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JCI table of contents, November 15 2004

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ACCOMPANYING COMMENTARY:
TITLE: RIP-ed and ready to dance: new mechanisms for polycystin-1 signaling

AUTHOR CONTACT: Lisa M. Guay-Woodford
Department of Medicine, Genetics, and Pediatrics, University of Alabama at Birmingham, Atlanta, USA.
Phone: 205-934-7308; Fax: 205-975-5689; E-mail: lgw@uab.edu.

View the PDF of this commentary at: https://www.the-jci.org/press/23544.pdf

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Hobbling free of alpha-hemoglobin in beta-thalassemia

Hemoglobin carries oxygen throughout the body and is comprised of four subunits: two alpha-hemoblobins (alpha-Hb) and two beta-hemoglobins (beta-Hb). Hempoglobin synthesis is carefully coordinated to avoid accumulation of free alpha-Hb or beta-Hb subunits, which can be toxic. In the disease beta-thalassemia, characterized by severe anemia, loss of beta-Hb leaves alpha-Hb subunits unpaired and alpha-Hb production of toxic oxygen molecules reduces the lifespan of circulating red blood cells.

In the November 15 issue of the Journal of Clinical Investigation, Mitchell Weiss and colleagues investigated the role of the alpha-Hbstabilizing protein (AHSP) in limiting the damage caused by free alpha-Hb. The authors developed mice deficient in AHSP and found that their red blood cells were short-lived due to increased levels of toxic reactive oxygen species and free Hb. Providing purified AHSP in culture inhibited toxic alpha-Hb oxygen production. The study indicates an essential role for AHSP during Hb production and red blood cell production. The authors propose that developing means to alter human AHSP expression could reduce the severity of beta-thalassemia.
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Contact: Brooke Grindlinger
press_releases@the-jci.org
212-342-9006
Journal of Clinical Investigation
15-Nov-2004


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