Linked Life Data

17572164

Source:http://linkedlifedata.com/resource/pubmed/id/17572164

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2007-8-13
pubmed:abstractText
The elucidation of molecular cell-extracellular matrix (ECM) interactions regulating tissue dynamics necessitates straightforward model systems that can dissect the associated physiological complexity into a smaller number of distinct interactions. Here we employ a previously developed artificial ECM model system to study dynamic cell-matrix interactions involved in proteolytic three-dimensional (3-D) migration and matrix remodeling at the level of single cells. Quantitative time-lapse microscopy of primary human fibroblasts exposed to exogenous physiological matrix metalloproteinase (MMP) inhibitors revealed that 3-D migration is dependent on cell seeding density and occurred via highly localized MMP- and tissue inhibitor of metalloproteinases-2-dependent processes. Stimulation of cells by tumor necrosis factor alpha led to a striking augmentation in fibroblast migration that was accompanied by induction of alphaVbeta3 integrin expression. In long-term cultures, extensive localized cellular matrix remodeling resulted in the morphogenesis of single cells into interconnected multicellular networks. Therefore, these tailor-made artificial ECMs can replicate complex 3-D cell-matrix interactions involved in tissue development and regeneration, an important step in the design of next-generation synthetic biomaterials for tissue engineering.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1742-7061
pubmed:author
pubmed:issnType
Print
pubmed:volume
3
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
615-29
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Mechanisms of 3-D migration and matrix remodeling of fibroblasts within artificial ECMs.
pubmed:affiliation
Institute of Bioengineering and Institute of Chemical Sciences and Engineering, Ecole Polytechnique Fédérale de Lausanne, CH-1015 Lausanne, Switzerland.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't