Linked Life Data

15191880

Source:http://linkedlifedata.com/resource/pubmed/id/15191880

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2004-9-13
pubmed:abstractText
Superficial wounds in the gastrointestinal tract rapidly reseal by coordinated epithelial cell migration facilitated by cytokines such as hepatocyte growth factor (HGF)/scatter factor released in the wound vicinity. However, the mechanisms by which HGF promotes physiological and pathophysiologic epithelial migration are incompletely understood. Using in vitro models of polarized T84 and Caco-2 intestinal epithelia, we report that HGF promoted epithelial spreading and RhoA GTPase activation in a time-dependent manner. Inducible expression of enhanced green fluorescent protein-tagged dominant-negative RhoA significantly attenuated HGF-induced spreading. HGF expanded a zone of partially flattened cells behind the wound edge containing basal F-actin fibers aligned in the direction of spreading. Concomitantly, plaques positive for the focal adhesion protein paxillin were enhanced. HGF induced an increase in the translation of paxillin and, to a lesser extent, beta1-integrin. This was independent of cell-matrix adhesion through beta1-integrin. Subcellular fractionation revealed increased cosedimentation of paxillin with plasma membrane-containing fractions following HGF stimulation, without corresponding enhancements in paxillin coassociation with beta1 integrin or actin. Tyrosine phosphorylation of paxillin was reduced by HGF and was sensitive to the Src kinase inhibitor PP2. With these taken together, we propose that HGF upregulates a free cytosolic pool of paxillin that is unaffiliated with either the cytoskeleton or focal cell-matrix contacts. Thus early spreading responses to HGF may partly relate to increased paxillin availability for incorporation into, and turnover within, dynamic cytoskeletal/membrane complexes whose rapid and transient adhesion to the matrix drives migration.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0193-1857
pubmed:author
pubmed:issnType
Print
pubmed:volume
287
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
G886-98
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:15191880-Actins, pubmed-meshheading:15191880-Antigens, CD29, pubmed-meshheading:15191880-Caco-2 Cells, pubmed-meshheading:15191880-Cell Membrane, pubmed-meshheading:15191880-Cell Movement, pubmed-meshheading:15191880-Cells, Cultured, pubmed-meshheading:15191880-Colon, pubmed-meshheading:15191880-Cytoskeletal Proteins, pubmed-meshheading:15191880-Cytosol, pubmed-meshheading:15191880-Epithelial Cells, pubmed-meshheading:15191880-Focal Adhesions, pubmed-meshheading:15191880-Hepatocyte Growth Factor, pubmed-meshheading:15191880-Humans, pubmed-meshheading:15191880-Paxillin, pubmed-meshheading:15191880-Phosphoproteins, pubmed-meshheading:15191880-Phosphorylation, pubmed-meshheading:15191880-Protein Processing, Post-Translational, pubmed-meshheading:15191880-Up-Regulation, pubmed-meshheading:15191880-rhoA GTP-Binding Protein, pubmed-meshheading:15191880-src-Family Kinases
pubmed:year
2004
pubmed:articleTitle
Epithelial cell spreading induced by hepatocyte growth factor influences paxillin protein synthesis and posttranslational modification.
pubmed:affiliation
Dept. of Pathology and Laboratory Medicine, Emory Univ., Rm. 105E, Whitehead Research Bldg., 615 Michael St., Atlanta, GA 30322, USA. anusrat@emory.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't