Sickle hemoglobin disturbs normal coupling among erythrocyte O2 content, glycolysis, and antioxidant capacity-Reference-Cited by-同舟云学术

Sickle hemoglobin disturbs normal coupling among erythrocyte O2 content, glycolysis, and antioxidant capacity

Published:2013-02-28 Issue:9 Volume:121 Page:1651-1662
ISSN:0006-4971
Container-title:Blood
language:en
Short-container-title:

Author:

Rogers Stephen C.¹²,Ross Jerlinda G. C.¹³⁴,d'Avignon Andre⁵,Gibbons Lindsey B.¹²,Gazit Vered¹²,Hassan Mojibade N.¹²,McLaughlin Dylan¹²,Griffin Sherraine³⁴,Neumayr Tara¹,DeBaun Malcolm¹²,DeBaun Michael R.³⁴,Doctor Allan¹²

Affiliation:

1. Division of Critical Care Medicine, Department of Pediatrics, School of Medicine,

2. Department of Biochemistry and Molecular Biophysics, School of Medicine,

3. Division of Hematology and Oncology, Department of Pediatrics, School of Medicine,

4. Division of Genetics and Genomic Medicine, Department of Pediatrics, School of Medicine, and

5. Department of Chemistry, College of Arts and Sciences, Washington University, St Louis, MO

Abstract

Key PointsHb-conformation–dependent interaction with band 3 protein regulates glycolysis in RBCs. In hypoxia, HbS disrupts this system, disabling RBC antioxidant defense.

Publisher

American Society of Hematology

Subject

Cell Biology,Hematology,Immunology,Biochemistry

Link

http://ashpublications.org/blood/article-pdf/121/9/1651/1369328/zh800913001651.pdf

Reference46 articles.

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4. Accelerated autoxidation and heme loss due to instability of sickle hemoglobin.;Hebbel;Proc Natl Acad Sci U S A,1988

5. Interaction of sickle cell hemoglobin with erythrocyte membranes.;Shaklai;Proc Natl Acad Sci U S A,1981

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