|
||
Article |
Address correspondence to Jorma Keski-Oja, Department of Pathology, P.O. Box 63, Biomedicum Helsinki, University of Helsinki, Helsinki FIN-00014, Finland. Tel.: 358-9-191-25566. Fax: 358-9-191-25573. email: jorma.keski-oja{at}helsinki.fi
We have analyzed the effects of latent TGF-ß binding protein 2 (LTBP-2) and its fragments on lung fibroblast adhesion. Quantitative cell adhesion assays indicated that fibroblasts do not adhere to full-length LTBP-2. Interestingly, LTBP-2 had dominant disrupting effects on the morphology of fibroblasts adhering to fibronectin (FN). Fibroblasts plated on LTBP-2 and FN substratum exhibited less adherent morphology and displayed clearly decreased actin stress fibers than cells plated on FN. These cells formed, instead, extensive membrane ruffles. LTBP-2 had no effects on cells adhering to collagen type I. Fibroblasts adhered weakly to the NH2-terminal fragment of LTBP-2. Unlike FN, this fragment did not augment actin stress fiber formation. Interestingly, the adhesion-mediating and cytoskeleton-disrupting effects were localized to the same NH2-terminal proline-rich region of LTBP-2. LTBP-2 and its antiadhesive fragment bound to FN in vitro, and the antiadhesive fragment associated with the extracellular matrix FN fibrils. These observations reveal a potentially important role for LTBP-2 as an antiadhesive matrix component.
Key Words: extracellular matrix; LTBP; cell adhesion; antiadhesion; fibronectin
This article has been cited by other articles:
|
|