Beta-galactoside alpha-2,6-sialyltransferase 1 is an enzyme that in humans is encoded by the ST6GAL1 gene.[5]
The protein encoded by this gene is a type II membrane protein that catalyzes the transfer of sialic acid from CMP-sialic acid to galactose-containing substrates. The encoded protein, which is normally found in the Golgi but which can be proteolytically processed to a soluble form, is involved in the generation of the cell-surface carbohydrate determinants and differentiation antigens HB-6, CDw75, and CD76. This protein is a member of glycosyltransferase family 29. Three transcript variants encoding two different isoforms have been found for this gene.[6]
Transcripts of ST6GAL1 are found in mouse high endothelial cells of mesenteric lymph node and Peyer's patches, and it could be involved in the B cell homing to Peyer's patches.[7] ST6GAL1 expression has also shown to be upregulated in several types of cancers and has been shown to haves roles in cancer survival and metastasis.[8]
References
- 1 2 3 GRCh38: Ensembl release 89: ENSG00000073849 – Ensembl, May 2017
- 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000022885 – Ensembl, May 2017
- ↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ↑ Grundmann U, Nerlich C, Rein T, Zettlmeissl G (April 1990). "Complete cDNA sequence encoding human beta-galactoside alpha-2,6-sialyltransferase". Nucleic Acids Research. 18 (3): 667. doi:10.1093/nar/18.3.667. PMC 333489. PMID 2408023.
- ↑ "Entrez Gene: ST6GAL1 ST6 beta-galactosamide alpha-2,6-sialyltransferase 1".
- ↑ Lee M, Kiefel H, LaJevic MD, Macauley MS, Kawashima H, O'Hara E, et al. (October 2014). "Transcriptional programs of lymphoid tissue capillary and high endothelium reveal control mechanisms for lymphocyte homing". Nature Immunology. 15 (10): 982–995. doi:10.1038/ni.2983. PMC 4222088. PMID 25173345.
- ↑ Garnham R, Scott E, Livermore KE, Munkley J (August 2019). "ST6GAL1: A key player in cancer". Oncology Letters. 18 (2): 983–989. doi:10.3892/ol.2019.10458. PMC 6607188. PMID 31423157.
Further reading
- Bast BJ, Zhou LJ, Freeman GJ, Colley KJ, Ernst TJ, Munro JM, et al. (January 1992). "The HB-6, CDw75, and CD76 differentiation antigens are unique cell-surface carbohydrate determinants generated by the beta-galactoside alpha 2,6-sialyltransferase". The Journal of Cell Biology. 116 (2): 423–435. doi:10.1083/jcb.116.2.423. PMC 2289289. PMID 1730763.
- Stamenkovic I, Asheim HC, Deggerdal A, Blomhoff HK, Smeland EB, Funderud S (August 1990). "The B cell antigen CD75 is a cell surface sialytransferase". The Journal of Experimental Medicine. 172 (2): 641–643. doi:10.1084/jem.172.2.641. PMC 2188328. PMID 2373995.
- Lance P, Lau KM, Lau JT (1989). "Isolation and characterization of a partial cDNA for a human sialyltransferase". Biochemical and Biophysical Research Communications. 164 (1): 225–232. doi:10.1016/0006-291X(89)91706-3. PMID 2803295.
- Rabouille C, Hui N, Hunte F, Kieckbusch R, Berger EG, Warren G, et al. (April 1995). "Mapping the distribution of Golgi enzymes involved in the construction of complex oligosaccharides". Journal of Cell Science. 108. 108 ( Pt 4) (4): 1617–1627. doi:10.1242/jcs.108.4.1617. PMID 7615680.
- Bruneau N, Lombardo D (1995). "Chaperone function of a Grp 94-related protein for folding and transport of the pancreatic bile salt-dependent lipase". The Journal of Biological Chemistry. 270 (22): 13524–13533. doi:10.1074/jbc.270.22.13524. PMID 7768954.
- Wang X, Vertino A, Eddy RL, Byers MG, Jani-Sait SN, Shows TB, et al. (February 1993). "Chromosome mapping and organization of the human beta-galactoside alpha 2,6-sialyltransferase gene. Differential and cell-type specific usage of upstream exon sequences in B-lymphoblastoid cells". The Journal of Biological Chemistry. 268 (6): 4355–4361. doi:10.1016/S0021-9258(18)53617-6. PMID 7786324.
