Superoxide dismutase within the bovine erythrocyte membrane

Petkau, A.; Copps, T. P.; Kelly, K.

doi:10.1016/0005-2736(81)90513-7

Cited by 14 publications

(5 citation statements)

References 39 publications

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“…Misfolded SOD1 is found at high levels around vacuoles in transgenic mouse neurons in what appears to remain of the IMS (Wong et al ., 1995; Jaarsma et al ., 2001; Graffmo et al ., 2013). SOD1 associates with the intracellular face of the plasma membrane but misfolded SOD1 is also found on the outer mitochondrial membrane in ALS spinal cord cells (Petkau and Copps, 1979; Vande Velde et al ., 2008). Accumulation is progressive and, importantly, begins just prior to the onset of ALS (Pickles et al ., 2013).…”

Section: Sod1 Aggregation In Alsmentioning

confidence: 99%

“…Accumulation is progressive and, importantly, begins just prior to the onset of ALS (Pickles et al ., 2013). SOD1, particularly the metal-free state, incorporates within biological membranes and disorders lipid packing (Petkau and Chelack, 1976; Petkau and Copps, 1979; Lepock et al ., 1981). Chng and Strange (2014) used molecular dynamics simulations to show how residues in the conformationally dynamic electrostatic and zinc-binding loops bind octanol and mediate interactions with bilayer surfaces.…”

Section: Sod1 Aggregation In Alsmentioning

confidence: 99%

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The biophysics of superoxide dismutase-1 and amyotrophic lateral sclerosis

Wright

Antonyuk

Hasnain

2019

Quart. Rev. Biophys.

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Few proteins have come under such intense scrutiny as superoxide dismutase-1 (SOD1). For almost a century, scientists have dissected its form, function and then later its malfunction in the neurodegenerative disease amyotrophic lateral sclerosis (ALS). We now know SOD1 is a zinc and copper metalloenzyme that clears superoxide as part of our antioxidant defence and respiratory regulation systems. The possibility of reduced structural integrity was suggested by the first crystal structures of human SOD1 even before deleterious mutations in thesod1gene were linked to the ALS. This concept evolved in the intervening years as an impressive array of biophysical studies examined the characteristics of mutant SOD1 in great detail. We now recognise how ALS-related mutations perturb the SOD1 maturation processes, reduce its ability to fold and reduce its thermal stability and half-life. Mutant SOD1 is therefore predisposed to monomerisation, non-canonical self-interactions, the formation of small misfolded oligomers and ultimately accumulation in the tell-tale insoluble inclusions found within the neurons of ALS patients. We have also seen that several post-translational modifications could push wild-type SOD1 down this toxic pathway. Recently we have come to view ALS as a prion-like disease where both the symptoms, and indeed SOD1 misfolding itself, are transmitted to neighbouring cells. This raises the possibility of intervention after the initial disease presentation. Several small-molecule and biologic-based strategies have been devised which directly target the SOD1 molecule to change the behaviour thought to be responsible for ALS. Here we provide a comprehensive review of the many biophysical advances that sculpted our view of SOD1 biology and the recent work that aims to apply this knowledge for therapeutic outcomes in ALS.

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Section: Sod1 Aggregation In Alsmentioning

confidence: 99%

Section: Sod1 Aggregation In Alsmentioning

confidence: 99%

The biophysics of superoxide dismutase-1 and amyotrophic lateral sclerosis

Wright

Antonyuk

Hasnain

2019

Quart. Rev. Biophys.

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“…The enzyme SOD (EC 1.15.1.1; O2 Á -:O 2 Áoxidoreductase; SOD, m.w. 32,500) consists of a class of metallo-proteins, which includes a copper zinc-superoxide dismutase (CuZn-SOD) that is found abundantly in the cytosol of oxygen-metabolizing eukaryotic cells (3,4). SOD is highly efficient in scavenging superoxide (O 2 Á -) radical by catalyzing the disproportionation of the radical to hydrogen peroxide (H 2 O 2 ) and molecular oxygen, thereby greatly accelerating the rate at which O 2 Áis removed (5).…”

Section: Introductionmentioning

confidence: 99%

Activities of erythrocyte antioxidant enzymes in cancer patients

Abiaka

Al-Awadi

Al‐Sayer

et al. 2002

Clinical Laboratory Analysis

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We measured the activities of erythrocyte superoxide dismutase (SOD) and glutathione peroxidase (GPX) before therapy in 97 patients with cancer in various sites (gastrointestinal tract (GIT) (n=40), breast (n=30), and others (n=27)), and in 60 matched controls to assess antioxidant enzyme protection. Hemolysate hemoglobin (Hb) was measured spectrophotometrically. The activity of SOD (U/g Hb) was significantly lower in all sites (when all the cancer sites were considered as a group), GIT, breast, and other sites compared to the controls (P<0.0001, P<0.0001, P<0.0001 and P<0.0001, respectively). The activity of GPX (U/g Hb) was significantly decreased in all sites, GIT, and breast cancer sites than in the controls (P=0.024, P=0.033, and P=0.043, respectively). Age showed a weak negative correlation with enzyme activities in controls and patients. There was no significant association between SOD and GPX activities in either the controls or the patients. These results suggest that there may be a greater antioxidant burden for SOD than GPX in cancer, and that a weak association exists between the activities of the two enzymes in antioxidant protection.

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“…Such samples may conceivably arise in the case of membrane preparations where it is proposed that approximately 0.2% of the superoxide dismutase in a cell resides. 33 Furthermore, ideally the radiant power should supply adequate energy in the absorption band of the reactant and negligible energy outside the band. The laser as a light source fulfils this requirement to a nicety.…”

Section: Discussionmentioning

confidence: 99%

An improved photochemical method for the rapid spectrophotometric detection of superoxide dismutase

Madon

2001

Redox Report

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A sensitive and convenient method is described for estimating superoxide dismutase activity using a photochemical augmentation procedure. This method is applicable to both liquid assays and polyacrylamide gel electropherograms. The flux of superoxide is generated by illuminating a reaction mixture containing dianisidine and riboflavin by either a laser source or light from a fluorescent lamp. The oxidation of dianisidine, as sensitized by riboflavin, is enhanced by superoxide dismutase. The increase is linearly dependent on superoxide dismutase concentration. The photochemical reaction is allowed to proceed uninterrupted for a standardized optimum time and intensity of illumination and then terminated by addition of a buffer, 'finibuf', which stabilizes the chromophoric complex formed. This permits the spectrophotometric absorbance measurements of a number of samples collectively and also eliminates the interruption of illumination with the concomitant requirement of a spectrophotometer for constant recording of the absorbance. This method is of utility to both biochemists and clinicians.

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Superoxide dismutase within the bovine erythrocyte membrane

Cited by 14 publications

References 39 publications

The biophysics of superoxide dismutase-1 and amyotrophic lateral sclerosis

The biophysics of superoxide dismutase-1 and amyotrophic lateral sclerosis

Activities of erythrocyte antioxidant enzymes in cancer patients

An improved photochemical method for the rapid spectrophotometric detection of superoxide dismutase

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