caa a22 4500 397557167 CHVBK 20180308164806.0 cr unu---uuuuu 161202e199607 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021383 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021383 An Arginine-213 to Glycine Mutation in Human Extracellular-Superoxide Dismutase Reduces Susceptibility to Trypsin-Like Proteinases [Elektronische Daten] [Tetsuo Adachi, Naoaki Morihara, Naoya Yamazaki, Harutaka Yamada, Arao Futenina, Katsumi Kato, Kazuyuki Hirano] Molecular genetic studies of extracellular-superoxide dismutase (EC-SOD) have shown that individuals with high serum EC-SOD content have a single base substitution generating the exchange of glycine for arginine-213 (R213G) in the heparin-binding domain of this enzyme [Sandström J. et al. (1994) J. Biol. Chem. 269, 19163-19166], which causes the impairment of its binding ability to endothelial cell surface [Adachi T. et al. (1996) Biochem. J. 313, 235-239]. Serum EC-SOD in healthy individuals without the above mutation is heterogeneous with regard to heparin affinity and consists of five fractions, forms (I) to (V), of which (IV) and (V) are the main fractions with high affinity for heparin [AdaChi T. et al. (1995) J. Biochem. 117, 586-590], whereas the major fraction in hemodialysis patients was serum EC-SOD form (I), which is thought to be the proteolytic truncated form. On the other hand, serum EC-SOD in both healthy individuals and hemodialysis patients with the R213G mutation consisted mainly of the high heparin-affinity type. This observation suggests that the susceptibility of EC-SOD to protelnases is reduced by the R213G mutation. The affinity of normal EC-SOD (n-EC-SOD) for heparin decreased by the treatment with trypsin, accompanied by a reduction in the molecular mass. The IC50 of trypsin for the heparin affinity of R213G mutant EC-SOD (m-EC-SOD) was 0.15 μg/ml, fivefold that for n-EC-SOD. Heparin affinity of n-EC-SOD was again more susceptible to neutrophils than that of m-EC-SOD. These results suggested that m-EC-SOD is more resistant to trypsin and neutrophil-release trypsin-like protelnases than n-EC SOD, which causes the heparin affinity of serum EC-SOD to differ in individuals with and without the R213G mutation. © 1996 BY THE JOURNAL OF BIOCHEMISTRY Regular Papers nationallicence extracellular-superoxide dismutase nationallicence hemodialysis patient nationallicence heparin nationallicence neutrophil nationallicence trypsin nationallicence Adachi Tetsuo Department of Pharmaceutics, Gifu Pharmaceutical University Gifu 502 aut Morihara Naoaki Department of Pharmaceutics, Gifu Pharmaceutical University Gifu 502 aut Yamazaki Naoya Department of Pharmaceutics, Gifu Pharmaceutical University Gifu 502 aut Yamada Harutaka First Department of Internal Medicine, Aichi Medical University Aichi 480-11 aut Futenina Arao First Department of Internal Medicine, Aichi Medical University Aichi 480-11 aut Kato Katsumi First Department of Internal Medicine, Aichi Medical University Aichi 480-11 aut Hirano Kazuyuki Department of Pharmaceutics, Gifu Pharmaceutical University Gifu 502 aut The Journal of Biochemistry Oxford University Press 120/1(1996-07), 184-188 0021-924X 120:1<184 1996 120 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021383 text/html Onlinezugriff via DOI 1 other jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021383 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Adachi Tetsuo Department of Pharmaceutics, Gifu Pharmaceutical University Gifu 502 aut NATIONALLICENCE 700 1- Morihara Naoaki Department of Pharmaceutics, Gifu Pharmaceutical University Gifu 502 aut NATIONALLICENCE 700 1- Yamazaki Naoya Department of Pharmaceutics, Gifu Pharmaceutical University Gifu 502 aut NATIONALLICENCE 700 1- Yamada Harutaka First Department of Internal Medicine, Aichi Medical University Aichi 480-11 aut NATIONALLICENCE 700 1- Futenina Arao First Department of Internal Medicine, Aichi Medical University Aichi 480-11 aut NATIONALLICENCE 700 1- Kato Katsumi First Department of Internal Medicine, Aichi Medical University Aichi 480-11 aut NATIONALLICENCE 700 1- Hirano Kazuyuki Department of Pharmaceutics, Gifu Pharmaceutical University Gifu 502 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 120/1(1996-07), 184-188 0021-924X 120:1<184 1996 120 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford