 ([heparan sulfate]-glucosamine 3-sulfotransferase 3) prefers IdoA2S.
The enzyme appears in viruses and cellular organisms
Synonyms
hs3st2, 3-ost-2, 3-o-sulfotransferase-2, 3-ost2, heparan sulfate 3-o-sulfotransferase 2, heparan sulfate (glucosamine) 3-o-sulfotransferase 2, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
3-OST-2
glucosaminyl 3-O-sulfotransferase 3a,3b
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heparan sulfate 3-O-sulfotransferase
heparan sulfate 3-O-sulfotransferase 2
heparan sulfate D-glucosaminy 3-O-sulfotransferase
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HS3ST2
additional information
3-OST-2
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HS3ST2
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additional information
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the enzyme belongs to the 3-OST gene family with two distinct 3-OST family subgroups
additional information
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the enzyme belongs to the family of 3-O-sulfotransferases
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine = adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
This enzyme sulfates the residues marked with an asterisk in sequences containing at least IdoA2S-GlcN*- or ?GlcA2S.GlcN*-. Preference for GlcN2S vs. unmodified GlcN has not yet been established. Additional structural features are presumably required for substrate recognition, since the 3-O-sulfated residue is of low abundance, whereas the above IdoA-containing sequence is quite abundant. This enzyme differs from the other, [heparan sulfate]-glucosamine 3-sulfotransferases by modifying selected glucosamines residues preceded by GlcA2S. EC 2.8.2.23, [heparan sulfate]-glucosamine 3-sulfotransferase 1, prefers GlcA or IdoA, whereas EC 2.8.2.30, [heparan sulfate]-glucosamine 3-sulfotransferase 3, prefers IdoAS
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
sulfate group transfer
sulfate group transfer
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PATHWAY SOURCE
PATHWAYS
MetaCyc
heparan sulfate biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
3'-phosphoadenylyl-sulfate:[heparan sulfate]-glucosamine 3-sulfotransferase
This enzyme sulfates the residues marked with an asterisk in sequences containing at least -> IdoA2S-> GlcN*-> or -> GlcA2S-> GlcN*-> (symbols as in {iupac/2carb/38::2-Carb-38}). Preference for GlcN2S vs. unmodified GlcN has not yet been established. Additional structural features are presumably required for substrate recognition, since the 3-O-sulfated residue is of low abundance, whereas the above IdoA-containing sequence is quite abundant. This enzyme differs from the other [heparan sulfate]-glucosamine 3-sulfotransferases by modifying selected glucosamine residues preceded by GlcA2S; EC 2.8.2.23 ([heparan sulfate]-glucosamine 3-sulfotransferase 1) prefers GlcA or IdoA, whereas EC 2.8.2.30 ([heparan sulfate]-glucosamine 3-sulfotransferase 3) prefers IdoA2S.
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CAS REGISTRY NUMBER
COMMENTARY
183257-54-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-diphosphate + [heparan sulfate]-glucosamine 3-sulfate
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
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Substrates: -
Products: -
Products: -
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
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Substrates: -
Products: i.e. HSgD+, 3-O-sulfated motifs that bind the gD envelope protein of Herpes simplex virus 1 mediating the viral cellular entry, overview
Products: i.e. HSgD+, 3-O-sulfated motifs that bind the gD envelope protein of Herpes simplex virus 1 mediating the viral cellular entry, overview
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
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Substrates: -
Products: i.e. HSgD+, 3-O-sulfated motifs that bind the gD envelope protein of Herpes simplex virus 1
Products: i.e. HSgD+, 3-O-sulfated motifs that bind the gD envelope protein of Herpes simplex virus 1
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
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Substrates: -
Products: -
Products: -
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
Substrates: -
Products: -
Products: -
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
Substrates: -
Products: -
Products: -
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
Substrates: -
Products: -
Products: -
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
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Substrates: -
Products: -
Products: -
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-diphosphate + [heparan sulfate]-glucosamine 3-sulfate
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Substrates: -
Products: -
Products: -
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-diphosphate + [heparan sulfate]-glucosamine 3-sulfate
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Substrates: does not make active heparan sulfate, transfers sulfate to GlcA2S-GlcNS and IdoA2S-GlcNS
Products: -
Products: -
?
additional information
?
