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Background: Despite the genetic heterogeneity reported in familial ALS (FALS), SOD1 gene mutations are the most frequent cause of FALS, accounting for around 20% of familial cases (ALS1) and isolated sporadic cases. Mutant forms of SOD1 exhibit toxicity that promotes the death of motor neurons. It is well documented that FALS produces protein aggregates in the motor neurons of FALS patients, which have been found to be associated to mitochondria. Methods: In this study, we cloned the SOD1 gene, using reverse transcriptase-polymerase chain reaction (RT-PCR) method, from both a healthy control and a living 79 -year-old man with diagnosis of sporadic form of ALS who had shown unusual rapid progression of disease. RNA samples were available from lymphocytes of them. pET28a expression system and BL21 chemically competent Escherichia coli strain as host were used for protein expression. Results: DNA Sequencing data showed both heterozygosis C to G transition at nucleotide position 21 leading to a C6W changing at protein level and a deletion at nucleotides position 73 to 169 leading to complete deletion of exon two.

Keywords: Sporadic amyotrophic lateral sclerosis (SALS), Familial amyotrophic lateral sclerosis (FALS), Cu/Zn Superoxide dismutase 1 (SOD1), Exon deletion, Point mutation

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