Substrata formed by combinations of extracellular matrix components alter neural crest cell motility in vitro
Open Access
- 1 May 1983
- journal article
- Published by The Company of Biologists in Journal of Cell Science
- Vol. 61 (1) , 299-323
- https://doi.org/10.1242/jcs.61.1.299
Abstract
Extracellular matrix components such as collagen, fibronectin and sulphated glycosaminoglycans can act as substrata that promote neural crest motility in vitro, in the absence of serum. The cells appear to be less adhesive and move more randomly on collagen or chondroitin sulphate substrata than on fibronectin substrata. Cells do not spread or become motile on plastic dishes to which hyaluronate has been bound, presumably owing to weak adhesion to this surface. Hyaluronate added to the medium alone has little effect on cell motility. When combinations of matrix molecules are used as substrata, however, the presence of fibronectin increases spreading, directional persistence of cell motility and speed of movement above that observed on collagen alone. When added to fibronectin, chondroitin sulphate appears to reduce adhesions slightly, since the cells are more rounded. Hyaluronate added in the medium significantly reduces the extent, speed and directionality of movement on fibronectin substrata. The presence of collagen in combination with fibronectin plus glycosaminoglycans does not have a noticeable effect on cell motile behaviour, beyond that observed with fibronectin alone. The effects of combinations of matrix compounds on neural crest cell motility are thus predictable, and can be explained in terms of the known adhesive properties and reported binding interactions of these molecules. These studies in vitro are compared with neural crest cell motility in vivo.Keywords
This publication has 39 references indexed in Scilit:
- Glycosaminoglycans in the basal lamina and extracellular matrix of the developing mouse mammary ductDevelopmental Biology, 1982
- Role of fibronectin in collagen deposition: Fab' to the gelatin-binding domain of fibronectin inhibits both fibronectin and collagen organization in fibroblast extracellular matrix.The Journal of cell biology, 1982
- Basal lamina glycoproteins laminin and type IV collagen are assembled into a fine-fibered matrix in cultures of a teratocarcinoma-derived endodermal cell lineExperimental Cell Research, 1982
- Defective basal lamina formation by transformed mammary epithelial cells: A reduced effect of collagen on basal lamina (heparan sulfate‐rich) proteoglycan degradationJournal of Cellular Physiology, 1982
- Spontaneous glycosylation of glycosaminoglycan substrates by adherent fibroblastsCell, 1979
- Distribution and synthesis of glycosaminoglycans during quail neural crest morphogenesisDevelopmental Biology, 1978
- Analysis of glycosaminoglycans within the extracellular environments encountered by migrating neural crest cellsDevelopmental Biology, 1978
- The early migration of neural crest cells in the trunk region of the avian embryo: An electron microscopic studyDevelopmental Biology, 1978
- Structural analyses on the matrical organization of glycosaminoglycans in developing endocardial cushionsDevelopmental Biology, 1978
- Studies on intercellular adhesive selectivityDevelopmental Biology, 1968