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Substrates: heparan sulfate chains contain sulfated domains termed the HS fine structure, which gives HS specific binding affinities for extracellular ligands, heparan sulfate 3-O-sulfotransferases catalyze the transfer of sulfate groups to the 3-O position of glucosamine residues of heparan sulfate, a rare, but essential heparan sulfate chain modification required for HS fine structure
Products: -
Products: -
?
additional information
?
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Substrates: a gD-type-3-OST isozyme is essential for a conserved neurogenic signaling pathway regulated by Notch
Products: -
Products: -
?
additional information
?
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Substrates: modification of heparan sulfate and the ability of 3-OST-2 to generate receptors for both wild-types and some mutant forms of HSV-1, spreading of receptors mediating cell-to-cell fusion
Products: -
Products: -
?
additional information
?
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Substrates: modification of heparan sulfate and the ability of 3-OST-2 to generate receptors for both wild-types and some mutant forms of HSV-1, spreading of receptors mediating cell-to-cell fusion
Products: -
Products: -
?
additional information
?
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Substrates: HSV-1 glycoprotein gD, both the wild-type and the mutant Rid1 form, can interact with [heparan sulfate]-glucosamine 3-sulfate generated by HS 3-OST-2, overview
Products: -
Products: -
?
additional information
?
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Substrates: HSV-1 glycoprotein gD, both the wild-type and the mutant Rid1 form, can interact with [heparan sulfate]-glucosamine 3-sulfate generated by HS 3-OST-2, overview
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-diphosphate + [heparan sulfate]-glucosamine 3-sulfate
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
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Substrates: -
Products: -
Products: -
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
Substrates: -
Products: i.e. HSgD+, 3-O-sulfated motifs that bind the gD envelope protein of Herpes simplex virus 1 mediating the viral cellular entry, overview
Products: i.e. HSgD+, 3-O-sulfated motifs that bind the gD envelope protein of Herpes simplex virus 1 mediating the viral cellular entry, overview
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
Substrates: -
Products: -
Products: -
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
Substrates: -
Products: -
Products: -
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
Substrates: -
Products: -
Products: -
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
Substrates: -
Products: -
Products: -
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-bisphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
Substrates: -
Products: -
Products: -
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-diphosphate + [heparan sulfate]-glucosamine 3-sulfate
-
Substrates: -
Products: -
Products: -
?
3'-phosphoadenylyl sulfate + [heparan sulfate]-glucosamine
adenosine 3',5'-diphosphate + [heparan sulfate]-glucosamine 3-sulfate
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Substrates: does not make active heparan sulfate, transfers sulfate to GlcA2S-GlcNS and IdoA2S-GlcNS
Products: -
Products: -
?
additional information
?
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Substrates: heparan sulfate chains contain sulfated domains termed the HS fine structure, which gives HS specific binding affinities for extracellular ligands, heparan sulfate 3-O-sulfotransferases catalyze the transfer of sulfate groups to the 3-O position of glucosamine residues of heparan sulfate, a rare, but essential heparan sulfate chain modification required for HS fine structure
Products: -
Products: -
?
additional information
?
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Substrates: a gD-type-3-OST isozyme is essential for a conserved neurogenic signaling pathway regulated by Notch
Products: -
Products: -
?
additional information
?
-
Substrates: modification of heparan sulfate and the ability of 3-OST-2 to generate receptors for both wild-types and some mutant forms of HSV-1, spreading of receptors mediating cell-to-cell fusion
Products: -
Products: -
?
additional information
?
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Substrates: modification of heparan sulfate and the ability of 3-OST-2 to generate receptors for both wild-types and some mutant forms of HSV-1, spreading of receptors mediating cell-to-cell fusion
Products: -
Products: -
?
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5-aza-2'-deoxycytidine
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exposure of chondrosarcoma cells to the DNA-methyltransferase inhibitor 5-Aza-dc up-regulates expression of 3-OST2 mRNA
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
CpG Islands Methylation Analysis of CDH11, EphA5, and HS3ST2 Genes in Gastric Adenocarcinoma Patients.
