| Id |
Subject |
Object |
Predicate |
Lexical cue |
| T1 |
0-125 |
Sentence |
denotes |
An endoplasmic reticulum transmembrane prolyl 4-hydroxylase is induced by hypoxia and acts on hypoxia-inducible factor alpha. |
| T2 |
126-325 |
Sentence |
denotes |
Prolyl 4-hydroxylases (P4Hs) act on collagens (C-P4Hs) and the oxygen-dependent degradation domains (ODDDs) of hypoxia-inducible factor alpha subunits (HIF-P4Hs) leading to degradation of the latter. |
| T3 |
326-399 |
Sentence |
denotes |
We report data on a human P4H possessing a transmembrane domain (P4H-TM). |
| T4 |
400-467 |
Sentence |
denotes |
Its gene is also found in zebrafish but not in flies and nematodes. |
| T5 |
468-607 |
Sentence |
denotes |
Its sequence more closely resembles those of the C-P4Hs than the HIF-P4Hs, but it lacks the peptide substrate-binding domain of the C-P4Hs. |
| T6 |
608-835 |
Sentence |
denotes |
P4H-TM levels in cultured cells are increased by hypoxia, and P4H-TM is N-glycosylated and is located in endoplasmic reticulum membranes with its catalytic site inside the lumen, a location differing from those of the HIF-P4Hs. |
| T7 |
836-1057 |
Sentence |
denotes |
Despite this, P4H-TM overexpression in cultured neuroblastoma cells reduced HIF-alpha ODDD reporter construct levels, and its small interfering RNA increased HIF-1alpha protein level, in the same way as those of HIF-P4Hs. |
| T8 |
1058-1289 |
Sentence |
denotes |
Furthermore, recombinant P4H-TM hydroxylated the two critical prolines in HIF-1alpha ODDD in vitro, with a preference for the C-terminal proline, whereas it did not hydroxylate any prolines in recombinant type I procollagen chains. |
