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25 - Dyshemoglobinemias

from SECTION SIX - OTHER CLINICALLY IMPORTANT DISORDERS OF HEMOGLOBIN

Published online by Cambridge University Press:  03 May 2010

Martin H. Steinberg ,
Bernard G. Forget ,
Douglas R. Higgs  and
David J. Weatherall
By
Neeraj Agarwal ,
Ronald L. Nagel  and
Josef T. Prchal
Martin H. Steinberg
Affiliation:
Boston University
Bernard G. Forget
Affiliation:
Yale University, Connecticut
Douglas R. Higgs
Affiliation:
MRC Institute of Molecular Medicine, University of Oxford
David J. Weatherall
Affiliation:
Albert Einstein College of Medicine, New York
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Summary

Hemoglobin can bind gases other than oxygen (O2). These include carbon monoxide (CO) and nitric oxide (NO). Carboxyhemoglobin (COHb) precludes normal O2 transport and is toxic. Nitrosohemoglobin has critical physiological functions discussed in Chapter 10. Normal hemoglobin can be oxidized to methemoglobin and sulfhemoglobin by exogenous agents and these hemoglobin forms can also be found as a result of germline mutations. In aggregate, these modified hemoglobins, referred as dyshemoglobinemias, are the basis of a group of acquired and genetic disorders that are rare but can have serious clinical implications.

METHEMOGLOBINEMIA

Methemoglobin is formed when the iron of the heme group is oxidized or converted from the ferrous (Fe2+) to the ferric (Fe3+) state. The ferric hemes of methemoglobin are unable to reversibly bind O2. In addition, the presence of ferric heme increases the O2 affinity of the accompanying ferrous hemes in the hemoglobin tetramer. This leads to a left shift in the hemoglobin–O2 dissociation curve, which impairs tissue delivery of O2. Normally, methemoglobin is generated and then reduced physiologically to maintain a very low steady-state blood methemoglobin level of 1% or less of the total hemoglobin. The half-life of methemoglobin is approximately 1 hour if the reductase mechanism is normal. Methemoglobinemia occurs when there is imbalance between methemoglobin production and methemoglobin reduction. Methemoglobinemia can have both inherited and acquired causes; hemoglobin oxidation has been recently reviewed.

Pathophysiology of Methemoglobinemia

Production of Methemoglobin. O2 binds the ferrous form of iron present in hemoglobin to form oxyhemoglobin.

Type
Chapter
Information
Disorders of Hemoglobin
Genetics, Pathophysiology, and Clinical Management
 , pp. 607 - 622
Publisher: Cambridge University Press
Print publication year: 2009

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