Sequence of Complementary DNA Encoding Human Extracellular-Superoxide Dismutase and Production of Recombinant Enzyme
Part of the
Basic Life Sciences
book series (BLSC, volume 49)
Extracellular-superoxide dismutase (EC-SOD; 188.8.131.52,) is the major SOD isoenzyme in extra- cellular fluids such as plasma, lymph1 and synovial fluid2 but also occurs in tissues.3,4 EC-SOD is heterogenous with regard to binding to Heparin-Sepharose and can be separated into three fractions: A, without affinity; B with weak affinity; and C, with relatively high affinity.5 Most EC-SOD in the vascular system apparently is bound to endothelial cell surfaces.6 Membrane-bound heparan sulfate is the likely receptor for the enzyme, and EC-SOD fraction C is the form that binds.6 EC-SOD is a tetrameric glycoprotein with an apparent subunit molecular weight of around 3 0 kDa.5 Like the CuZn SOD’s, EC-SOD contains one Cu and one Zn atom per subunit.5 Still, despite the similarities, the amino acid compositions of human CuZn SOD and EC-SOD are clearly different,5 and no cross-reaction between polyclonal rabbit antibodies directed towards the enzymes have been observed.7
KeywordsHeparan Sulfate Endothelial Cell Surface Synovial Fluid2 Terminal Amino Acid Sequence CuZn SODs
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.
S. L. Marklund, E. Holme, and L. Hellner, Superoxide dismutase in extracellular fluids, Clin. Chim. Acta.
126:41 (1982).PubMedCrossRefGoogle Scholar
S. L. Marklund, A. Bjelle, and L. G. Elmqvist, Superoxide dismutase isoenzymes of the synovial fluid in rheumatoid arthritis and in reactive arthritides, Ann. Rheum. Dis
. 45:847 (1986).PubMedCrossRefGoogle Scholar
S. L. Marklund, Extracellular-superoxide dismutase in human tissues and human cell lines, J. Clin. Invest.
74:1398 (1984).PubMedCrossRefGoogle Scholar
S. L. Marklund, Extracellular-superoxide dismutase and other superoxide dismutase isoenzymes in tissues from nine mammalian species, Biochem. J.
222:649 (1984).PubMedGoogle Scholar
S. L. Marklund, Human copper-containing superoxide dismutase of high molecular weight, Proc. Natl. Acad
. USA:79, 7634 (1982).PubMedCrossRefGoogle Scholar
K. Karlsson and S. L. Marklund, Heparin-induced release of extracellular-superoxide dismutase to human blood plasma, Biochem. J.
242:55 (1987).PubMedGoogle Scholar
S. L. Marklund, Properties of extracellular-superoxide dismutase from human lung, Biochem. J.
220:269 (1984).PubMedGoogle Scholar
K. Hjalmarsson, S. L. Marklund, A. Engström, and T. Edlund, Isolation and sequence of complementary DNA encoding human extracellular-superoxide dismutase, Proc. Natl. Acad. Sci. USA
84:6340 (1987).PubMedCrossRefGoogle Scholar
H. M. Steinman, Bacteriocuprein superoxide dismutase of Photobacterium leiognathi; isolation and sequence of the gene and evidence for a precursor form, J. Biol. Chem.
262:1882 (1987).PubMedGoogle Scholar
J. A. Tainer, E. D. Getzoff, K. M. Beem, J. S. Richardson, and D. C. Richardson, Determination and analysis of the 2 A structure of copper, zinc superoxide dismutase, J. Mol. Biol.
160:181 (1982).PubMedCrossRefGoogle Scholar
C. L. Borders, J. E. Saunders, D. M. Blech, and I. Fridovich, Essentiality of the active-site arginine residue for the normal catalytic activity of Cu, Zn superoxide dismutase, Biochem. J.
230:771 (1985).PubMedGoogle Scholar
L. Tibell, K. Hjalmarsson, T. Edlund, G. Skogman, Å. Engström, and S. L. Marklund, Expression of human extracellular-superoxide dismutase in Chinese hamster ovary cells and characterization of the product, Proc. Natl. Acad. Sci. USA
84:6634 (1987).PubMedCrossRefGoogle Scholar
© Plenum Press, New York 1988