Linked Life Data

7615058

Source:http://linkedlifedata.com/resource/pubmed/id/7615058

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-8-24
pubmed:abstractText
Reduced turn-over of tau by calpains is a possible mechanism to facilitate the incorporation into paired helical filaments (PHFs) in Alzheimer's disease. The present study shows that the differently phosphorylated fetal tau isoforms are all rapidly proteolysed to an equal extent by human brain m-calpain. This result argues against the hypothesis that this type of fetal phosphorylation is involved in reducing tau turn-over by calpain in Alzheimer's disease. Adult and fetal tau fragments in vitro generated by m-calpain, but not trypsin, cathepsin D or chymotrypsin resemble the post-mortem in situ degradation patterns, suggesting a possible role for calpains in tau metabolism in vivo. Tau incorporated into PHFs was considerably more resistant to proteolysis by calpain which can help to explain the persistence of these structures in Alzheimer's disease.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
10
pubmed:volume
368
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
10-4
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Differential sensitivity to proteolysis by brain calpain of adult human tau, fetal human tau and PHF-tau.
pubmed:affiliation
Laboratories for Molecular Neuroscience, McLean Hospital, Belmont, MA 02178, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.