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J. Biol. Chem., Vol. 269, Issue 44, 27224-27230, Nov, 1994
AP Mould, JA Askari, SE Craig, AN Garratt, J Clements and MJ Humphries
The integrin receptor alpha 4 beta 1 (also known as VLA-4) binds two
different ligands, the endothelial cell surface protein vascular cell
adhesion molecule-1 (VCAM-1) and the extracellular matrix component
fibronectin. Three distinct sites in fibronectin are recognized by alpha 4
beta 1. Two of these (represented by peptides CS1 and CS5) are present in
the alternatively spliced IIICS region and lie in separate, independently
spliced segments of this region. A third site resides in the adjacent
constitutively expressed HepII domain. Recombinant proteins containing the
HepII domain and different splice variants of the IIICS have been generated
and compared for their ability to mediate cell attachment, spreading and
migration. The activity of these proteins has also been compared with that
of a recombinant soluble form of VCAM-1 (rsVCAM-1). All the recombinant
proteins supported A375-SM human melanoma cell attachment and spreading in
an alpha 4 beta 1- dependent manner, but had varied adhesive activities
with rsVCAM-1 > fibronectin variants containing the CS1 sequence
>> other fibronectin variants. Low concentrations of rsVCAM-1 and
CS1-containing fibronectin variants effectively supported cell migration in
a trans-filter assay; however, cell motility was retarded at high
concentrations of the same proteins. Fibronectin variants lacking CS1
supported little or no migration. To obtain further insight into the
molecular basis of this varied adhesive activity, apparent dissociation
constants for each of the recombinant proteins were measured using a solid
phase receptor- ligand binding assay. The results revealed a hierarchy of
ligand affinities that mirrored their adhesive activity (rsVCAM-1 >
fibronectin variants containing CS1 >> other fibronectin variants).
Integrin alpha 4 beta 1-mediated melanoma cell adhesion and migration on vascular cell adhesion molecule-1 (VCAM-1) and the alternatively spliced IIICS region of fibronectin
School of Biological Sciences, University of Manchester, United Kingdom.
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G. Frankel, O. Lider, R. Hershkoviz, A. P. Mould, S. G. Kachalsky, D. C.A. Candy, L. Cahalon, M. J. Humphries, and G. Dougan The Cell-binding Domain of Intimin from Enteropathogenic Escherichia coli Binds to beta 1 Integrins J. Biol. Chem., August 23, 1996; 271(34): 20359 - 20364. [Abstract] [Full Text] [PDF]
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A. P. Mould, S. K. Akiyama, and M. J. Humphries The Inhibitory Anti-beta 1 Integrin Monoclonal Antibody 13Recognizes an Epitope That Is Attenuated by Ligand Occupancy. EVIDENCE FOR ALLOSTERIC INHIBITION OF INTEGRIN FUNCTION J. Biol. Chem., August 23, 1996; 271(34): 20365 - 20374. [Abstract] [Full Text] [PDF]
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A. P. Mould, S. K. Akiyama, and M. J. Humphries Regulation of Integrin alpha5beta1-Fibronectin Interactions by Divalent Cations J. Biol. Chem., November 3, 1995; 270(44): 26270 - 26277. [Abstract] [Full Text] [PDF]
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A. R. E. Shaw, A. Domanska, A. Mak, A. Gilchrist, K. Dobler, L. Visser, S. Poppema, L. Fliegel, M. Letarte, and B. J. Willett Ectopic Expression of Human and Feline CD9 in a Human B Cell Line Confers beta1 Integrin-dependent Motility on Fibronectin and Laminin Substrates and Enhanced Tyrosine Phosphorylation J. Biol. Chem., October 13, 1995; 270(41): 24092 - 24099. [Abstract] [Full Text] [PDF]
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M. M. Robledo, R. A. Bartolome, N. Longo, J. M. Rodriguez-Frade, M. Mellado, I. Longo, G. N. P. van Muijen, P. Sanchez-Mateos, and J. Teixido Expression of Functional Chemokine Receptors CXCR3 and CXCR4 on Human Melanoma Cells J. Biol. Chem., November 21, 2001; 276(48): 45098 - 45105. [Abstract] [Full Text] [PDF]
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