Uncoupling of the spectrin-based skeleton from the lipid bilayer in sickled red cells.
The distribution of spectrin and band 3 in deoxygenated reversibly sickled cells was visualized by immunofluorescence and immunoelectron microscopy. Antibodies against band 3, the major lipid-associated transmembrane protein, labeled the entire cell body, including the entire length of the long protruding spicule, whereas antibodies against spectrin labeled only the cell body and the base region of the spicules. The results suggest that the formation of long spicules during sickling is associated with a continuous polymerization of hemoglobin S polymers, presumably through gaps in the spectrin-actin meshwork, and a subsequent uncoupling of the lipid bilayer from the submembrane skeleton.
Liu
S C
SC
Division of Hematology-Oncology, St. Elizabeth's Hospital, Tufts University School of Medicine, Boston, MA 02135.
Derick
L H
LH
Zhai
S
S
Palek
J
J
D000755:Anemia, Sickle Cell / Q000097:blood*; D001457:Anion Exchange Protein 1, Erythrocyte / Q000648:ultrastructure*; D004910:Erythrocyte Membrane / Q000648:ultrastructure*; D006451:Hemoglobin, Sickle / Q000648:ultrastructure; D006801:Humans; D008051:Lipid Bilayers; D008563:Membrane Lipids / Q000097:blood*; D008854:Microscopy, Electron; D008855:Microscopy, Electron, Scanning; D016253:Microscopy, Immunoelectron; D013049:Spectrin / Q000648:ultrastructure*
D001457:Anion Exchange Protein 1, Erythrocyte; D006451:Hemoglobin, Sickle; D008051:Lipid Bilayers; D008563:Membrane Lipids; D013049:Spectrin