Document Detail

Redox Reactions of Hemoglobin: Mechanisms of Toxicity and Control.
MedLine Citation:
PMID:  23330885     Owner:  NLM     Status:  Publisher    
In the last several years, significant work has been done studying hemoglobin (Hb) oxidative reactions and clearance mechanisms using both in vitro and in vivo model systems. One active research area involves the study of molecular chaperones and other proteins which are thought to mitigate the toxicity of acellular Hb. For example, the plasma protein haptoglobin (Hp) and the pre-erythroid protein Alpha-Hemoglobin Stabilizing Protein (AHSP) bind to acellular Hb and alpha subunits of Hb, respectively, to reduce these adverse effects. Moreover, there has been significant work studying hemopexin (Hpx) and Alpha-1 Microglobulin (A1M), both of which are thought to be involved with hemin degradation. These studies have coincided with the timely publication of the first crystal structure of the Hb-Hp complex. In constructing this Forum Issue, we have invited a number of researchers in the area of Hb and myoglobin (Mb) redox biochemistry, as well as those who have contributed fundamentally to our knowledge of Hp function. Our goal has been to update this critically important research area because we believe it will ultimately impact the practice of transfusion medicine in a number of important ways.
Todd Mollan; Abdu I Alayash
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-20
Journal Detail:
Title:  Antioxidants & redox signaling     Volume:  -     ISSN:  1557-7716     ISO Abbreviation:  Antioxid. Redox Signal.     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-21     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  100888899     Medline TA:  Antioxid Redox Signal     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
US Food and Drug Administration, Division of Hematology, Center for Biologics Evaluation and Research, Bethesda, Maryland, United States;
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