Linked Life Data

16267829

Source:http://linkedlifedata.com/resource/pubmed/id/16267829

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2005-12-5
pubmed:abstractText
Binding of integrins to proteins of the extracellular matrix (ECM) provides structural and signaling information for biological processes such as cell proliferation, migration, neurite outgrowth, and differentiation. Integrins represent a family of heterodimeric transmembrane cell surface receptors. Besides connecting the ECM with the cytoskeleton, integrins also induce various signaling pathways in response to ligand binding. Integrin ligation leads to cytoplasmic protein-protein interactions requiring both integrin cytoplasmic tails. These sequences are initiation points for focal adhesion formation and subsequent signal transduction cascades. In this study, we addressed the question of whether the short cytoplasmic tail of the alpha(3) integrin subunit of alpha(3)beta(1) integrin is required for alpha(3)beta(1) integrin-dependent processes. For this purpose, cDNA representing the extracellular and transmembrane domain of the interleukin 2 receptor (IL2R) alpha subunit and the cytoplasmic sequence of the alpha(3) integrin subunit was transfected into PC12 cells. Autonomous expression of the cytoplasmic alpha(3) tail does not affect attachment but leads to inhibition of neuronal differentiation on laminin 5. This indicates that the cytoplasmic alpha(3) sequence is not required for cell attachment but is necessary for long-term adhesion and for the reorganization of the cytoskeleton that precedes neuronal differentiation. Inhibition of neurite outgrowth by chimeric IL2R-alpha(3) can be rescued by treatment of transfected cells with the pharmacological inhibitor Y27632, which inhibits the RhoA downstream effector Rho kinase alpha.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0360-4012
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
82
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
753-61
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:16267829-Animals, pubmed-meshheading:16267829-Antibodies, pubmed-meshheading:16267829-Blotting, Western, pubmed-meshheading:16267829-Carcinoma, pubmed-meshheading:16267829-Cell Adhesion Molecules, pubmed-meshheading:16267829-Cell Differentiation, pubmed-meshheading:16267829-Cell Line, Tumor, pubmed-meshheading:16267829-Cytoplasm, pubmed-meshheading:16267829-Enzyme Inhibitors, pubmed-meshheading:16267829-Flow Cytometry, pubmed-meshheading:16267829-Fluorescent Antibody Technique, pubmed-meshheading:16267829-Gene Expression Regulation, pubmed-meshheading:16267829-Humans, pubmed-meshheading:16267829-Integrin alpha3beta1, pubmed-meshheading:16267829-Neurites, pubmed-meshheading:16267829-PC12 Cells, pubmed-meshheading:16267829-Protein Structure, Tertiary, pubmed-meshheading:16267829-RNA, Messenger, pubmed-meshheading:16267829-Rats, pubmed-meshheading:16267829-Receptors, Interleukin-2, pubmed-meshheading:16267829-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:16267829-Transfection
pubmed:year
2005
pubmed:articleTitle
The cytoplasmic tail of the alpha3 integrin subunit promotes neurite outgrowth in PC12 cells.
pubmed:affiliation
Charité-Universitätsmedizin Berlin, Campus Benjamin Franklin, Institut für Biochemie und Molekularbiologie, Berlin-Dahlem, Germany.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't