Linked Life Data

7815961

Source:http://linkedlifedata.com/resource/pubmed/id/7815961

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1995-2-6
pubmed:abstractText
The beta-thymosins are a family of < 5kDa (MW), mostly acidic, proteins which were originally defined in the immune system. Recently, specific members of this family of cytoplasmic polypeptides, namely beta-4 and beta-10, were shown to bind monomeric G-actin both in vitro and in vivo. Whilst many aspects of programmed cell death or 'apoptosis' remain to be defined, the Ca2+/Mg(2+)-dependent endonuclease, DNase I does feature in this process. Monomeric G-actin binds to and inhibits the DNA-degrading activity of DNase I. Given that the intracellular abundance of thymosins beta-4 and beta-10 is related to cell division and differentiation and that anticancer/morphogenic agents such as retinoic acid (RA) and cyclic AMP modulate expression of their respective genes, it is possible that these G-actin sequestering proteins play significant roles in apoptosis perhaps mediated via DNase I.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0306-9877
pubmed:author
pubmed:issnType
Print
pubmed:volume
43
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
125-31
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Molecular interactions between G-actin, DNase I and the beta-thymosins in apoptosis: a hypothesis.
pubmed:affiliation
Department of Pharmacology, University of Cambridge, UK.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.