Assessment of Cu-Zn, D-dimer, and superoxıde dismutase ın patıents with pulmonaray dıseases

FALS mutations in Cu, Zn superoxide dismutase destabilize the dimer and increase dimer dissociation propensity: a large-scale thermodynamic analysis.

Mutations in the dimeric enzyme Cu, Zn superoxide dismutase (SOD1) leading to its aggregation are implicated in the toxicity in familial amyotrophic lateral sclerosis (FALS). We and others have previously shown that aggregation occurs by a pathway involving dimer dissociation, metal-loss from monomers and multimeric assembly of apo-SOD1 monomers. We postulate that FALS mutations cause enhanced ...

The Cu, Zn Superoxide Dismutase: Not Only a Dismutase Enzyme

The Cu,Zn superoxide dismutase (SOD1) is an ubiquitary cytosolic dimeric carbohydrate free molecule, belonging to a family of isoenzymes involved in the scavenger of superoxide anions. This effect certainly represents the main and well known function ascribed to this enzyme. Here we highlight new aspects of SOD1 physiology that point out some inedited effects of this enzyme in addition to the c...

Sequence and structural determinants of Cu, Zn superoxide dismutase aggregation.

Diverse point mutations in the enzyme Cu, Zn superoxide dismutase (SOD1) are linked to its aggregation in the familial form of the disease amyotrophic lateral sclerosis. The disease-associated mutations are known to destabilize the protein, but the structural basis of the aggregation of the destabilized protein and the structure of aggregates are not well understood. Here, we investigate in sil...

Folding and Aggregation of Cu, Zn-Superoxide Dismutase

1.1 ALS and SOD1 In 1993, a genetic link was established between amyotrophic lateral sclerosis (ALS) and mutant forms of Cu,Zn superoxide dismutase (SOD1) (Deng et al. 1993; Rosen et al. 1993), an antioxidant enzyme that catalyzes the dismutation of the damaging free radical superoxide anion (O2-) to hydrogen peroxide (H2O2) and diatomic oxygen (O2) via cyclic reduction and oxidation of a prote...

Mutant mice, Cu,Zn superoxide dismutase, and motor neuron degeneration.