Linked Life Data

8485230

Source:http://linkedlifedata.com/resource/pubmed/id/8485230

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1993-6-9
pubmed:abstractText
The following proteins have been identified in mammalian lung and endothelium, using [32P]ADP-ribosylation by bacterial ADP-ribosyltransferase, immuno- and [alpha-32P]GTP-blottings: 41 kDa Gi1 alpha, 40 kDa Gi2 alpha, 41 kDa Gi3 alpha, 40 kDa and 45 kDa subunits of GS alpha, 36 kDa beta 1 and 35 kDa beta 2 subunits of signal-transmitting GTP-binding proteins (G-proteins), the 19-26 kDa low molecular weight GTP-binding proteins (SMG-proteins) ras, rho, rac, G25K (Gp), as well as ARF and SMG proteins binding with a high affinity to [alpha-32P]GTP. These G- and SMG-proteins are contained in various proportions in membrane and cytosol fractions of lung and endothelium cells. Subunits Gi2 alpha and GS alpha (but not beta 1 or SMG-proteins) my partially (approximately 1%) dissociate from the membrane by the action of the GTP analogs GTP[S] or Gpp(NH)p in the presence of magnesium ions. Extraction with low ionic strength buffer solutions in the presence of EDTA is accompanied by the release of G-actin sensitive to whooping cough toxin Gi2 alpha and beta i subunits. The functionally coupled into a alpha beta gamma heterodimer Gi-protein subunits (predominantly Gi2 alpha and beta i) present in the cytosol fraction as well as the SMG-proteins revealed by [alpha-32P]GTP-blotting (but not the SMG-proteins sensitive to the botulinic C3 exoenzyme, rho/rac, or ARF, may interact with F-actin. Approximately 20% of these proteins are associated with the Triton X-100 insoluble (cytoskeletal) fraction of the endothelium. A conclusion is drawn that interactions of G- and SMG-proteins with actin filaments may be the reason for the formation of "multidisperse" structure in a cell.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0320-9725
pubmed:author
pubmed:issnType
Print
pubmed:volume
58
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
438-55
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
[Signal-conducting and low molecular weight GTP-binding proteins from the lung and endothelium: localization in membranes and cytosol, interaction with F-actin].
pubmed:publicationType
Journal Article, English Abstract