Abstract
We have characterized the diversity of the chicken β1 integrin family and studied the expression of individual receptors during development. The diversity of the β1 integrin family was investigated by affinity purifying the β1 integrins from a variety of adult and embryonic tissues. These purifications reveal the relative levels of expression and also the differential expression of the α subunits in those tissues. Monoclonal antibodies were generated against the prominent 'band 1' of the embryonic chicken integrins and used to characterize the expression of this α subunit in embryonic and adult tissues. This α subunit is shown to be the chicken homologue of human α5 fibronectin receptor. The chicken α5β1 integrin is the most prominent β1 integrin in the embryo and is expressed on the majority of cell types through the day 17 stage. The distribution of this receptor in the embryo closely parallels the distribution of its ligand, fibronectin. In adult tissues, expression of this receptor is greatly diminished relative to the expression of other α subunits. The cell type distribution is highly restricted: limited primarily to the vasculature and to connective tissue regions. These studies reveal a prominent role for the α5β1 integrin in embryonic cell types and a down-regulation of this receptor on many cell types during development.
Original language | English (US) |
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Pages (from-to) | 327-337 |
Number of pages | 11 |
Journal | Development |
Volume | 113 |
Issue number | 1 |
State | Published - Sep 1991 |
Externally published | Yes |
Keywords
- Chick αβ integrin
- Collagen
- Fibronectin
- Laminin
- Monoclonal antibody
- Receptor
ASJC Scopus subject areas
- Molecular Biology
- Developmental Biology