Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1999-4-21
pubmed:abstractText
The attachment of cells to the extracellular matrix is of crucial importance in the maintenance of tissue structure and integrity. In stratified epithelia such as in skin as well as in other complex epithelia multiprotein complexes called hemidesmosomes are involved in promoting the adhesion of epithelial cells to the underlying basement membrane. In the past few years our understanding of the role of hemidesmosomes has improved considerably. Their importance has become apparent in clinical conditions, in which absence or defects of hemidesmosomal proteins result in devastating blistering diseases of the skin. Molecular genetic studies have increased our knowledge of the function of the various components of hemidesmosomes and enabled the characterization of protein-protein interactions involved in their assembly. It has become clear that the alpha6beta4 integrin, a major component of hemidesmosomes, is able to transduce signals from the extracellular matrix to the interior of the cell, that critically modulate the organization of the cytoskeleton, proliferation, apoptosis, and differentiation. Nevertheless, our knowledge of the mechanisms regulating the functional state of hemidesmosomes and, hence, the dynamics of cell adhesion, a process of crucial importance in development, wound healing or tumor invasion, remains limited. The aims of this review are to highlight the recent progresses of our knowledge on the organization and assembly of hemidesmosomes, their involvement in signaling pathways as well as their participation in clinical pathologic conditions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Surface, http://linkedlifedata.com/resource/pubmed/chemical/Autoantigens, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules, http://linkedlifedata.com/resource/pubmed/chemical/Collagen, http://linkedlifedata.com/resource/pubmed/chemical/Cytoskeletal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/DST protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Dst protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Integrin alpha6beta4, http://linkedlifedata.com/resource/pubmed/chemical/Integrins, http://linkedlifedata.com/resource/pubmed/chemical/Intermediate Filament Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Non-Fibrillar Collagens, http://linkedlifedata.com/resource/pubmed/chemical/PLEC protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Plec protein, mouse, http://linkedlifedata.com/resource/pubmed/chemical/Plectin, http://linkedlifedata.com/resource/pubmed/chemical/collagen type XVII, http://linkedlifedata.com/resource/pubmed/chemical/kalinin
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0022-202X
pubmed:author
pubmed:issnType
Print
pubmed:volume
112
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
411-8
pubmed:dateRevised
2011-10-27
pubmed:meshHeading
pubmed-meshheading:10201522-Animals, pubmed-meshheading:10201522-Antigens, Surface, pubmed-meshheading:10201522-Autoantigens, pubmed-meshheading:10201522-Carrier Proteins, pubmed-meshheading:10201522-Cell Adhesion, pubmed-meshheading:10201522-Cell Adhesion Molecules, pubmed-meshheading:10201522-Collagen, pubmed-meshheading:10201522-Cytoskeletal Proteins, pubmed-meshheading:10201522-Desmosomes, pubmed-meshheading:10201522-Humans, pubmed-meshheading:10201522-Integrin alpha6beta4, pubmed-meshheading:10201522-Integrins, pubmed-meshheading:10201522-Intermediate Filament Proteins, pubmed-meshheading:10201522-Mice, pubmed-meshheading:10201522-Mice, Knockout, pubmed-meshheading:10201522-Nerve Tissue Proteins, pubmed-meshheading:10201522-Non-Fibrillar Collagens, pubmed-meshheading:10201522-Plectin
pubmed:year
1999
pubmed:articleTitle
Structure and function of hemidesmosomes: more than simple adhesion complexes.
pubmed:affiliation
Department of Dermatology, DHURDV, University Hospital of Geneva, Switzerland.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't