Inactivation and modification of superoxide dismutase by glyoxal: Prevention by antibodies

Jabeen, Rukhsana; Saleemuddin, M.; Petersen, John R.; Mohammad, Amin A.

doi:10.1016/j.biochi.2006.10.015

Cited by 16 publications

(7 citation statements)

References 53 publications

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“…The results show that Also, there is a strong correspondence between the estimated content of secondary structure and the AGEs formation kinetics reported in Figure 1 clearly indicating that the reduction in the helical content beta structure is directly related to the glycation extent. Such structural alterations induced by glycation could be responsible for the loss of activity recently observed for native SOD glycated in vitro in the presence of glucose, glyoxal, and methylglyoxal (Jabeen et al, 2007 ; Khan et al, 2014 ).…”

Section: Resultsmentioning

confidence: 95%

“…Interestingly, both glycated SOD and ApoSOD were able to trigger intracellular ROS production. This effect might be associated to the loss of activity in the native SOD upon glycation and to the ability of AGEs products to induce oxidative stress (Jabeen et al, 2007 ; Wei et al, 2009 ; Kong et al, 2011 ; Khan et al, 2014 ). This observation is in line with previous reports showing that ROS production increases in AGEs-induced toxicity for several cell lines (Yamagishi and Takeuchi, 2004 ; Khan et al, 2013 ; Iannuzzi et al, 2016 ).…”

Section: Resultsmentioning

confidence: 99%

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Glycation in Demetalated Superoxide Dismutase 1 Prevents Amyloid Aggregation and Produces Cytotoxic Ages Adducts

Sirangelo

Vella

Irace

et al. 2016

Front. Mol. Biosci.

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Superoxide dismutase 1 (SOD1) has been implicated with familial amyotrophic lateral sclerosis (fALS) through accumulation of protein amyloid aggregates in motor neurons of patients. Amyloid aggregates and protein inclusions are a common pathological feature of many neurological disorders in which protein aggregation seems to be directly related to neurotoxicity. Although, extensive studies performed on the aggregation process of several amyloidogenic proteins in vitro allowed the identification of many physiological factors involved, the molecular mechanisms underlying the formation of amyloid aggregates in vivo and in pathological conditions are still poorly understood. Post-translational modifications are known to affect protein structure and function and, recently, much attention has been devoted to the role played by non-enzymatic glycation in stimulating amyloid aggregation and cellular toxicity. In particular, glycation seems to have a determining role both in sporadic and familial forms of ALS and SOD1 has been shown to be glycated in vivo The aim of this study was to investigate the role of glycation on the amyloid aggregation process of both wild-type SOD1 and its ALS-related mutant G93A. To this aim, the glycation kinetics of both native and demetalated SOD have been followed using two different glycating agents, i.e., D-ribose and methylglyoxal. The effect of glycation on the structure and the amyloid aggregation propensity of native and ApoSOD has been also investigated using a combination of biophysical and biochemical techniques. In addition, the effect of SOD glycated species on cellular toxicity and reactive oxygen species (ROS) production has been evaluated in different cellular models. The results provided by this study contribute to clarify the role of glycation in amyloid aggregation and suggest a direct implication of glycation in the pathology of fALS.

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Section: Resultsmentioning

confidence: 95%

Section: Resultsmentioning

confidence: 99%

Glycation in Demetalated Superoxide Dismutase 1 Prevents Amyloid Aggregation and Produces Cytotoxic Ages Adducts

Sirangelo

Vella

Irace

et al. 2016

Front. Mol. Biosci.

