Using direct force measurements to determine the mechanism of neural cell adhesion molecule (NCAM) function

Author

Leckband, D. ; Johnson, C. ; Roberts, R. ; Fujimoto, I. ; Anderson, B. ; Rutishauser, U.

Author_Institution

Dept. of Chem. Eng., Illinois Univ., Urbana, IL, USA

Volume

1

fYear

2002

fDate

2002

Firstpage

339

Abstract

The molecular mechanism of homophilic adhesion between neural cell adhesion molecules (NCAM) was investigated by direct force measurements. The force-distance profiles demonstrated that multiple domains are involved in adhesion. In addition, the effect of polysialylation on the interprotein forces provided insights into the molecular mechanism by which posttranslational modification regulates NCAM function.

Keywords

adhesion; biomechanics; force measurement; molecular biophysics; neurophysiology; proteins; cell-cell signaling; direct force measurements; force-distance profiles; homophilic adhesion; homophilic interactions; identical proteins on opposing cells; molecular mechanism; multiple domains; neural cell adhesion molecules; neuronal cell adhesion proteins; polysialylation effect; posttranslational modification; Adhesives; Biophysics; Cancer; Cells (biology); Chemical engineering; Chemistry; Computational biology; Force measurement; Lipidomics; Protein engineering;

fLanguage

English

Publisher

ieee

Conference_Titel

Engineering in Medicine and Biology, 2002. 24th Annual Conference and the Annual Fall Meeting of the Biomedical Engineering Society EMBS/BMES Conference, 2002. Proceedings of the Second Joint

ISSN

1094-687X

Print_ISBN

0-7803-7612-9

Type

conf

DOI

10.1109/IEMBS.2002.1134524

Filename

1134524