4.2 Article

The Effect of the Gly139His, Gly143His, and Ser142His Mouse Heme Oxygenase-1 Mutants on the HO Reaction In Vivo and In Vitro

Publisher

WILEY
DOI: 10.1002/ar.21284

Keywords

heme oxygenase-1; Gly139His mutant; Gly143His mutant; mouse

Funding

  1. Major State Basic Research Development Program of China [2009CB521702]
  2. Heilongjiang Province Foundation for Returnees [LC06C21]

Ask authors/readers for more resources

Heme oxygenase-1 (HO-1), which catalyzes the degradation of heme to iron, carbon monoxide, and biliverdin, performs a cytoprotective function. Previous studies on the crystal structure of the human and rat HO-1 in complex with heme showed that Gly139His (G139H) and Gly143His (G143H) mutants have no HO activity. In the present study, we reported the effect of the G139H, G143H, and Ser142His mutants of mouse HO-1 on the HO reaction in vivo and in vitro. In vitro, of the mutant transfectants, only Ser142His catalyzed degradation of heme, retaining 31.7% of the wildtype mouse HO-1 activity, whereas G139H and G143H mutants exhibited no activity. In vivo, only Tg HO-1 G143H females presented with anemia, enlarged spleen and tissue iron overload, which was similar to HO-1(-/-) mice. The results suggested the critical role of Gly139 and Gly143 in maintaining HO-1 activity in vitro and the critical role of Gly143 in maintaining HO-1 activity in vivo. Anat Rec, 294:112-118, 2011. (C) 2010 Wiley-Liss, Inc.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.2
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available