Adenocarcinoma
Down-regulation of Gal 3-O-sulfotransferase-2 (Gal3ST-2) expression in human colonic non-mucinous adenocarcinoma.
Alzheimer Disease
HS3ST2 expression is critical for the abnormal phosphorylation of tau in Alzheimer's disease-related tau pathology.
Breast Neoplasms
Analysis of DNA Methylation of Multiple Genes in Microdissected Cells From Formalin-fixed and Paraffin-embedded Tissues.
Breast Neoplasms
HS3ST2 modulates breast cancer cell invasiveness via MAP kinase- and Tcf4 (Tcf7l2)-dependent regulation of protease and cadherin expression.
Breast Neoplasms
Laboratory validation of formal concept analysis of the methylation status of microarray-detected genes in primary breast cancer.
Breast Neoplasms
Methylation-associated silencing of heparan sulfate D-glucosaminyl 3-O-sulfotransferase-2 (3-OST-2) in human breast, colon, lung and pancreatic cancers.
Breast Neoplasms
Prognostic significance of hedgehog signaling network-related gene expression in breast cancer patients.
Breast Neoplasms
The Heparan Sulfate Sulfotransferases HS2ST1 and HS3ST2 Are Novel Regulators of Breast Cancer Stem-Cell Properties.
Breast Neoplasms
The Pro-Tumoral Activity of Heparan Sulfate 3-O-Sulfotransferase 3B (HS3ST3B) in Breast Cancer MDA-MB-231 Cells Is Dependent on the Expression of Neuropilin-1.
Carcinogenesis
Correction: epigenetic inactivation of heparan sulfate (glucosamine) 3-o-sulfotransferase 2 in lung cancer and its role in tumorigenesis.
Carcinogenesis
Epigenetic inactivation of heparan sulfate (glucosamine) 3-o-sulfotransferase 2 in lung cancer and its role in tumorigenesis.
Carcinoma
Methylation status of KLF4 and HS3ST2 genes as predictors of endometrial cancer and hyperplastic endometrial lesions.
Carcinoma, Ductal
Analysis of DNA Methylation of Multiple Genes in Microdissected Cells From Formalin-fixed and Paraffin-embedded Tissues.
Carcinoma, Non-Small-Cell Lung
Epigenetic inactivation of heparan sulfate (glucosamine) 3-o-sulfotransferase 2 in lung cancer and its role in tumorigenesis.
Chondrosarcoma
Epigenetics: methylation-associated repression of heparan sulfate 3-O-sulfotransferase gene expression contributes to the invasive phenotype of H-EMC-SS chondrosarcoma cells.
Colorectal Neoplasms
HS3ST2 and Its Related Molecules as Potential Biomarkers for Predicting Lymph Node Metastasis in Patients with Colorectal Cancer.
Colorectal Neoplasms
Pipeline for large-scale microdroplet bisulfite PCR-based sequencing allows the tracking of hepitype evolution in tumors.
Dermatitis, Atopic
Possible role of hsa-miR-194-5p, via regulation of HS3ST2, in the pathogenesis of atopic dermatitis in children.
Endometrial Hyperplasia
Methylation status of KLF4 and HS3ST2 genes as predictors of endometrial cancer and hyperplastic endometrial lesions.
Endometrial Neoplasms
Methylation status of KLF4 and HS3ST2 genes as predictors of endometrial cancer and hyperplastic endometrial lesions.
Herpes Simplex
A synthetic heparan sulfate oligosaccharide library reveals the novel enzymatic action of D-glucosaminyl 3-O-sulfotransferase-3a.
Infections
A role for heparan sulfate 3-O-sulfotransferase isoform 2 in herpes simplex virus type 1 entry and spread.
Infections
Methylation in the promoters of HS3ST2 and CCNA1 genes is associated with cervical cancer in Uygur women in Xinjiang.
Lung Neoplasms
Correction: epigenetic inactivation of heparan sulfate (glucosamine) 3-o-sulfotransferase 2 in lung cancer and its role in tumorigenesis.
