TY - JOUR
T1 - Calcium-dependent human erythrocyte cytoskeleton stability analysis through atomic force microscopy
AU - Liu, Fei
AU - Mizukami, Hiroshi
AU - Sarnaik, Sharada
AU - Ostafin, Agnes
PY - 2005/5
Y1 - 2005/5
N2 - Erythrocytes affected by age and diseases such as sickle cell anemia, hypertension, diabetes, etc., exhibit abnormally high intracellular Ca 2+ ion levels, and appear to have altered cytoskeleton properties. It has been proposed that extra binding of Ca2+ to membrane-associated calmodulin attenuates the spectrin-ankyrin-Band 3 tether of the cytoskeleton to the cytoplasmic membrane and might change the cytoskeleton structure. Due to the close apposition of the network, direct observation of such a structural change in vivo is restricted. In this study, atomic force microscopy and quantitative image analysis were applied to investigate the structural change of young healthy erythrocyte cytoskeletons upon extra Ca2+ binding to the cytoplasmic membrane in vitro. The results show that extra Ca2+ binding increased the cytoskeleton rigidity and prevented spectrin aggregation during sample preparation. The cytoskeleton morphology observed in Ca 2+-incubated healthy young cell were similar to the glutaraldehyde-fixed healthy young cells.
AB - Erythrocytes affected by age and diseases such as sickle cell anemia, hypertension, diabetes, etc., exhibit abnormally high intracellular Ca 2+ ion levels, and appear to have altered cytoskeleton properties. It has been proposed that extra binding of Ca2+ to membrane-associated calmodulin attenuates the spectrin-ankyrin-Band 3 tether of the cytoskeleton to the cytoplasmic membrane and might change the cytoskeleton structure. Due to the close apposition of the network, direct observation of such a structural change in vivo is restricted. In this study, atomic force microscopy and quantitative image analysis were applied to investigate the structural change of young healthy erythrocyte cytoskeletons upon extra Ca2+ binding to the cytoplasmic membrane in vitro. The results show that extra Ca2+ binding increased the cytoskeleton rigidity and prevented spectrin aggregation during sample preparation. The cytoskeleton morphology observed in Ca 2+-incubated healthy young cell were similar to the glutaraldehyde-fixed healthy young cells.
KW - Atomic force microscopy
KW - Calcium
KW - Calmodulin
KW - Cytoskeleton
KW - Erythrocyte
UR - http://www.scopus.com/inward/record.url?scp=18144375945&partnerID=8YFLogxK
U2 - 10.1016/j.jsb.2005.02.001
DO - 10.1016/j.jsb.2005.02.001
M3 - Article
C2 - 15866743
AN - SCOPUS:18144375945
VL - 150
SP - 200
EP - 210
JO - Journal of Structural Biology
JF - Journal of Structural Biology
SN - 1047-8477
IS - 2
ER -