- Hanasaki K, Varki A, Stamenkovic I, Bevilacqua MP (1994). "Cytokine-induced beta-galactoside alpha-2,6-sialyltransferase in human endothelial cells mediates alpha 2,6-sialylation of adhesion molecules and CD22 ligands". The Journal of Biological Chemistry. 269 (14): 10637–10643. doi:10.1016/S0021-9258(17)34107-8. PMID 8144653.
- Aasheim HC, Aas-Eng DA, Deggerdal A, Blomhoff HK, Funderud S, Smeland EB (April 1993). "Cell-specific expression of human beta-galactoside alpha 2,6-sialyltransferase transcripts differing in the 5' untranslated region". European Journal of Biochemistry. 213 (1): 467–475. doi:10.1111/j.1432-1033.1993.tb17783.x. PMID 8477718.
- Andersson B, Wentland MA, Ricafrente JY, Liu W, Gibbs RA (April 1996). "A "double adaptor" method for improved shotgun library construction". Analytical Biochemistry. 236 (1): 107–113. doi:10.1006/abio.1996.0138. PMID 8619474.
- Sgroi D, Nocks A, Stamenkovic I (1996). "A single N-linked glycosylation site is implicated in the regulation of ligand recognition by the I-type lectins CD22 and CD33". The Journal of Biological Chemistry. 271 (31): 18803–18809. doi:10.1074/jbc.271.31.18803. PMID 8702538.
- Lo NW, Lau JT (1996). "Transcription of the beta-galactoside alpha 2,6-sialyltransferase gene in B lymphocytes is directed by a separate and distinct promoter". Glycobiology. 6 (3): 271–279. doi:10.1093/glycob/6.3.271. PMID 8724135.
- Lo NW, Lau JT (1996). "Novel heterogeneity exists in the 5'-untranslated region of the beta-galactoside alpha 2,6-sialytransferase mRNAs in the human B-lymphoblastoid cell line, louckes". Biochemical and Biophysical Research Communications. 228 (2): 380–385. doi:10.1006/bbrc.1996.1670. PMID 8920923.
- Tsuji S, Datta AK, Paulson JC (1997). "Systematic nomenclature for sialyltransferases". Glycobiology. 6 (7): v–vii. doi:10.1093/glycob/6.7.647. PMID 8953271.
- Ma J, Qian R, Rausa FM, Colley KJ (1997). "Two naturally occurring alpha2,6-sialyltransferase forms with a single amino acid change in the catalytic domain differ in their catalytic activity and proteolytic processing". The Journal of Biological Chemistry. 272 (1): 672–679. doi:10.1074/jbc.272.1.672. PMID 8995311.
- Yu W, Andersson B, Worley KC, Muzny DM, Ding Y, Liu W, et al. (April 1997). "Large-scale concatenation cDNA sequencing". Genome Research. 7 (4): 353–358. doi:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
- Lo NW, Lau JT (1999). "Transcription of the beta-galactoside alpha2,6-sialyltransferase gene (SIAT1) in B-lymphocytes: cell type-specific expression correlates with presence of the divergent 5'-untranslated sequence". Glycobiology. 9 (9): 907–914. doi:10.1093/glycob/9.9.907. PMID 10460832.
- Laroy W, Ameloot P, Contreras R (2001). "Characterization of sialyltransferase mutants using surface plasmon resonance". Glycobiology. 11 (3): 175–182. doi:10.1093/glycob/11.3.175. PMID 11320056.
- Qian R, Chen C, Colley KJ (2001). "Location and mechanism of alpha 2,6-sialyltransferase dimer formation. Role of cysteine residues in enzyme dimerization, localization, activity, and processing". The Journal of Biological Chemistry. 276 (31): 28641–28649. doi:10.1074/jbc.M103664200. PMID 11356854.
- Szabo R, Skropeta D (March 2017). "Advancement of Sialyltransferase Inhibitors: Therapeutic Challenges and Opportunities". Medicinal Research Reviews. 37 (2): 219–270. doi:10.1002/med.21407. PMID 27678392. S2CID 26280291.
- Perez, SJLP, Hsu, ZF, Chang, TT, et al. (2025). "Harnessing the bishomolithocholic acid scaffold for selective sialyltransferase inhibition: A targeted approach to suppress breast cancer metastasis". European Journal of Medicinal Chemistry. 292 117674. doi:10.1016/j.ejmech.2025.117674.