Linked Life Data

8387605

Source:http://linkedlifedata.com/resource/pubmed/id/8387605

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1993-6-4
pubmed:abstractText
The usual rate of actin polymerization is increased if one starts from actin nuclei. We have noticed that, using alpha-actinin crosslinked actin nuclei, the initial net elongation rate is further enhanced. Also initial net depolymerization rates of alpha-actinin crosslinked F-actin samples are higher than those of controls. These results should imply that alpha-actinin increases the filament end concentration of actin samples. The experiments with barbed and blocking substances (cytochalasin D and gelsolin-actin complex) confirmed such an increase. We have shown that: (1) alpha-actinin does not significantly influence actin polymerization over all; (2) alpha-actinin inhibits the recovery of the filament size in F-actin samples after sonication; and (3) the influence of alpha-actinin on actin filament end concentration is counteracted by tropomyosin. Therefore, we suggest that, upon filament shearing, alpha-actinin crosslinking inhibits the annealing of short actin polymers into longer filaments.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
230
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1151-8
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Alpha-actinin increases actin filament end concentration by inhibiting annealing.
pubmed:affiliation
University of Milan, Department of Biology, Italy.
pubmed:publicationType
Journal Article