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Vol. 8, Issue 12, 2647-2657, December 1997
-Chain Sites That
Affect Cell Adhesion and Adhesion Strengthening without Altering
Soluble Ligand Binding
§
*Division of Tumor Virology, Dana-Farber Cancer Institute, Harvard
Medical School, Boston, Massachusetts 02115;
It was previously shown that mutations of integrin Department
of Immunology, The Weizmann Institute of Science, Rehovot 76100, Israel;
§Center for Blood Research, Harvard Medical
School, Boston, Massachusetts 02115; and
¶Biogen Inc.,
Cambridge, Massachusetts 02142
4
chain sites, within putative EF-hand-type divalent cation-binding
domains, each caused a marked reduction in 4
1-dependent cell
adhesion. Some reports have suggested that -chain "EF-hand"
sites may interact directly with ligands. However, we show here that
mutations of three different 4 "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 41-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 4 "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.
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