Lung Neoplasms
Epigenetic inactivation of heparan sulfate (glucosamine) 3-o-sulfotransferase 2 in lung cancer and its role in tumorigenesis.
Lymphatic Metastasis
HS3ST2 and Its Related Molecules as Potential Biomarkers for Predicting Lymph Node Metastasis in Patients with Colorectal Cancer.
Lymphoma
Pipeline for large-scale microdroplet bisulfite PCR-based sequencing allows the tracking of hepitype evolution in tumors.
Neoplasm Metastasis
HS3ST2 and Its Related Molecules as Potential Biomarkers for Predicting Lymph Node Metastasis in Patients with Colorectal Cancer.
Neoplasms
A comprehensive microarray-based DNA methylation study of 367 hematological neoplasms.
Neoplasms
Aberrant gene promoter methylation associated with sporadic multiple colorectal cancer.
Neoplasms
Epigenetic loss of heparan sulfate 3-O-sulfation sensitizes ovarian carcinoma to oncogenic signals and predicts prognosis.
Neoplasms
GLAD-PCR Assay of R(5mC)GY Sites in the Regulatory Region of Tumor-Suppressor Genes Associated with Gastric Cancer.
Neoplasms
Methylation status of KLF4 and HS3ST2 genes as predictors of endometrial cancer and hyperplastic endometrial lesions.
Neoplasms
Methylation-associated silencing of heparan sulfate D-glucosaminyl 3-O-sulfotransferase-2 (3-OST-2) in human breast, colon, lung and pancreatic cancers.
Neoplasms
Novel methylation panel for the early detection of neoplasia in high-risk ulcerative colitis and Crohn's colitis patients.
Neoplasms
Pipeline for large-scale microdroplet bisulfite PCR-based sequencing allows the tracking of hepitype evolution in tumors.
Neoplasms
The heparan sulfate 3-O-sulfotransferases (HS3ST) 2, 3B and 4 enhance proliferation and survival in breast cancer MDA-MB-231 cells.
Ovarian Neoplasms
Epigenetic loss of heparan sulfate 3-O-sulfation sensitizes ovarian carcinoma to oncogenic signals and predicts prognosis.
Pancreatic Neoplasms
Methylation-associated silencing of heparan sulfate D-glucosaminyl 3-O-sulfotransferase-2 (3-OST-2) in human breast, colon, lung and pancreatic cancers.
Stomach Neoplasms
CpG Islands Methylation Analysis of CDH11, EphA5, and HS3ST2 Genes in Gastric Adenocarcinoma Patients.
Stomach Neoplasms
GLAD-PCR Assay of R(5mC)GY Sites in the Regulatory Region of Tumor-Suppressor Genes Associated with Gastric Cancer.
Stomach Neoplasms
High-definition CpG methylation of novel genes in gastric carcinogenesis identified by next-generation sequencing.
Tauopathies
HS3ST2 expression is critical for the abnormal phosphorylation of tau in Alzheimer's disease-related tau pathology.
Urinary Bladder Neoplasms
Promoter hypermethylation of HS3ST2, SEPTIN9 and SLIT2 combined with FGFR3 mutations as a sensitive/specific urinary assay for diagnosis and surveillance in patients with low or high-risk non-muscle-invasive bladder cancer.
Uterine Cervical Neoplasms
Evaluation of candidate methylation markers to detect cervical neoplasia.
Uterine Cervical Neoplasms
Methylation in the promoters of HS3ST2 and CCNA1 genes is associated with cervical cancer in Uygur women in Xinjiang.
