Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-7-31
pubmed:abstractText
A large body of biochemical and morphological evidence suggests that actin polymerizes in response to various stimuli which activate platelets. Previous work has shown the presence in platelets of gelsolin, a Ca(2+)-dependent regulator of actin filament length. This present work demonstrates that human platelets contain scinderin, another Ca(2+)-dependent actin filament-severing protein recently discovered in our laboratory. Extracts prepared from platelets were subjected to DNase-I-Sepharose 4B affinity chromatography. EGTA eluates from the affinity columns contained scinderin as demonstrated by mono and two-dimensional polyacrylamide gel electrophoresis and immunoblotting with scinderin antibodies. The concentration of scinderin in platelets was 75 fmol/mg total protein. This might represent 11% of the total actin filament-severing activity if both proteins are equally potent, on a molar basis, in severing actin filaments. Double staining immunocytochemical studies with antibodies against scinderin and rhodamine phalloidin, a probe for F-actin, also demonstrated the presence of scinderin in platelets. These findings suggest that scinderin may participate in the regulation of platelet actin networks.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0340-6245
pubmed:author
pubmed:issnType
Print
pubmed:day
3
pubmed:volume
67
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
248-51
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Human platelets contain scinderin, a Ca(2+)-dependent actin filament-severing protein.
pubmed:affiliation
Department of Pharmacology, Faculty of Medicine, University of Ottawa, Ontario, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't