J. Biol. Chem., Vol. 259, Issue 7, 4031-4034, Apr, 1984
Inhibition of embryonic neural retina cell-substratum adhesion with a monoclonal antibody
GJ Cole and L Glaser
The C1H3 monoclonal antibody recognizes two distinct developmentally
regulated cell surface antigens, with molecular masses of 170,000 and
140,000 daltons, in embryonic chick neural retina (Cole, G. J., and Glaser,
L. (1984) Proc. Natl. Acad. Sci. U. S. A., in press). In vitro, the
170,000-dalton polypeptide is released by retinal cells into the
surrounding culture medium and is present in material sedimentable at
100,000 X g. This pelletable material contains particles designated as
adherons (Schubert, D., LaCorbiere, M., Klier, F. G., and Birdwell, G.
(1983) J. Cell Biol. 96, 990-998) which promote cell-substratum adhesion of
chick neural retina cells. In the present study, evidence is provided that
the C1H3 monoclonal antibody inhibits cell adhesion to adheron-coated
dishes when bound either to cells or to the adherons. The failure of other
monoclonal antibodies, that bind to retinal cells with equal abundance, to
disrupt adhesion demonstrates that the effect is specific. These data
suggest that the neural-specific 170,000-dalton C1H3 polypeptide is the
neural cell-adhesion molecule which is responsible for the ability of
adherons to bind to cells.
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