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
primary macrophages. HS3ST2 is highly expressed in non-activated macrophages
brenda
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of trigeminal ganglia, gD-type-3-OST-2 is one of the major enzymes, highly located in neuronal cell bodies not in axons, overview
brenda
additional information
additional information
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developmental expression analysis of the 3-OST gene family, mRNA expression patterns in several tissues/organs throughout early zebrafish development, including early cleavage stages, somites, brain, internal body organ primordial, and pectoral fin development, overview
brenda
additional information
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neuronal tissue distribution of 3-O-sulfotransferases, overview
brenda
additional information
isozyme HS3ST2 is not expressed in cell lines representative of the different molecular breast cancer subgroups
brenda
additional information
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isozyme HS3ST2 is not expressed in cell lines representative of the different molecular breast cancer subgroups
brenda
additional information
subcellular distribution of isozymes HS3ST2 and HS3ST3B is analysed by using overexpression systems in HeLa cells
brenda
additional information
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subcellular distribution of isozymes HS3ST2 and HS3ST3B is analysed by using overexpression systems in HeLa cells
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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transmembrane enzyme with a short cytoplasmic tail at the N-terminus
brenda
additional information
additional information
the catalytic domain might support correct addressing of HS3ST2 to cell surface. Partial colocalization of HS3ST2 with syndecan-2 in HeLa cells and primary macrophages. Silencing the expression of this proteoglycan altered the localization of HS3ST2, which suggests that syndecan-2 is required to address the isozyme outside of the Golgi apparatus
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brenda
additional information
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the catalytic domain might support correct addressing of HS3ST2 to cell surface. Partial colocalization of HS3ST2 with syndecan-2 in HeLa cells and primary macrophages. Silencing the expression of this proteoglycan altered the localization of HS3ST2, which suggests that syndecan-2 is required to address the isozyme outside of the Golgi apparatus
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brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
both isozymes, HS3ST3B (EC 2.8.2.30) and HS3ST2, are differently expressed in monocytes and macrophages depending on the inflammatory environment
evolution
HS3STs represent the largest family of HS-modifying enzymes, and yet the reaction of 3-O-sulfation is the rarest maturation step, when compared to other sulfations. Seven HS3STs have been characterized in human, for which the expression is dependent on cell type and tissue environment
malfunction
expression of the genes encoding HS-modifying enzymes is frequently dysregulated in cancer and other diseases. The enzymes show either anti-oncogenic or tumor-promoting effects. The 5' region of the HS3ST2 gene is hypermethylated in tumor tissue but not in surrounding non-cancerous tissue. The expression level of HS3ST2 is markedly reduced in the cancer sample compared with the matched normal counterpart. Reversing methylation restores the expression of the enzyme, confirming the silencing effect of gene methylation. Moreover, HS3ST2 gene hypermethylation is detected in the majority of primary breast cancer samples analysed, and also in human colon, lung and pancreatic cancers. Hypermethylation s found at high frequency in gastric, breast, colorectal, prostate and cervix cancers, as well as in hematological neoplasms. In breast and cervix, hypermethylation of the HS3ST2 gene occurs early during malignant transformation, suggesting a correlation between HS3ST2 silencing and progression of the disease. The exogenous reexpression of HS3ST2 is efficient to inhibit cell migration, invasion and proliferation in various lung cancer cell lines. But the tumor size is not significantly different between patients with HS3ST2 gene hypermethylation and those without, in spite of the anti-proliferative property of HS3ST2 observed in vitro. Re-expression of HS3ST2 in MDA-MB-231 cells leads to an increase in cell viability and invasion, MDA-MB-231 cells carrying HS3ST2 expression display a significant increase in proliferation and survival
