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(Received for publication, December 23, 1996, and in revised form, March 28, 1997)
From the 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
Volume 272, Number 44,
Issue of October 31, 1997
pp. 28008-28019
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
Molecular Cloning and Expression of Mouse and Human cDNAs
Encoding Heparan Sulfate D-Glucosaminyl
3-O-Sulfotransferase
§
,
,§
,
,
,
and§
Department of Biology, Massachusetts
Institute of Technology, Cambridge, Massachusetts 02139 and the
§ Department of Medicine, Harvard Medical School, Beth
Israel Hospital, Boston, Massachusetts 02215
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 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 ~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 (~34
kDa) and the previously purified enzyme (~46 kDa). The two 3-OST
species also exhibit ~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.
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N. Hiraoka, H. Nakagawa, E. Ong, T. O. Akama, M. N. Fukuda, and M. Fukuda Molecular Cloning and Expression of Two Distinct Human Chondroitin 4-O-Sulfotransferases That Belong to the HNK-1 Sulfotransferase Gene Family J. Biol. Chem., June 23, 2000; 275(26): 20188 - 20196. [Abstract] [Full Text] [PDF]
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K. Honke, M. Tsuda, S. Koyota, Y. Wada, N. Iida-Tanaka, I. Ishizuka, J. Nakayama, and N. Taniguchi Molecular Cloning and Characterization of a Human beta -Gal-3'-sulfotransferase That Acts on Both Type 1 and Type 2 (Galbeta 1-3/1-4GlcNAc-R) Oligosaccharides J. Biol. Chem., January 5, 2001; 276(1): 267 - 274. [Abstract] [Full Text] [PDF]
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T. Okuda, S. Mita, S. Yamauchi, M. Fukuta, H. Nakano, T. Sawada, and O. Habuchi Molecular Cloning and Characterization of GalNAc 4-Sulfotransferase Expressed in Human Pituitary Gland J. Biol. Chem., December 15, 2000; 275(51): 40605 - 40613. [Abstract] [Full Text] [PDF]
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L. Zhang, R. Lawrence, J. J. Schwartz, X. Bai, G. Wei, J. D. Esko, and R. D. Rosenberg The Effect of Precursor Structures on the Action of Glucosaminyl 3-O-Sulfotransferase-1 and the Biosynthesis of Anticoagulant Heparan Sulfate J. Biol. Chem., July 27, 2001; 276(31): 28806 - 28813. [Abstract] [Full Text] [PDF]
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M. A. S. Pinhal, B. Smith, S. Olson, J.-i. Aikawa, K. Kimata, and J. D. Esko Enzyme interactions in heparan sulfate biosynthesis: Uronosyl 5-epimerase and 2-O-sulfotransferase interact in vivo PNAS, November 6, 2001; 98(23): 12984 - 12989. [Abstract] [Full Text] [PDF]
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B. L. Allen, M. S. Filla, and A. C. Rapraeger Role of heparan sulfate as a tissue-specific regulator of FGF-4 and FGF receptor recognition J. Cell Biol., November 26, 2001; 155(5): 845 - 858. [Abstract] [Full Text] [PDF]
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