Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: UMLS:C0001511 (Adhesion)
 5,955 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Wounding of skin activates epidermal cell migration over exposed dermal collagen and fibronectin and over laminin 5 secreted into the provisional basement membrane. Gap junctional intercellular communication (GJIC) has been proposed to integrate the individual motile cells into a synchronized colony. We found that outgrowths of human keratinocytes in wounds or epibole cultures display parallel changes in the expression of laminin 5, integrin alpha3beta1, E-cadherin, and the gap junctional protein connexin 43. Adhesion of keratinocytes on laminin 5, collagen, and fibronectin was found to differentially regulate GJIC. When keratinocytes were adhered on laminin 5, both structural (assembly of connexin 43 in gap junctions) and functional (dye transfer) assays showed a two- to threefold increase compared with collagen and five- to eightfold over fibronectin. Based on studies with immobilized integrin antibody and integrin-transfected Chinese hamster ovary cells, the interaction of integrin alpha3beta1 with laminin 5 was sufficient to promote GJIC. Mapping of intermediate steps in the pathway linking alpha3beta1-laminin 5 interactions to GJIC indicated that protein trafficking and Rho signaling were both required. We suggest that adhesion of epithelial cells to laminin 5 in the basement membrane via alpha3beta1 promotes GJIC that integrates individual cells into synchronized epiboles.
 ...
PMID:Cellular interaction of integrin alpha3beta1 with laminin 5 promotes gap junctional communication. 985 64

Adhesion, segregation, and cellular plasticity are regulated by actin filaments anchored at the plaques of adherens junctions, sites of mechanical stabilization, and interfaces of multiple signaling networks. Drebrins were originally identified in neuronal cells, but the isoform drebrin E was also detected at adherens junctions of a wide range of non-neuronal cells, including polarized epithelia, endothelia, and fibroblasts. Here the protein is enriched at actin filament bundles associated with junctional plaques. Polarized epithelial cells contain two types of actin-associated complexes, one comprising drebrin but not vinculin and the other involving vinculin, but not drebrin. At gap junctions drebrin interacts with connexin 43, stabilizes this protein at membranes, and links it to the actin cytoskeleton. In vivo drebrin is widespread in diverse non-neuronal tissues of epithelial, endothelial, and smooth muscle origin, but not ubiquitous. In intestinal cells it is involved in cell compaction, linking of actin filaments to microtubules and formation and stabilization of the terminal web. Upregulation of drebrin was noted in several types of cancers, e.g., basal cell carcinomas for which it may serve as marker, liver metastases of colon carcinomas, and bladder cancer, suggesting that it is involved in regulating actin dynamics during tumor development, progression, and metastasis.
 ...
PMID:Drebrin at Junctional Plaques. 2886 28