## Abstract The I domain of integrin αE was modeled on the crystal structure of that in CD11b and mutated to produce an open (high affinity) or closed (low affinity) conformation. K562 transfectants expressing mutant αE and wild‐type β7 were tested for adhesion to E‐cadherin‐Fc. Downward displaceme
Role for the α7β1 integrin in vascular development and integrity
✍ Scribed by Nichole L. Flintoff-Dye; Jennifer Welser; Jachinta Rooney; Paul Scowen; Susan Tamowski; William Hatton; Dean J. Burkin
- Publisher
- John Wiley and Sons
- Year
- 2005
- Tongue
- English
- Weight
- 329 KB
- Volume
- 234
- Category
- Article
- ISSN
- 1058-8388
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📜 SIMILAR VOLUMES
Adhesion to collagens by most cell types is mediated by the integrins a1b1 and a2b1. Both integrin a subunits belong to a group which is characterized by the presence of an I domain in the N-terminal half of the molecule, and this domain has been implicated in the ligand recognition. Since purified
Grant sponsor: Association pour la Recherche sur le Cancer (ARC); Grant sponsor: Fondation Recherche et Partage (Caisse d'Epargne); Grant sponsor: Fonds de Recherche de la Socie ´te ´Nationale Franc ¸aise de Gastroente ´rologie.
Cytofluorimetric and reverse-transcription polymerase chain reaction (RT-PCR) analysis showed that adriamycinresistant (ADR R ), but not sensitive (WT), MCF-7 human mammary carcinoma cell lines express a4b1 and a5b1 integrins. ADR R cells adhere to fibronectin (FN), and only a5b1 is involved in cell