Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2003-2-18
pubmed:abstractText
Subcellular fractionation of human neutrophils on linear sucrose density gradients was utilized to test the hypothesis that priming regulates the subcellular and sub-plasma membrane distribution of neutrophil G-protein subunits, G(ialpha2) and G(ialpha3), N-formyl peptide receptor, Lyn kinase and phospholipase C(beta2). G(ialpha2), but not G(ialpha3), moved from a lighter to a higher density plasma membrane fraction. Unoccupied N-formyl peptide receptors were found throughout the plasma membrane fractions and this distribution did not change with priming. In unprimed cells G(ialpha2) and its effector, phospholipase C(beta2), were segregated in different membrane compartments; priming caused G(ialpha2) to move to the compartment in which phospholipase C(beta2) resided. Thus, an important component of the mechanism of priming may involve regulation of the location of G-proteins and effector molecules in plasma membrane compartments where their abilities to couple may be enhanced.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Alkaline Phosphatase, http://linkedlifedata.com/resource/pubmed/chemical/GNAI3 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Protein alpha Subunit..., http://linkedlifedata.com/resource/pubmed/chemical/GTP-Binding Protein alpha..., http://linkedlifedata.com/resource/pubmed/chemical/Heterotrimeric GTP-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes, http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides, http://linkedlifedata.com/resource/pubmed/chemical/NADPH Oxidase, http://linkedlifedata.com/resource/pubmed/chemical/PLCB2 protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Phospholipase C beta, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Formyl Peptide, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Immunologic, http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Peptide, http://linkedlifedata.com/resource/pubmed/chemical/Tumor Necrosis Factor-alpha, http://linkedlifedata.com/resource/pubmed/chemical/Type C Phospholipases, http://linkedlifedata.com/resource/pubmed/chemical/lyn protein-tyrosine kinase, http://linkedlifedata.com/resource/pubmed/chemical/src-Family Kinases
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0006-291X
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
301
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
862-72
pubmed:dateRevised
2011-11-2
pubmed:meshHeading
pubmed-meshheading:12589792-Alkaline Phosphatase, pubmed-meshheading:12589792-Cell Compartmentation, pubmed-meshheading:12589792-Cell Membrane, pubmed-meshheading:12589792-Cytosol, pubmed-meshheading:12589792-GTP-Binding Protein alpha Subunit, Gi2, pubmed-meshheading:12589792-GTP-Binding Protein alpha Subunits, Gi-Go, pubmed-meshheading:12589792-Heterotrimeric GTP-Binding Proteins, pubmed-meshheading:12589792-Isoenzymes, pubmed-meshheading:12589792-Lipopolysaccharides, pubmed-meshheading:12589792-Membrane Microdomains, pubmed-meshheading:12589792-Models, Biological, pubmed-meshheading:12589792-NADPH Oxidase, pubmed-meshheading:12589792-Neutrophils, pubmed-meshheading:12589792-Phospholipase C beta, pubmed-meshheading:12589792-Proto-Oncogene Proteins, pubmed-meshheading:12589792-Receptors, Formyl Peptide, pubmed-meshheading:12589792-Receptors, Immunologic, pubmed-meshheading:12589792-Receptors, Peptide, pubmed-meshheading:12589792-Signal Transduction, pubmed-meshheading:12589792-Tumor Necrosis Factor-alpha, pubmed-meshheading:12589792-Type C Phospholipases, pubmed-meshheading:12589792-src-Family Kinases
pubmed:year
2003
pubmed:articleTitle
Priming-induced localization of G(ialpha2) in high density membrane microdomains.
pubmed:affiliation
Department of Surgery, University of Michigan, Ann Arbor, MI 48105, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S., Research Support, Non-U.S. Gov't