Role of third N-terminal domain of VCAM-1.
The interaction between VLA-4 and VCAM-1 has been implicated in the recruitment, adhesion, and activation of mononuclear leukocytes in chronic inflammatory conditions and autoimmune disease. The seven domain extracellular portion of VCAM-1, sVCAM1-7, and the first three and two N-terminal domains of VCAM-1, sVCAM1-3 and sVCAM1-2, respectively, were expressed in baculovirus and purified. Using these purified soluble forms of VCAM-1 and cellular transfectants expressing various cell bound forms of VCAM-1, we show that the major binding site for VLA-4 is located within the first two domains of VCAM-1 and that the third domain of VCAM-1 appears to be required for functional integrity of the VLA-4 binding site.
Webb
D L
DL
Institute for Bone and Joint Disorders, Miles Research Center, West Haven, CT 06516.
Marlor
C W
CW
Conrad
P J
PJ
Barkowski-Clark
S
S
Blue
M L
ML
D016367:Baculoviridae / Q000235:genetics; D002448:Cell Adhesion; D015815:Cell Adhesion Molecules / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism*; D002460:Cell Line; D002478:Cells, Cultured; D004730:Endothelium, Vascular / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D010446:Peptide Fragments / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism; D010957:Plasmids; D016029:Receptors, Very Late Antigen / Q000378:metabolism; D014162:Transfection; D014407:Tumor Cells, Cultured; D014471:Umbilical Veins; D019010:Vascular Cell Adhesion Molecule-1
D015815:Cell Adhesion Molecules; D010446:Peptide Fragments; D016029:Receptors, Very Late Antigen; D019010:Vascular Cell Adhesion Molecule-1