malfunction
influence of HS3ST2 overexpression on the CSC phenotype in breast cancer cell lines representative of the triple-negative (MDA-MB-231) and hormone-receptor positive subtype (MCF-7). The CD44+/CD24-/low phenotype is significantly reduced in MDA-MB-231 cells after overexpression of the enzyme, remaining unaltered in MCF-7 cells. Colony and spheroid formation are increased after HS3ST2 overexpression in MCF-7 cells. The phenotypic changes are associated with complex changes in the expression of the stemness-associated notch and Wnt-signaling pathways constituents, syndecans, heparanase and Sulf1. Heparan sulfotransferase subtype-specific impact of HS modifications on the CSC phenotype of triple-negative and hormone receptor positive breast cancer model cell lines. In MDA-MB-231 cells, ALDH1 activity increases from 2.88% in the control transfected cells to 5.36% after overexpression of HS3ST2 overexpressing cells
metabolism
heparan sulfate (HS) 3-O-sulfation can be catalysed by seven 3-sulfotransferases (HS3STs) in humans, but nevertheless it is the rarest modification in heparan sulfate (HS). Isozymes HS3ST2 and HS3ST3B (EC 2.8.2.30) exhibit the same activity in vitro. But they are differently expressed in macrophages depending on cell environment, which suggests that they may be involved in distinct cellular processes
metabolism
high sulfation degree of heparan mediates functional interactions with positively charged amino acids in proteins. 2-O-sulfation of iduronic acid and 3-O-sulfation of glucosamine in heparan sulfate (HS) are mediated by the sulfotransferases HS2ST and HS3ST, respectively, which are dysregulated in several cancers. Both sulfotransferases regulate breast cancer cell viability and invasion. The syndecan family of HSPGs and the Notch pathway are part of the regulatory circuit of HS sulfotransferases. The expression levels of several genes are altered by overexpression of HS3ST2, breast cancer cell transcriptome analysis, overview
metabolism
HS3ST-mediated 3-O-sulfation leads to at least two distinct forms of 3-O-sulfated motifs. HS3ST1 and HS3ST5 participate in the generation of anticoagulant-active HS/heparin sequences for antithrombin-III, while HS3ST2, HS3ST3A, HS3ST3B, HS3ST4, and HS3ST6 are described to provide the HS-binding motifs for the glycoprotein gD of herpes simplex virus-1 (HSV-1). HS3ST regulations in cancer cells, cell proliferation, and tumor progression, overview
physiological function
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3-O-sulfotransferase-2-generated heparan sulfate serves as a receptor during herpes simplex virus type-1 entry and spread. The enzyme plays a role in HSV-1 pathogenesis
physiological function
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enzyme expression in lung cancer cells H460 and H23 inhibits cell migration, invasion, cell proliferation
physiological function
-
isoform 3-OST-2 mediates herpes simplex virus-1 entry and spread
physiological function
the enzyme is involved in heparan sulfate biosynthesis
physiological function
isozymes HS3ST2, HS3ST3B, and HS3ST4 may exhibit a broader selectivity. Re-expression of HS3ST2 in MDA-MB-231 cells leads to an increase in cell viability and invasion, MDA-MB-231 cells carrying HS3ST2 expression display a significant increase in proliferation and survival. Consistent with a proinvasive phenotype, Erk1/2 and beta-catenin signalling is upregulated in HS3ST2-expressing cells in an HS-dependent manner. The tumor-promoting effects of HS3ST2, HS3ST3B, and HS3ST4 are related to sustained activation of Src, Akt, and NF-kappaB, and upregulation of the anti-apoptotic proteins survivin and XIAP. Importantly, all these signalling molecules have been well described to play a critical role in promoting tumor growth and resistance to apoptosis
physiological function
the sulfotransferase HS3ST2 regulates breast cancer cell viability and invasion. It catalyzes the 3-O-sulfation of glucosamine in heparan sulfate. 3-O-sulfation of glucosamine is the rarest heparan sulfate (HS) modification step, yet strongly mediating selective cellular processes
additional information
to date, only a few ligands are known to selectively interact with 3-O-sulfated motifs, whereas hundreds of HS-binding proteins have been identified
additional information
-
to date, only a few ligands are known to selectively interact with 3-O-sulfated motifs, whereas hundreds of HS-binding proteins have been identified
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). HS3S2_HUMAN
367
1
