Extracellular-Superoxide Dismutase Association with Cell Surface-Bound Sulfated Glucosaminoglycans
Part of the
Basic Life Sciences
book series (BLSC, volume 49)
Extracellular-superoxide dismutase (EC 188.8.131.52., abbreviation EC-SOD) is a tetrameric glycoprotein with an apparent subunit molecular weight of around 30 kDa.1 Like the CuZn SODs, EC-SOD contains one Cu and one Zn atom per subunit1 and is inhibited by cyanide, azide, and diethyldithiocar-bamate,2 and H2O2 is the product of the catalysed reaction.3 Still, despite the similarities, the amino acid compositions of human CuZn SOD and EC-SOD are clearly different,’ and no cross-reaction between polyclonal rabbit antibodies directed towards the enzymes have been observed.2 EC-SOD is the major SOD isoenzyme in extracellular fluids like plasma, lymph,4 and synovial fluid,5 but also occurs in tissues.6,7 The total plasma EC-SOD concentration varies greatly between species, whereas the tissue concentrations are more equal.7
KeywordsHeparan Sulfate Chondroitin Sulfate Dextran Sulfate Platelet Factor Human Blood Plasma
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, Human copper-containing superoxide dismutase of high molecular weight, Proc. Natl. Acad. Sci. USA
79; 7634 (1982).PubMedCrossRefGoogle Scholar
S. L. Marklund, Properties of extracellular-superoxide dismutase from human lung, Biochem
. J. 220; 269 (1984).PubMedGoogle Scholar
S. L. Marklund, Product of extracellular-superoxide dismutase catalysis, FEBS Lett
. 184; 237 (1985).PubMedCrossRefGoogle Scholar
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
R. M. Krauss, H. C. Windmüeler, and D. S. Fredrickson, Selective measurement of two different triglyceride lipase activities in rat post heparin plasma, J. Lipid. Res.
14;286 (1973).PubMedGoogle Scholar
R. Hansson, C. G. Holmberg, G. Tibbling, N. Tryding, A. Westling, and H. Wetterquist, Heparin-induced diamine oxidase increase in human blood plasma, Acta. Med. Scand
. 180;533 (1966).PubMedCrossRefGoogle Scholar
J. Dawes, R. C. Smith and, D. S. Pepper, The release, distribution, and clearance of human β-thromboglobulin and platelet factor 4, Tromb. Res
. 12;851 (1978).CrossRefGoogle Scholar
A. Robinson-White, S. B. Baylin, T. Olivecrona, and M. A. Beaven, Binding of diamine oxidase activity to rat and guinea pig microvascular endothelial cells, J. Clin. Invest
. 76;93 (1985).PubMedCrossRefGoogle Scholar
C. Busch, J. Dawes, D. S. Pepper and, Å. Wasteson, Binding of platelet factor 4 to cultured human umbilical vein endothelial cells, Tromb. Res.
19;129 (1980).CrossRefGoogle 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
© Plenum Press, New York 1988