Molecular cloning and expression of mouse and human cDNAs encoding heparan sulfate D-glucosaminyl 3-O-sulfotransferase - PubMed (original) (raw)
. 1997 Oct 31;272(44):28008-19.
doi: 10.1074/jbc.272.44.28008.
Affiliations
- PMID: 9346953
- DOI: 10.1074/jbc.272.44.28008
Free article
Molecular cloning and expression of mouse and human cDNAs encoding heparan sulfate D-glucosaminyl 3-O-sulfotransferase
N W Shworak et al. J Biol Chem. 1997.
Free article
Abstract
The cellular rate of anticoagulant heparan sulfate proteoglycan (HSPGact) generation is determined by the level of a kinetically limiting microsomal activity, HSact conversion activity, which is predominantly composed of the long sought heparan sulfate D-glucosaminyl 3-O-sulfotransferase (3-OST) (Shworak, N. W., Fritze, L. M. S., Liu, J., Butler, L. D., and Rosenberg, R. D. (1996) J. Biol. Chem. 271, 27063-27071; Liu, J., Shworak, N. W., Fritze, L. M. S., Edelberg, J. M., and Rosenberg, R. D. (1996) J. Biol. Chem. 271, 27072-27082). Mouse 3-OST cDNAs were isolated by proteolyzing the purified enzyme with Lys-C, sequencing the resultant peptides as well as the existing amino terminus, employing degenerate polymerase chain reaction primers corresponding to the sequences of the peptides as well as the amino terminus to amplify a fragment from LTA cDNA, and utilizing the resultant probe to obtain full-length enzyme cDNAs from a lambda Zap Express LTA cDNA library. Human 3-OST cDNAs were isolated by searching the expressed sequence tag data bank with the mouse sequence, identifying a partial-length human cDNA and utilizing the clone as a probe to isolate a full-length enzyme cDNA from a lambda TriplEx human brain cDNA library. The expression of wild-type mouse 3-OST as well as protein A-tagged mouse enzyme by transient transfection of COS-7 cells and the expression of both wild-type mouse and human 3-OST by in vitro transcription/translation demonstrate that the two cDNAs directly encode both HSact conversion and 3-OST activities. The mouse 3-OST cDNAs exhibit three different size classes because of a 5'-untranslated region of variable length, which results from the insertion of 0-1629 base pairs (bp) between residues 216 and 217; however, all cDNAs contain the same open reading frame of 933 bp. The length of the 3'-untranslated region ranges from 301 to 430 bp. The nucleic acid sequence of mouse and human 3-OST cDNAs are approximately 85% similar, encoding novel 311- and 307-amino acid proteins of 35,876 and 35,750 daltons, respectively, that are 93% similar. The encoded enzymes are predicted to be intraluminal Golgi residents, presumably interacting via their C-terminal regions with an integral membrane protein. Both 3-OST species exhibit five potential N-glycosylation sites, which account for the apparent discrepancy between the molecular masses of the encoded enzyme (approximately 34 kDa) and the previously purified enzyme (approximately 46 kDa). The two 3-OST species also exhibit approximately 50% similarity with all previously identified forms of the heparan biosynthetic enzyme N-deacetylase/N-sulfotransferase, which suggests that heparan biosynthetic enzymes share a common sulfotransferase domain.
Similar articles
- Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. Isolation, characterization, and expression of human cdnas and identification of distinct genomic loci.
Shworak NW, Liu J, Petros LM, Zhang L, Kobayashi M, Copeland NG, Jenkins NA, Rosenberg RD. Shworak NW, et al. J Biol Chem. 1999 Feb 19;274(8):5170-84. doi: 10.1074/jbc.274.8.5170. J Biol Chem. 1999. PMID: 9988767 - Expression of heparan sulfate D-glucosaminyl 3-O-sulfotransferase isoforms reveals novel substrate specificities.
Liu J, Shworak NW, Sinaÿ P, Schwartz JJ, Zhang L, Fritze LM, Rosenberg RD. Liu J, et al. J Biol Chem. 1999 Feb 19;274(8):5185-92. doi: 10.1074/jbc.274.8.5185. J Biol Chem. 1999. PMID: 9988768 - Purification of heparan sulfate D-glucosaminyl 3-O-sulfotransferase.
Liu J, Shworak NW, Fritze LM, Edelberg JM, Rosenberg RD. Liu J, et al. J Biol Chem. 1996 Oct 25;271(43):27072-82. doi: 10.1074/jbc.271.43.27072. J Biol Chem. 1996. PMID: 8900198 - Human dehydroepiandrosterone sulfotransferase: molecular cloning of cDNA and genomic DNA.
Otterness DM, Weinshilboum R. Otterness DM, et al. Chem Biol Interact. 1994 Jun;92(1-3):145-59. doi: 10.1016/0009-2797(94)90060-4. Chem Biol Interact. 1994. PMID: 8033249 Review.
Cited by
- Genome-wide screens uncover KDM2B as a modifier of protein binding to heparan sulfate.
Weiss RJ, Spahn PN, Chiang AWT, Liu Q, Li J, Hamill KM, Rother S, Clausen TM, Hoeksema MA, Timm BM, Godula K, Glass CK, Tor Y, Gordts PLSM, Lewis NE, Esko JD. Weiss RJ, et al. Nat Chem Biol. 2021 Jun;17(6):684-692. doi: 10.1038/s41589-021-00776-9. Epub 2021 Apr 12. Nat Chem Biol. 2021. PMID: 33846619 Free PMC article. - Glypicans and Heparan Sulfate in Synaptic Development, Neural Plasticity, and Neurological Disorders.
Kamimura K, Maeda N. Kamimura K, et al. Front Neural Circuits. 2021 Feb 10;15:595596. doi: 10.3389/fncir.2021.595596. eCollection 2021. Front Neural Circuits. 2021. PMID: 33679334 Free PMC article. Review. - Heparan Sulfate Proteoglycans: Key Mediators of Stem Cell Function.
Ravikumar M, Smith RAA, Nurcombe V, Cool SM. Ravikumar M, et al. Front Cell Dev Biol. 2020 Nov 19;8:581213. doi: 10.3389/fcell.2020.581213. eCollection 2020. Front Cell Dev Biol. 2020. PMID: 33330458 Free PMC article. Review. - A quantitative method to detect non-antithrombin-binding 3-O-sulfated units in heparan sulfate.
Mochizuki H, Futatsumori H, Suzuki E, Kimata K. Mochizuki H, et al. J Biol Chem. 2021 Jan-Jun;296:100115. doi: 10.1074/jbc.RA120.015864. Epub 2020 Dec 3. J Biol Chem. 2021. PMID: 33234593 Free PMC article. - Expression and functional characterization of two natural heparin-binding site variants of antithrombin.
Dinarvand P, Yang L, Villoutreix BO, Rezaie AR. Dinarvand P, et al. J Thromb Haemost. 2018 Feb;16(2):330-341. doi: 10.1111/jth.13920. Epub 2018 Jan 8. J Thromb Haemost. 2018. PMID: 29215785 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Molecular Biology Databases