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“…These consequences of oxidative stress can further aggravate the complications associated with DM (60). A previous study indicated that SOD was inactivated by glycation (61). Another study reported that SOD activity was decreased in STZ-induced rat models of DM (62).…”

Section: Discussionmentioning

confidence: 99%

Effect of Azadirachta indica flower extract on functional recovery of sciatic nerve crush injury in rat models of DM

et al. 2018

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Chronic hyperglycemia causes nerves to be more susceptible to compression, which often occurs as a result of hyperglycemia-induced oxidative stress. Oxidative stress impairs nerve function and delays nerve recovery. Azadirachta indica, a herb from Thailand, possesses antioxidant and antidiabetic properties. The aim of the present study was therefore to investigate the effect of A. indica flower extract on the functional recovery of a sciatic nerve crush injury in rat models of diabetes mellitus (DM). Male Wistar rats were randomly assigned into seven groups including the control rats, rats with DM subjected to sham surgery and treated with vehicle, and rats with DM subjected to the crush surgery and treated with vehicle or A. indica flower extract at a dose of 250, 500 or 750 mg/kg animal body weight, or with vitamin C. DM was induced using a single intraperitoneal injection of streptozotocin (55 mg/kg animal body weight). Rats subjected to a sciatic nerve crush injury or sham surgery were orally treated with either vehicle, A. indica flower extract or vitamin C for 21 days. Functional recovery was assessed every 3 days using a walking track analysis, foot withdrawal reflex test and rotarod test. At the end of the study, the rats were sacrificed and their left sciatic nerves were harvested in order to determine malondialdehyde levels, superoxide dismutase activity and axon density. The treatment with A. indica flower extract significantly improved functional recovery, especially motor and sensory functions. The extract significantly decreased malondialdehyde levels, and increased superoxide dismutase activity and axon density. The results of the current study indicate that the mechanism underlying the enhanced functional recovery of the sciatic nerve following treatment with A. indica flower extract may be associated with an antioxidative effect. However, further studies are required to confirm the current results.

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“…The levels of GO-derived modifications such as N ε -(carboxymethyl)lysine (CML) and N δ -(5-hydro-4-imidazolon-2-yl) (G-H1) have been shown to correlate with diabetic complications suggesting their potential contribution to pathogenesis (19). The mechanisms of such contribution are still unknown but several studies demonstrated the detrimental impact of GO-derived modifications on function of proteins involved in antioxidant defenses, neurodegenerative disorders, and cell-matrix interactions (20–22). …”

Section: Go-derived Ages and Their Impact On Protein Structure And Fumentioning

confidence: 99%

Site-specific AGE modifications in the extracellular matrix: a role for glyoxal in protein damage in diabetes

Voziyan

Brown

Chetyrkin

et al. 2014

Clinical Chemistry and Laboratory Medicine

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Non-enzymatic modification of proteins in hyperglycemia is a major proposed mechanism of diabetic complications. Specifically, advanced glycation end products (AGEs) derived from hyperglycemia-induced reactive carbonyl species (RCS) can have pathogenic consequences when they target functionally critical protein residues. Modification of a small number of these critical residues, often undetectable by the methodologies relying on measurements of total AGE levels, can cause significant functional damage. Therefore, detection of specific sites of protein damage in diabetes is central to understanding molecular basis of diabetic complications and for identification of biomarkers which are mechanistically linked to the disease. The current paradigm of RCS-derived protein damage places the major focus on methylglyoxal (MGO), an intermediate of cellular glycolysis. We propose that glyoxal (GO) is a major contributor to extracellular matrix (ECM) damage in diabetes. Here, we review the current knowledge and provide new data about GO-derived site-specific ECM modification in experimental diabetes.

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Inactivation and modification of superoxide dismutase by glyoxal: Prevention by antibodies

Cited by 16 publications

References 53 publications

Glycation in Demetalated Superoxide Dismutase 1 Prevents Amyloid Aggregation and Produces Cytotoxic Ages Adducts

Glycation in Demetalated Superoxide Dismutase 1 Prevents Amyloid Aggregation and Produces Cytotoxic Ages Adducts

Effect of Azadirachta indica flower extract on functional recovery of sciatic nerve crush injury in rat models of DM

Site-specific AGE modifications in the extracellular matrix: a role for glyoxal in protein damage in diabetes

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