Copper,zinc superoxide dismutase is primarily a cytosolic protein in human cells.
The intracellular localization of human copper,zinc superoxide dismutase (Cu,Zn-SOD; superoxide:superoxide oxidoreductase, EC 1.15.1.1) was evaluated by using EM immunocytochemistry and both isolated human cell lines and human tissues. Eight monoclonal antibodies raised against either native or recombinant human Cu,Zn-SOD and two polyclonal antibodies raised against either native or recombinant human Cu,Zn-SOD were used. Fixation with 2% paraformaldehyde/0.2% glutaraldehyde was found necessary to preserve normal distribution of the protein. Monoclonal antibodies were less effective than polyclonal antibodies in recognizing the antigen after adequate fixation of tissue. Cu,Zn-SOD was found widely distributed in the cell cytosol and in the cell nucleus, consistent with it being a soluble cytosolic protein. Mitochondria and secretory compartments did not label for this protein. In human cells, peroxisomes showed a labeling density slightly less than that of cytoplasm.
Crapo
J D
JD
Department of Medicine, Duke University Medical Center, Durham, NC 27710.
Oury
T
T
Rabouille
C
C
Slot
J W
JW
Chang
L Y
LY
D000368:Aged; D000818:Animals; D000906:Antibodies; D002277:Carcinoma / Q000201:enzymology* / Q000648:ultrastructure; D006528:Carcinoma, Hepatocellular; D003600:Cytosol / Q000201:enzymology / Q000648:ultrastructure; D005347:Fibroblasts / Q000201:enzymology / Q000648:ultrastructure; D006801:Humans; D007527:Isoenzymes / Q000032:analysis* / Q000276:immunology; D008113:Liver Neoplasms; D008168:Lung / Q000201:enzymology* / Q000648:ultrastructure; D008175:Lung Neoplasms / Q000201:enzymology* / Q000648:ultrastructure; D008297:Male; D016253:Microscopy, Immunoelectron; D051381:Rats; D011994:Recombinant Proteins / Q000276:immunology; D013482:Superoxide Dismutase / Q000032:analysis* / Q000276:immunology; D014407:Tumor Cells, Cultured
D000906:Antibodies; D007527:Isoenzymes; D011994:Recombinant Proteins; D013482:Superoxide Dismutase