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HEPARAN SULFATE-GLUCOSAMINE 3-SULFOTRANSFERASE 1; HS3ST1

HEPARAN SULFATE-GLUCOSAMINE 3-SULFOTRANSFERASE 1; HS3ST1

Alternative titles; symbolsHEPARAN SULFATE (GLUCOSAMINE) 3-O-SULFOTRANSFERASE 1HEPARAN SULFATE D-GLUCOSAMINYL 3-O-SULFOTRANSFERASE 13OST3OST1HGNC Approved Gene S...

Alternative titles; symbols

  • HEPARAN SULFATE (GLUCOSAMINE) 3-O-SULFOTRANSFERASE 1
  • HEPARAN SULFATE D-GLUCOSAMINYL 3-O-SULFOTRANSFERASE 1
  • 3OST
  • 3OST1

HGNC Approved Gene Symbol: HS3ST1

Cytogenetic location: 4p15.33 Genomic coordinates (GRCh38): 4:11,393,149-11,434,397 (from NCBI)

▼ Description
The cellular rate of anticoagulant heparan sulfate proteoglycan generation is determined by the level of the microsomal activity 'HS-act conversion activity,' which is predominantly composed of the enzyme heparan sulfate D-glucosaminyl 3-O-sulfotransferase (EC 2.8.2.23) (summary by Shworak et al., 1997).

▼ Cloning and Expression
Liu et al. (1996) isolated the mouse 3Ost protein and found that it migrates as a 46-kD polypeptide by SDS-PAGE.

Shworak et al. (1997) cloned mouse and human 3OST cDNAs. The predicted 307-amino acid human 3OST protein shares 93% sequence similarity with mouse 3Ost. The 3OST protein contains a signal sequence and 5 potential N-glycosylation sites. Both human and mouse 3OST have a calculated molecular mass of approximately 36 kD; Shworak et al. (1997) attributed the discrepancy between the observed and calculated molecular masses to glycosylation. Based on the proposed site of heparan biosynthesis and on structural analysis of the 3OST protein, the authors suggested that 3OST is an intraluminal Golgi enzyme. Northern blot analysis of human cells showed that 3OST is expressed as a 1.7-kb mRNA.

▼ Gene Structure
HajMohammadi et al. (2003) determined that exon 8 of the mouse Hs3st1 gene contains the entire enzyme-coding region.

▼ Mapping
Gross (2014) mapped the HS3ST1 gene to chromosome 4p15.33 based on an alignment of the HS3ST1 sequence (GenBank AF019386) with the genomic sequence (GRCh37).

▼ Gene Function
Shworak et al. (1997) showed that the human and mouse 3OST proteins exhibited HS-act conversion and 3OST activities when expressed in vitro.

▼ Animal Model
HajMohammadi et al. (2003) demonstrated that Hs3st1-knockout mice were devoid of 3OST1 activity in plasma and tissue extracts. Hs3st1-null mice showed dramatic reductions in tissue levels of anticoagulant heparan sulfate, but they maintained wildtype levels of tissue fibrin accumulation under both normoxic and hypoxic conditions. Following induction of deendothelialization and occlusive thrombosis, Hs3st1-null mice and wildtype mice had indistinguishable occlusion times and comparable levels of thrombin-antithrombin complexes; thus, mutant mice showed no obvious procoagulant phenotype. However, Hs3st1-null mice exhibited genetic background-specific lethality and intrauterine growth retardation without gross coagulopathy.

Tags: 4p15.33