Localization of the cytoadhesin integrins in the human cornea
| Autor: | L. Missotten, Brigitte Lauweryns, Joost van den Oord |
|---|---|
| Rok vydání: | 1992 |
| Předmět: |
Integrins
Pathology medicine.medical_specialty Corneal endothelium Integrin Platelet Membrane Glycoproteins Epithelium Corneal Diseases Cornea Immunoenzyme Techniques Cellular and Molecular Neuroscience medicine Humans Receptors Vitronectin Receptors Immunologic Corneal epithelium biology Cell adhesion molecule Endothelium Corneal Antibodies Monoclonal Sensory Systems Ophthalmology medicine.anatomical_structure biology.protein Immunohistochemistry Vitronectin |
| Zdroj: | Graefe's Archive for Clinical and Experimental Ophthalmology. 230:264-268 |
| ISSN: | 1435-702X 0721-832X |
| DOI: | 10.1007/bf00176302 |
| Popis: | Cell-matrix interactions play a fundamental role in normal and pathological conditions. They can be mediated by the cytoadhesin subgroup of the integrin superfamily of adhesion molecules. Its members include the vitronectin receptor (VNR) and the platelet glycoprotein IIb/IIIa (GP IIb/IIIa). Both receptors are composed of an alpha-chain (alpha v and alpha IIb, respectively) coupled to a beta 3-chain. Using in situ immunohistochemistry and monoclonal antibodies, the authors studied the distribution of GP IIIa (common beta 3-chain), GP IIb/IIIa (alpha IIb-chain) and VNR (alpha v-chain) in normal and pathological corneal tissues. In the normal cornea, the limbal vascular endothelium was weakly alpha v-positive. Occasionally, faint and granular staining was seen in the epithelium. In the pathological samples, an upregulated expression of the alpha v-chain was noticed on the corneal epithelium as well as on fibroblasts and corneal endothelium. The alpha IIb and beta 3-chains were consistently absent. These data suggest that expression of the VNR-alpha v-chain in the human cornea is modulated by soluble factors released during inflammation and wound healing. Dissociation of expression of the alpha v and beta 3-chains suggests usage of an alternative beta-chain by the VNR-alpha v-chain. |
| Databáze: | OpenAIRE |
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