41501
Swiss-Prot
Mitochondrion (Reliability: 4)
HS3S2_MOUSE
367
1
41378
Swiss-Prot
Mitochondrion (Reliability: 5)
HS3S2_RAT
367
1
41378
Swiss-Prot
Mitochondrion (Reliability: 5)
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
expression of 3-OST-2 renders CHO-K1 cell, which are normally resistant, susceptible to viral entry of wild-type and a Q27P mutant, Rid1, forms of HSV-1, requiring the gD receptors, Rid1 mutation at gD prevents its entry via some receptors including HVEM and 3-OS HS generated by 3-OST-3, overview
additional information
-
expression of 3-OST-2 renders CHO-K1 cell, which are normally resistant, susceptible to viral entry of wild-type and a Q27P mutant, Rid1, forms of HSV-1, requiring the gD receptors, Rid1 mutation at gD prevents its entry via some receptors including HVEM and 3-OS HS generated by 3-OST-3, overview
additional information
generation of a truncated mutant enzyme depleted of its catalytic domain. The mutant remains in the Golgi apparatus, while the wild-type full-length enzyme localizes in the plasma membrane
additional information
-
generation of a truncated mutant enzyme depleted of its catalytic domain. The mutant remains in the Golgi apparatus, while the wild-type full-length enzyme localizes in the plasma membrane
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis and developmental expression analysis of the 3-OST gene family, sequence comparisons, phylogentic analysis, overview
-
gD-type-3-OST-2, DNA and amino acid sequence determination and sequence comparisons, neuronal tissue expression analysis
-
gene HS3ST2, quantitative real-time PCR enzyme expression analysis, recombinant overexpression in MDA-MB-231 and MCF-7 cells, cell transcriptome analysis, overview. The expression levels of several genes are altered by overexpression of HS3ST2
gene HS3ST2, real-time RT-PCR expression analysis, functional recombinant overexpression of HS3ST2 in HeLa cells. Transfection with the plasmid encoding non-tagged HS3ST2 results in the production of 3-O-sulfated HS. HS3ST2-transfected HeLa cells are indeed capable of interacting with HSV-1 gD protein. Analysis of subcellular localization of the recombinant isozyme
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
exposure of chondrosarcoma cells to 5-aza-2'-deoxycytidine up-regulates expression of 3-OST2 mRNA
-
expression of the genes encoding HS-modifying enzymes is frequently dysregulated in cancer and other diseases
the overall transcriptional activity of the main heparan sulfate biosynthesis-involved genes (EXT1, EXT2, NDST1, NDST2, GLCE, HS2ST1, HS3ST1, HS3ST2, HS6ST1, HS6ST2, SULF1, SULF2, HPSE) is decreased by 1.5-2fold in Grade II-III glioma (p < 0.01) and by 3-fold in Grade IV glioma (glioblastoma multiforme, GBM) (p < 0.05), as compared with the para-tumourous tissue
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
possible role of 3-OST-2 in the spread of HSV-1 infection in the brain
medicine
-
Silencing of the 3-OST-2 gene is present in a wide range of human cancers. Possible diagnostic and potentially therapeutic value.
medicine
-
the results provide evidence for specific epigenetic regulation of 3-OST genes resulting in altered heparan sulfate proteoglycans and point to a defect of heparan sulfate-3-O-sulfation as a factor in cancer progression
medicine
-
enzyme hypermethylation is an independent prognostic indicator for overall survival in node-negative stage I-II non-small cell lung cancer
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shworak, N.W.; Liu, J.; Petros, L.M.; Zhang, L.; Kobayashi, M.; Copeland, N.G.; Jenkins, N.A.; Rosenberg, R.D.
Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase
J. Biol. Chem.
274
5170-5184
1999
Homo sapiens
brenda
Liu, J.; Shworak, N.W.; Sinay, P.; Schwartz, J.J.; Zhang, L.; Fritze, L.M.S.; Rosenberg, R.D.
Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities
J. Biol. Chem.
274
5185-5192
1999
Homo sapiens
brenda
Miyamoto, K.; Asada, K.; Fukutomi, T.; Okochi, E.; Yagi, Y.; Hasegawa, T.; Asahara, T.; Sugimura, T.; Ushijima, T.
Methylation-associated silencing of heparan sulfate D-glucosaminyl 3-O-sulfotransferase-2 (3-OST-2) in human breast, colon, lung and pancreatic cancers
Oncogene
22
274-280
2003
Homo sapiens
brenda
O'Donnell C.D.; Tiwari, V.; Oh, M.J.; Shukla, D.
A role for heparan sulfate 3-O-sulfotransferase isoform 2 in herpes simplex virus type 1 entry and spread
Virology
346 Iss 2
452-459
2005
Homo sapiens
brenda
Cadwallader, A.B.; Yost, H.J.
Combinatorial expression patterns of heparan sulfate sulfotransferases in zebrafish: I. The 3-O-sulfotransferase family
Dev. Dyn.
