| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-73 |
Sentence |
denotes |
Multiple isoforms of heparan sulfate D-glucosaminyl 3-O-sulfotransferase. |
| T2 |
74-177 |
Sentence |
denotes |
Isolation, characterization, and expression of human cdnas and identification of distinct genomic loci. |
| T3 |
178-322 |
Sentence |
denotes |
3-O-Sulfated glucosaminyl residues are rare constituents of heparan sulfate and are essential for the activity of anticoagulant heparan sulfate. |
| T4 |
323-497 |
Sentence |
denotes |
Cellular production of the critical active structure is controlled by the rate-limiting enzyme, heparan sulfate D-glucosaminyl 3-O-sulfotransferase-1 (3-OST-1) (EC 2.8.2.23). |
| T5 |
498-658 |
Sentence |
denotes |
We have probed the expressed sequence tag data base with the carboxyl-terminal sulfotransferase domain of 3-OST-1 to reveal three novel, incomplete human cDNAs. |
| T6 |
659-727 |
Sentence |
denotes |
These were utilized in library screens to isolate full-length cDNAs. |
| T7 |
728-883 |
Sentence |
denotes |
Clones corresponding to predominant transcripts were obtained for the 367-, 406-, and 390-amino acid enzymes 3-OST-2, 3-OST-3A, and 3-OST-3B, respectively. |
| T8 |
884-1070 |
Sentence |
denotes |
These type II integral membrane proteins are comprised of a divergent amino-terminal region and a very homologous carboxyl-terminal sulfotransferase domain of approximately 260 residues. |
| T9 |
1071-1125 |
Sentence |
denotes |
Also recovered were partial length clones for 3-OST-4. |
| T10 |
1126-1269 |
Sentence |
denotes |
Expression of the full-length enzymes confirms the 3-O-sulfation of specific glucosaminyl residues within heparan sulfate (Liu, J., Shworak, N. |
| T11 |
1270-1297 |
Sentence |
denotes |
W., Sinaÿ, P., Schwartz, J. |
| T12 |
1298-1300 |
Sentence |
denotes |
J. |
| T13 |
1301-1322 |
Sentence |
denotes |
Zhang, L., Fritze, L. |
| T14 |
1323-1325 |
Sentence |
denotes |
M. |
| T15 |
1326-1347 |
Sentence |
denotes |
S., and Rosenberg, R. |
| T16 |
1348-1360 |
Sentence |
denotes |
D. (1999) J. |
| T17 |
1361-1366 |
Sentence |
denotes |
Biol. |
| T18 |
1367-1372 |
Sentence |
denotes |
Chem. |
| T19 |
1373-1389 |
Sentence |
denotes |
274, 5185-5192). |
| T20 |
1390-1510 |
Sentence |
denotes |
Southern analyses suggest the human 3OST1, 3OST2, and 3OST4 genes, and the corresponding mouse isologs, are single copy. |
| T21 |
1511-1614 |
Sentence |
denotes |
However, 3OST3A and 3OST3B genes are each duplicated in humans and show at least one copy each in mice. |
| T22 |
1615-1762 |
Sentence |
denotes |
Intriguingly, the entire sulfotransferase domain sequence of the 3-OST-3B cDNA (774 base pairs) was 99.2% identical to the same region of 3-OST-3A. |
| T23 |
1763-1920 |
Sentence |
denotes |
Together, these data argue that the structure of this functionally important region is actively maintained by gene conversion between 3OST3A and 3OST3B loci. |
| T24 |
1921-2134 |
Sentence |
denotes |
Interspecific mouse back-cross analysis identified the loci for mouse 3Ost genes and syntenic assignments of corresponding human isologs were confirmed by the identification of mapped sequence-tagged site markers. |
| T25 |
2135-2357 |
Sentence |
denotes |
Northern blot analyses indicate brain exclusive and brain predominant expression of 3-OST-4 and 3-OST-2 transcripts, respectively; whereas, 3-OST-3A and 3-OST-3B isoforms show widespread expression of multiple transcripts. |
| T26 |
2358-2492 |
Sentence |
denotes |
The reiteration and conservation of the 3-OST sulfotransferase domain suggest that this structure is a self-contained functional unit. |
| T27 |
2493-2720 |
Sentence |
denotes |
Moreover, the extensive number of 3OST genes with diverse expression patterns of multiple transcripts suggests that the novel 3-OST enzymes, like 3-OST-1, regulate important biologic properties of heparan sulfate proteoglycans. |