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10-fold increase in human plasma extracellular superoxide dismutase content caused by a mutation in heparin-binding domain

SANDSTRÖM, J ; NILSSON, P ; KARLSSON, K ; MARKLUND, S. L

The Journal of biological chemistry, 1994-07, Vol.269 (29), p.19163-19166 [Periódico revisado por pares]

Bethesda, MD: American Society for Biochemistry and Molecular Biology

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  • Título:
    10-fold increase in human plasma extracellular superoxide dismutase content caused by a mutation in heparin-binding domain
  • Autor: SANDSTRÖM, J ; NILSSON, P ; KARLSSON, K ; MARKLUND, S. L
  • Assuntos: Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Base Sequence ; Biological and medical sciences ; Cell Compartmentation ; Enzymes and enzyme inhibitors ; Extracellular Space - enzymology ; Fundamental and applied biological sciences. Psychology ; Heparin - metabolism ; Humans ; Molecular Sequence Data ; Mutation ; Oxidoreductases ; Protein Binding ; Superoxide Dismutase - blood ; Superoxide Dismutase - chemistry
  • É parte de: The Journal of biological chemistry, 1994-07, Vol.269 (29), p.19163-19166
  • Notas: ObjectType-Article-2
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  • Descrição: Extracellular superoxide dismutase (EC-SOD) is a secretory SOD isoenzyme. 99% of EC-SOD is anchored to heparan sulfate proteoglycans in the tissue interstitium, and 1% is located in the vasculature in equilibrium between the plasma and the endothelium. Analysis of EC-SOD in plasma samples from 504 random blood donors revealed a common (2.2%) phenotypic variant displaying 10-fold increased plasma EC-SOD content. The EC-SOD in the plasma of these individuals, collected both before and after intravenous injection of heparin, displayed a reduced heparin affinity when compared with samples from normal individuals. The specific enzymatic activity was the same as that of normal enzyme. Nucleotide sequence analyses of two of the affected subjects revealed a nucleotide exchange resulting in a substitution of Arg-213 by Gly. The substitution is located in the center of the carboxyl-terminal cluster of positively charged amino acid residues, which defines the heparin-binding domain. Polymerase chain reaction-single-strand conformational polymorphism and allele-specific polymerase chain reaction showed that all 11 affected individuals are heterozygous, carrying the same single-base mutation. Recombinant EC-SOD containing this mutation had a reduced heparin affinity similar to that of EC-SOD C from variant persons. The high plasma activity can be explained by an accelerated release from the tissue interstitium heparan sulfate to the vasculature and should thus be accompanied by significantly reduced tissue EC-SOD activities.
  • Editor: Bethesda, MD: American Society for Biochemistry and Molecular Biology
  • Idioma: Inglês
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  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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