@article {529786,
	title = {Defining extracellular integrin α chain sites that affect cell adhesion and adhesion strengthening without altering soluble ligand binding},
	journal = {Mol. Biol. Cell},
	volume = {8},
	number = {12},
	year = {1997},
	note = {This work was supported by TAS grants CA31798 and HL48675Reprint Status: In File},
	pages = {2647-2657},
	abstract = {It was previously shown that mutations of integrin alpha4 chain sites, within putative EF-hand-type divalent cation-binding domains, each caused a marked reduction in alpha4beta1-dependent cell adhesion. Some reports have suggested that alpha-chain "EF-hand" sites may interact directly with ligands. However, we show here that mutations of three different alpha4 "EF-hand" sites each had no effect on binding of soluble monovalent or bivalent vascular cell adhesion molecule 1 whether measured indirectly or directly. Furthermore, these mutations had minimal effect on alpha4beta1-dependent cell tethering to vascular cell adhesion molecule 1 under shear. However, EF-hand mutants did show severe impairments in cellular resistance to detachment under shear flow. Thus, mutation of integrin alpha4 "EF-hand-like" sites may impair 1) static cell adhesion and 2) adhesion strengthening under shear flow by a mechanism that does not involve alterations of initial ligand binding.},
	keywords = {CD49d},
	author = {Pujades,C. and Yauch,R. and Alon, R. and Masumoto,A. and Burkly,L. and Springer, T.A. and Chen, C and Lobb,R.R. and Hemler,M.E.}
}
