Mouse alpha chains inhibit polymerization of hemoglobin induced by human beta S or beta S Antilles chains.
A murine model of sickle cell disease was tested by studying the polymerization of hybrid hemoglobin tetramers between alpha mouse and human beta S or beta S Antilles chains were prepared from Hb S Antilles, which was a new sickling hemoglobin inducing a sickle cell syndrome more severe than Hb S. The hybrid molecules did not polymerize in solution, indicating that the mouse alpha chains inhibited fiber formation. Consequently, a mouse model for sickle cell disease requires the transfer and expression of both alpha and beta S or beta S Antilles genes.
Rhoda
M D
MD
INSERM U.91, CNRS EA 607, Hôpital Henri Mondor, Créteil, France.
Domenget
C
C
Vidaud
M
M
Bardakdjian-Michau
J
J
Rouyer-Fessard
P
P
Rosa
J
J
Beuzard
Y
Y
D000595:Amino Acid Sequence; D000818:Animals; D006451:Hemoglobin, Sickle / Q000302:isolation & purification / Q000378:metabolism*; D006801:Humans; D046911:Macromolecular Substances; D051379:Mice; D010108:Oxyhemoglobins / Q000378:metabolism; D055503:Protein Multimerization; D013045:Species Specificity
D006451:Hemoglobin, Sickle; D046911:Macromolecular Substances; D010108:Oxyhemoglobins; C055657:hemoglobin S-Antilles