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J Biol Chem, Vol. 274, Issue 31, 21609-21616, July 30, 1999
V
3 Detected with a Novel Patch-engineered
Monovalent Ligand
,,,¶,
From the Departments of Integrin Vascular Biology,
¶ Immunology, and Molecular and Experimental Medicine,
Scripps Research Institute, La Jolla, California 92037
V
3
mediates diverse responses in vascular cells, ranging from cell
adhesion, migration, and proliferation to uptake of adenoviruses.
However, the extent to which V3 is
regulated by changes in receptor conformation (affinity),
receptor diffusion/clustering (avidity), or post-receptor events is
unknown. Affinity regulation of the related integrin,
IIb3, has been established using a monovalent ligand-mimetic antibody, PAC1 Fab. To determine the role of
affinity modulation of V3, a novel
monovalent ligand-mimetic antibody (WOW-1) was created by replacing the
heavy chain hypervariable region 3 of PAC1 Fab with a single
V integrin-binding domain from multivalent adenovirus
penton base. Both WOW-1 Fab and penton base bound selectively to
activated V3, but not to
IIb3, in receptor and cell binding
assays. V3 affinity varied with the cell
type. Unstimulated B-lymphoblastoid cells bound WOW-1 Fab poorly
(apparent Kd = 2.4 µM), but acute
stimulation with phorbol 12-myristate 13-acetate increased receptor
affinity >30-fold (Kd = 80 nM), with
no change in receptor number. In contrast,
V3 in melanoma cells was constitutively
active, but ligand binding could be suppressed by overexpression of
3 cytoplasmic tails. Up-regulation of
V3 affinity had functional consequences
in that it increased cell adhesion and spreading and promoted
adenovirus-mediated gene transfer. These studies establish that
V3 is subject to rapid regulated changes
in affinity that influence the biological functions of this integrin.
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