The adhesion modulating properties of tenascin-W.
Tenascins are extracellular matrix glycoproteins associated with cell motility, proliferation and differentiation. Tenascin-C inhibits cell spreading by binding to fibronectin; tenascin-R and tenascin-X also have anti-adhesive properties in vitro. Here we have studied the adhesion modulating properties of the most recently characterized tenascin, tenascin-W. C2C12 cells, a murine myoblast cell line, will form broad lamellipodia with stress fibers and focal adhesion complexes after culture on fibronectin. In contrast, C2C12 cells cultured on tenascin-W fail to spread and form stress fibers or focal adhesion complexes, and instead acquire a multipolar shape with short, actin-tipped pseudopodia. The same stellate morphology is observed when C2C12 cells are cultured on a mixture of fibronectin and tenascin-W, or on fibronectin in the presence of soluble tenascin-W. Tenascin-W combined with fibronectin also inhibits the spreading of mouse embryo fibroblasts when compared with cells cultured on fibronectin alone. The similarity between the adhesion modulating effects of tenascin-W and tenascin-C in vitro led us to study the possibility of tenascin-W compensating for tenascin-C in tenascin-C knockout mice, especially during epidermal wound healing. Dermal fibroblasts harvested from a tenascin-C knockout mouse express tenascin-W, but dermal fibroblasts taken from a wild type mouse do not. However, there is no upregulation of tenascin-W in the dermis of tenascin-C knockout mice, or in the granulation tissue of skin wounds in tenascin-C knockout animals. Similarly, tenascin-X is not upregulated in early wound granulation tissue in the tenascin-C knockout mice. Thus, tenascin-W is able to inhibit cell spreading in vitro and it is upregulated in dermal fibroblasts taken from the tenascin-C knockout mouse, but neither it nor tenascin-X are likely to compensate for missing tenascin-C during wound healing.
Friedrich Miescher Institute for Biomedical Research, Novartis Research Foundation, Basel, Switzerland.
Florence
F
Brellier
Enrico
E
Martina
Matthias
M
Chiquet
Jacqueline
J
Ferralli
Michael
M
van der Heyden
Gertraud
G
Orend
Johannes C
JC
Schittny
Ruth
R
Chiquet-Ehrismann
Richard P
RP
Tucker
D000199:Actins / Q000378:metabolism / Q000502:physiology; D000818:Animals; D002448:Cell Adhesion; D018929:Cell Culture Techniques; D002460:Cell Line; D002465:Cell Movement; D002478:Cells, Cultured; D005353:Fibronectins / Q000378:metabolism / Q000494:pharmacology / Q000502:physiology; D005786:Gene Expression Regulation; D055786:Gene Knockout Techniques; D051379:Mice; D011554:Pseudopodia / Q000502:physiology / Q000648:ultrastructure; D019063:Tenascin / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology / Q000502:physiology*; D014945:Wound Healing / Q000235:genetics
D000199:Actins; D005353:Fibronectins; D019063:Tenascin; C477504:tenascin-N protein, mouse