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Expression of a Cu,Zn superoxide dismutase typical of familial amyotrophic lateral sclerosis induces mitochondrial alteration and increase of cytosolic Ca 2+ concentration in transfected neuroblastoma SH‐SY5Y cells
Author(s) -
Maria Teresa Carrı̀,
Alberto Ferri,
Andrea Battistoni,
Laila Famhy,
Roberta Gabbianelli,
Fabrizio Poccia,
Giuseppe Rotilio
Publication year - 1997
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01051-x
Subject(s) - superoxide dismutase , sh sy5y , cytosol , amyotrophic lateral sclerosis , microbiology and biotechnology , transfection , cell culture , dismutase , mitochondrion , chemistry , neuroblastoma , biology , biochemistry , enzyme , medicine , disease , genetics
We have set up a model system for familial amyotrophic lateral sclerosis (FALS) by transfecting human neuroblastoma cell line SH‐SY5Y with plasmids directing constitutive expression of either wild‐type human Cu,Zn superoxide dismutase (Cu,ZnSOD) or a mutant of this enzyme (G93A) associated with FALS. We have tested mitochondrial function and determined cytosolic Ca 2+ concentration in control cells (untransfected) and in cells expressing either wild‐type Cu,ZnSOD or G93A. We report that G93A induces a significant loss of mitochondrial membrane potential, an increased sensitivity toward valinomycin and a parallel increase in cytosolic Ca 2+ concentration. The above phenomena are not related to total Cu,ZnSOD content and activity in the cell.