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

Oral lichen planus exhibits features of a mucosal type IV immunopathologic process. Adhesion molecules involved in the trafficking and homing of T lymphocytes to the subepithelial compartment were assessed by immunohistochemical methods. Laminin, type IV collagen and type VII collagen extracellular matrix components at the epithelial-connective tissue junction are significantly increased and serve as ligands for beta 1 integrins on lymphocyte membranes. Endothelial-associated intercellular adhesion molecule 1 and extracellular matrix basement membrane components are also significantly increased in the submucosa. Keratinocyte expression of major histocompatibility complex class II molecules and intercellular adhesion molecule 1 may serve as ligands for lymphocyte T cell receptor complex and beta 2 integrins, respectively. These adhesion molecules are probably involved in the trafficking of lymphocytes to the epithelial connective tissue interface in response to as of yet undefined antigens.
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PMID:Leukocyte adhesion molecules in oral lichen planus: a T cell-mediated immunopathologic process. 787 Apr 74

Integrin dimer alpha 6 beta 4 is a transmembrane component of an epithelial cell adhesion complex that consists of hemidesmosomes (HDs), basement membrane (BM)-associated laminin-5 (Ln-5), and anchoring filaments/type VII collagen, all of which are absent from normal thyroid follicular epithelium. In the present study, the expression of epithelial cell adhesion complex antigens in thyroid tumours was investigated using immunohistochemistry. In addition to integrin subunits alpha 6 and beta 4, immunoreactivity was found for all chains of Ln-5, alpha 3, beta 3 and gamma 2, type VII collagen and hemidesmosomal antigen, HD1, in most thyroid carcinomas associated with tumour anaplasia and papillary growth pattern and located at the border of parenchymal cells and connective tissue or blood vessel walls. In addition, a more restricted expression of bullous pemphigoid antigens 180 and 230 (BP180 and BP230), constituents of HDs, was found in some papillary and anaplastic carcinomas and atypical adenomas. Adhesion complex antigens were located to regions of cells which were immunoreactive for cytokeratin (ck)-5 and proliferating cell nuclear antigen Ki-67. The results suggest that in thyroid carcinomas, the emergence of adhesion complex antigens is associated with squamous differentiation and high proliferative activity.
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PMID:Neoexpression of the epithelial adhesion complex antigens in thyroid tumours is associated with proliferation and squamous differentiation markers. 960 11

Dermal fibroblasts are in apposition to type VII (anchoring fibril) collagen in both unwounded and wounded skin. The NC1 domain of type VII collagen contains multiple submodules with homology to known adhesive molecules, including fibronectin type III-like repeats and a potential RGD cell attachment site. We previously reported the structure and matrix binding properties of authentic and recombinant NC1. In this study, we examined the interaction between dermal fibroblasts and the NC1 domain of type VII collagen. We found that both recombinant and authentic NC1 vigorously promoted human fibroblast attachment. Adhesion of fibroblasts to NC1 was dose dependent, saturable, and abolished by both polyclonal and monoclonal antibodies to NC1. Cell adhesion to NC1 was divalent cation dependent and specifically inhibited by a monoclonal antibody directed against the alpha2 or beta1 integrin subunits, but not by the presence of RGD peptides. Furthermore, the cell-binding activity of NC1 was not conformation dependent, since heat-denatured NC1 still promoted cell adhesion. Using a series of recombinant NC1 deletion mutant proteins, the cell binding site of NC1 was mapped to a 158-aa (residues 202-360) subdomain. We conclude that human dermal fibroblasts interact with the NC1 domain of type VII collagen and this cell-matrix interaction is mediated by the alpha2beta1 integrin and is RGD independent.
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PMID:Alpha 2 beta 1 integrin mediates dermal fibroblast attachment to type VII collagen via a 158-amino-acid segment of the NC1 domain. 1036 22