Linked Life Data

15866743

Source:http://linkedlifedata.com/resource/pubmed/id/15866743

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2005-5-3
pubmed:abstractText
Erythrocytes affected by age and diseases such as sickle cell anemia, hypertension, diabetes, etc., exhibit abnormally high intracellular Ca2+ 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 Ca2+ -incubated healthy young cell were similar to the glutaraldehyde-fixed healthy young cells.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1047-8477
pubmed:author
pubmed:issnType
Print
pubmed:volume
150
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
200-10
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Calcium-dependent human erythrocyte cytoskeleton stability analysis through atomic force microscopy.
pubmed:affiliation
Department of Chemical and Biomolecular Engineering, University of Notre Dame, Notre Dame, IN 46556, USA.
pubmed:publicationType
Journal Article