Fibronectin fibril growth in the extracellular matrix of the Xenopus embryo.
We show that the mechanism of fibronectin fibril formation on the blastocoel roof of the Xenopus embryo is comparable to that in other systems. Fibril assembly is inhibited by RGD peptide, by an amino-terminal fragment of fibronectin, and by cytochalasin B. When added exogenously, intact fibronectin, but not a 110 kDa cell binding fragment of fibronectin, is incorporated into fibrils. Thus, the blastocoel roof of Xenopus represents a valid model system for the study of fibronectin fibril formation in situ. Moreover, we show that fibril formation can be induced experimentally in this system. Examination of fibril elongation by double-labelling experiments reveals that individual, unbranched fibronectin fibrils grow only at one end, i.e. in a unipolar fashion. The rate of elongation is 4.7 microns/min. Most fibrils grow only for a short time, and the increase in total fibril length per cell is driven by the repeated initiation of new fibrils. Assembly of fibronectin into fibrils precedes cross-linking of fibronectin into multimers in this system.
Winklbauer
R
R
Max-Planck-Institut für Entwicklungsbiologie, Tübingen, Germany.
Stoltz
C
C
D000818:Animals; D001755:Blastocyst / Q000166:cytology / Q000187:drug effects / Q000502:physiology*; D003571:Cytochalasin B / Q000494:pharmacology; D004625:Embryo, Nonmammalian / Q000166:cytology / Q000502:physiology*; D005353:Fibronectins / Q000096:biosynthesis / Q000502:physiology* / Q000648:ultrastructure; D009842:Oligopeptides / Q000494:pharmacology; D014508:Urea; D014982:Xenopus laevis
D005353:Fibronectins; D009842:Oligopeptides; D003571:Cytochalasin B; C047981:arginyl-glycyl-aspartic acid; D014508:Urea; C058161:glycyl-arginyl-glycyl-aspartyl-seryl-proline; C058347:glycyl-arginyl-glycyl-glutamyl-seryl-proline