Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2000-9-19
pubmed:abstractText
Hirano bodies are eosinophilic rod-like inclusions that are found predominantly in neuronal processes in the hippocampal CA1 sector with increasing age and are particularly numerous in Alzheimer's disease. They contain a variety of cytoskeletal epitopes, especially actin and actin-binding proteins. Actin cleavage by cysteinyl aspartate-specific proteases (caspases) is a feature of apoptosis. Cleavage at aspartate 244 generates N-terminal 32 kDa and C-terminal 15 kDa actin fragments. This has led to the development of a rabbit polyclonal antibody specific for caspase-cleaved actin, directed to the last five C-terminal amino acids of the 32 kDa fragment of actin ('fractin'). Fractin immunohistochemistry was performed on hippocampal sections from Alzheimer's disease and control cases containing numerous Hirano bodies, in addition to immunolabelling with CM1 antiserum which recognizes activated caspase-3. The Hirano bodies showed strong diffuse fractin immunoreactivity. They did not label with CM1 antiserum, perhaps reflecting too low a level of activated caspase-3 for immunodetection, or involvement of a different member of the caspase family. The finding of fractin immunoreactivity of Hirano bodies suggests that caspase-like cleavage of actin may play a role in their formation and further supports caspase-like activity in neuronal processes, distinct from that associated with acute perikaryal apoptosis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0305-1846
pubmed:author
pubmed:issnType
Print
pubmed:volume
26
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
342-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2000
pubmed:articleTitle
Caspase-cleaved actin (fractin) immunolabelling of Hirano bodies.
pubmed:affiliation
Department of Pathology, Queen's University and Kingston General Hospital, Kingston, Ontario, Canada. rossiter@cliff.path.queensu.ca
pubmed:publicationType
Journal Article