235
3423-3431
2006
Danio rerio
brenda
Lawrence, R.; Yabe, T.; Haj Mohammadi, S.; Rhodes, J.; McNeely, M.; Liu, J.; Lamperti, E.D.; Toselli, P.A.; Lech, M.; Spear, P.G.; Rosenberg, R.D.; Shworak, N.W.
The principal neuronal gD-type 3-O-sulfotransferases and their products in central and peripheral nervous system tissues
Matrix Biol.
26
442-455
2007
Drosophila melanogaster
brenda
O'Donnell, C.D.; Tiwari, V.; Oh, M.; Shukla, D.
A role for heparan sulfate 3-O-sulfotransferase isoform 2 in herpes simplex virus type 1 entry and spread
Virology
346
452-459
2006
Homo sapiens (Q9Y278), Homo sapiens
brenda
Bui, C.; Ouzzine, M.; Talhaoui, I.; Sharp, S.; Prydz, K.; Coughtrie, M.W.; Fournel-Gigleux, S.
Epigenetics: methylation-associated repression of heparan sulfate 3-O-sulfotransferase gene expression contributes to the invasive phenotype of H-EMC-SS chondrosarcoma cells
FASEB J.
24
436-450
2010
Homo sapiens
brenda
Baldwin, J.; Antoine, T.E.; Shukla, D.; Tiwari, V.
Zebrafish encoded 3-O-sulfotransferase-2 generated heparan sulfate serves as a receptor during HSV-1 entry and spread
Biochem. Biophys. Res. Commun.
432
672-676
2013
Danio rerio
brenda
Yakoub, A.M.; Rawal, N.; Maus, E.; Baldwin, J.; Shukla, D.; Tiwari, V.
Comprehensive analysis of herpes simplex virus 1 (HSV-1) entry mediated by zebrafish 3-O-sulfotransferase isoforms: implications for the development of a zebrafish model of HSV-1 infection
J. Virol.
88
12915-12922
2014
Danio rerio
brenda
Hwang, J.A.; Kim, Y.; Hong, S.H.; Lee, J.; Cho, Y.G.; Han, J.Y.; Kim, Y.H.; Han, J.; Shim, Y.M.; Lee, Y.S.; Kim, D.H.
Epigenetic inactivation of heparan sulfate (glucosamine) 3-O-sulfotransferase 2 in lung cancer and its role in tumorigenesis
PLoS ONE
8
e79634
2013
Homo sapiens
brenda
Ushakov, V.; Tsidulko, A.; De La Bourdonnaye, G.; Kazanskaya, G.; Volkov, A.; Kiselev, R.; Kobozev, V.; Kostromskaya, D.; Gaytan, A.; Krivoshapkin, A.; Aidagulova, S.; Grigorieva, E.
Heparan sulfate biosynthetic system is inhibited in human glioma due to EXT1/2 and HS6ST1/2 down-regulation
Int. J. Mol. Sci.
18
2301
2017
Homo sapiens (Q9Y278)
brenda
Delos, M.; Foulquier, F.; Hellec, C.; Vicogne, D.; Fifre, A.; Carpentier, M.; Papy-Garcia, D.; Allain, F.; Denys, A.
Heparan sulfate 3-O-sulfotransferase 2 (HS3ST2) displays an unexpected subcellular localization in the plasma membrane
Biochim. Biophys. Acta
1862
1644-1655
2018
Homo sapiens (Q9Y278), Homo sapiens
brenda
Teixeira, F.; Vijaya Kumar, A.; Kumar Katakam, S.; Cocola, C.; Pelucchi, P.; Graf, M.; Kiesel, L.; Reinbold, R.; Pavao, M.; Greve, B.; Goette, M.
The heparan sulfate sulfotransferases HS2ST1 and HS3ST2 are novel regulators of breast Cancer stem-cell Properties
Front. Cell Dev. Biol.
8
559554
2020
Homo sapiens (Q9Y278)
brenda
Denys, A.; Allain, F.
The emerging roles of heparan sulfate 3-O-sulfotransferases in cancer
Front. Oncol.
9
507
2019
Homo sapiens (Q9Y278), Homo sapiens
brenda
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