Article
Glycation proceeds faster in mutated Cu, Zn-superoxide dismutases related to familial amyotrophic lateral sclerosis.
FASEB journal : official publication of the Federation of American Societies for Experimental Biology - 1 May 2003
Takamiya Rina, Takahashi Motoko, Myint Theingi, Park Yong Seek, Miyazawa Nobuko, Endo Takeshi, Fujiwara Noriko, Sakiyama Haruhiko, Misonou Yoshiko, Miyamoto Yasuhide, Fujii Junichi, Taniguchi Naoyuki
Abstract excerpt
Amyotrophic lateral sclerosis (ALS) involves the progressive degeneration of motor neurons in the spinal cord and motor cortex. It has been shown that 15-20% of patients with familial ALS (FALS) have defects in the Sod1 gene that encodes Cu, Zn-superoxide dismutase (SOD). To elucidate the pathological role of mutated Cu, Zn-SODs in FALS, the susceptibility of mutants to glycation was examined. Mutated Cu, Zn-SODs...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.
