Cell Biology

E.A. Wayner, A. Garcia-Pardo, M.J. Humphries, J.A. McDonald, W.G. Carter, "Identification and characterization of the T lymphocyte adhesion receptor for an alternative cell attachment domain (CS-1) in plasma fibronectin," The Journal of Cell Biology, 109, 1321-30, September 1989. Elizabeth A. Wayner (Cytel Corp., La Jolla, Calif.): "It was originally thought that the adhesion of mesenchymal cells to fibronectin was solely determined by the interaction of the integrin receptor, a5b1, with the ce

The Scientist Staff
Jan 20, 1991

E.A. Wayner, A. Garcia-Pardo, M.J. Humphries, J.A. McDonald, W.G. Carter, "Identification and characterization of the T lymphocyte adhesion receptor for an alternative cell attachment domain (CS-1) in plasma fibronectin," The Journal of Cell Biology, 109, 1321-30, September 1989.

Elizabeth A. Wayner (Cytel Corp., La Jolla, Calif.): "It was originally thought that the adhesion of mesenchymal cells to fibronectin was solely determined by the interaction of the integrin receptor, a5b1, with the central cell binding domain that contains RGD [a specific adhesion sequence]. Our study was the first to identify the RGD-independent fibronectin receptor present on lymphocytes, integrin a4b1. Instead of RGD, this receptor recognizes an amino acid sequence (CS-1) located within the alternatively spliced, or V (for variable), region of fibronectin. Thus, lymphocyte adhesion to fibronectin involves at least two independent receptor-ligand interactions: a5b1 to RGD, and a4b1 to CS-1. These studies allowed us to identify the alternative adhesion sequence,...

Interested in reading more?

Become a Member of

Receive full access to digital editions of The Scientist, as well as TS Digest, feature stories, more than 35 years of archives, and much more!
Already a member?