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Published January 15, 1993 | Published
Journal Article Open

Expression and Structural Studies of Fasciclin I, an Insect Cell Adhesion Molecule


Fasciclin I is a lipid-linked cell-surface glycoprotein that can act as a homophilic adhesion molecule in tissue culture cells. It is thought to be involved in growth cone guidance in the embryonic insect nervous system. To facilitate structure-function studies, we have generated Chinese hamster ovary (CHO) cell lines expressing high levels of cell surface grasshopper and Drosophila fasciclin I. Grasshopper fasciclin I released by phospholipase C cleavage was purified on an immunoaffinity column and single crystals were obtained that diffracted to approximately 5-A resolution. We also generated CHO and Drosophila S2 cell lines that produce a secreted form of fasciclin I. Fasciclin I expressed in S2 cells contains significantly less carbohydrate than the protein expressed in CHO cells, and may therefore be more suitable for crystallization. Biochemical characterization of purified fasciclin I indicates that the extracellular portion exists as a monomer in solution. Circular dichroism studies suggest that fasciclin I is primarily alpha-helical. Its structure is therefore different from other known cell adhesion molecules, which are predicted to be elongated beta-sheet structures. This suggests that fasciclin I may define a new structural motif used to mediate adhesive interactions between cell surfaces.

Additional Information

© 1993 American Society for Biochemistry and Molecular Biology Inc. Received for publication, June 24, 1992, and in revised form, September 21, 1992. This work was supported by the Howard Hughes Medical Institute (P. J. B.) and the National Institutes of Health (NS28182 to K. Z.). The costs of publication of this article were defrayed in part by the payment of page charges. We thank Ilana Tamir and Jim Moore for help with CD analysis, Pantelis Tsoulfas for help with constructing the secreted form of fasciclin I, David Penny and Louis Gastinel for help with tissue culture, Chris Bebbington for the glutamine synthetase vector, and Peggy Fahnestock, Louis Gastinel, and Malini Raghavan for critically reading the manuscript.

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Published - J._Biol._Chem.-1993-Wang-1448-55.pdf


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