\ ALS Research \ Misfolded SOD1 not a feature of sporadic ALS
Abnormal folding of superoxide dismutase 1 (SOD1) – a protein known to gain harmful properties from heritable gene mutations in familial ALS – does not appear to cause cases of familial ALS without SOD1 mutations or sporadic cases non-hereditary, researchers say.
Scientists in the laboratory of Janice Robertson, PhD, at the University of Toronto used a special antibody that recognizes misfolded SOD1 protein to investigate whether the characteristic clumps of the abnormal protein -- seen within dying motor neurons in spinal cord tissue from familial ALS patients with SOD1 mutations -- were also present in the cells of patients without such mutations. Misfolded SOD1 was detected in all of the mutant SOD1 familial cases but in none of the non-mutant SOD1 familial or sporadic cases, the researchers reported in the July issue of Annals of Neurology.
Other studies have suggested that normal SOD1 protein can become misfolded, and therefore functionally abnormal, without genetic mutations under stressful conditions known to occur in ALS.
While Robertson and her group admit that the antibody they used may not recognize all misfolded forms of SOD1, they suggest that their results identify differences between cases of ALS resulting from SOD1 mutations and other variants of the disease, and their results don’t support the hypothesis that misfolded SOD1 is common to all types of ALS.
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Misfolded SOD1 not a feature of sporadic ALS
By: Katie Moisse, PhDAbnormal folding of superoxide dismutase 1 (SOD1) – a protein known to gain harmful properties from heritable gene mutations in familial ALS – does not appear to cause cases of familial ALS without SOD1 mutations or sporadic cases non-hereditary, researchers say.
Scientists in the laboratory of Janice Robertson, PhD, at the University of Toronto used a special antibody that recognizes misfolded SOD1 protein to investigate whether the characteristic clumps of the abnormal protein -- seen within dying motor neurons in spinal cord tissue from familial ALS patients with SOD1 mutations -- were also present in the cells of patients without such mutations. Misfolded SOD1 was detected in all of the mutant SOD1 familial cases but in none of the non-mutant SOD1 familial or sporadic cases, the researchers reported in the July issue of Annals of Neurology.
Other studies have suggested that normal SOD1 protein can become misfolded, and therefore functionally abnormal, without genetic mutations under stressful conditions known to occur in ALS.
While Robertson and her group admit that the antibody they used may not recognize all misfolded forms of SOD1, they suggest that their results identify differences between cases of ALS resulting from SOD1 mutations and other variants of the disease, and their results don’t support the hypothesis that misfolded SOD1 is common to all types of ALS.
| Posted On: Thursday, January 07, 2010 Modified: Thursday, January 07, 2010 Category: ALS Research Posted By: |