Linked Life Data

2116927

Source:http://linkedlifedata.com/resource/pubmed/id/2116927

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1990-9-18
pubmed:abstractText
Guanine nucleotide-binding regulatory proteins, or G proteins, mediate the interaction of agonist receptors on the platelet surface with phospholipase C and adenylyl cyclase. To better understand this process, we have used several approaches to identify which G proteins are present in platelets, normal human megakaryocytes, and human erythroleukemia (HEL) cells, a leukemic cell line with megakaryocytic features. Because platelet and HEL cell responses to thrombin are inhibited by pertussis toxin, we have focused upon the members of the Gi family, whose alpha subunits can be ADP-ribosylated by that toxin. Western blots with antisera specific for Gi alpha demonstrated the presence in both platelets and HEL cells of the three best-described forms of this protein: Gi alpha 1, Gi alpha 2, and Gi alpha 3. Based upon immunoprecipitation studies with [35S]-methionine-labeled HEL cells, their relative abundance appears to be Gi alpha 2 much greater than Gi alpha 3 greater than Gi alpha 1. A HEL cell cDNA library screened with the Gi alpha antisera produced clones encoding Gi alpha 2 and Gi alpha 3 that had sequences similar to those reported from other sources. Gi alpha-specific probes created from these cDNA clones confirmed the presence of mRNA encoding Gi alpha 2 and Gi alpha 3 in both platelets (by Northern blotting) and megakaryocytes (by in situ hybridization). Thus the pertussis toxin substrates that have previously been detected in platelets and HEL cells are shown to be members of the Gi alpha family, all of which are candidates for interaction with receptors for thrombin and other agonists.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0006-4971
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
76
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
721-30
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed-meshheading:2116927-Adenylate Cyclase Toxin, pubmed-meshheading:2116927-Amino Acid Sequence, pubmed-meshheading:2116927-Antibodies, pubmed-meshheading:2116927-Base Sequence, pubmed-meshheading:2116927-Blood Platelets, pubmed-meshheading:2116927-DNA, pubmed-meshheading:2116927-Electrophoresis, Gel, Two-Dimensional, pubmed-meshheading:2116927-GTP-Binding Proteins, pubmed-meshheading:2116927-Humans, pubmed-meshheading:2116927-Immunoblotting, pubmed-meshheading:2116927-Leukemia, Erythroblastic, Acute, pubmed-meshheading:2116927-Megakaryocytes, pubmed-meshheading:2116927-Molecular Sequence Data, pubmed-meshheading:2116927-Nucleic Acid Hybridization, pubmed-meshheading:2116927-Pertussis Toxin, pubmed-meshheading:2116927-Precipitin Tests, pubmed-meshheading:2116927-Virulence Factors, Bordetella
pubmed:year
1990
pubmed:articleTitle
Identification of the pertussis toxin-sensitive G proteins in platelets, megakaryocytes, and human erythroleukemia cells.
pubmed:affiliation
Department of Medicine, University of Pennsylvania, Philadelphia 19104.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't