Stretching fibronectin.

Published

Journal Article (Review)

Fibronectin (FN) matrix fibrils assembled in cell culture have been observed to stretch in response to cell movements, and when broken relax to 1/3 to 1/4 of their rest length. Two molecular mechanisms have been proposed, for the elasticity. One proposes that FN molecules in relaxed fibers are bent and looped into a compact conformation, and stretching pulls the molecules into the extended conformation but domains remain folded. The second proposes that molecules in fibrils are already extended, and stretching is produced by force-induced unfolding of FN type III domains. Experimental observations that may help distinguish these two possibilities are discussed.

Full Text

Duke Authors

Cited Authors

  • Erickson, HP

Published Date

  • January 2002

Published In

Volume / Issue

  • 23 / 5-6

Start / End Page

  • 575 - 580

PubMed ID

  • 12785106

Pubmed Central ID

  • 12785106

Electronic International Standard Serial Number (EISSN)

  • 1573-2657

International Standard Serial Number (ISSN)

  • 0142-4319

Digital Object Identifier (DOI)

  • 10.1023/a:1023427026818

Language

  • eng