The attachment of nematocytes from the primitive invertebrate Hydra to fibronectin is specific and RGD-dependent.
The transient attachment of cells to components of the extracellular matrix is an important step in the complex molecular mechanisms involved in amoeboid cell locomotion. We have analyzed the attachment of nematocytes from the freshwater cnidarian Hydra to fibronectin which is a constituent of the mesoglea, the extracellular matrix, of the polyps. The percentage of attaching cells increased gradually in a concentration-dependent manner and reached a plateau value at a fibronectin concentration of 50 micrograms/ml. Attachment was inhibited by exposure of the fibronectin-coated surfaces to antibodies against the cell binding domain of fibronectin or by incubating the cells with peptides containing the recognition sequence Arg-Gly-Asp (RGD) known from vertebrate cells. This, together with data obtained by affinity chromatography, indicates that RGD-dependent binding to fibronectin, mediated by a receptor which possibly belongs to the integrin family, already occurs in Hydra, a member of an evolutionary low invertebrate phylum.
Ziegler
U
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Department of Zoology, University of Zürich, Switzerland.
Stidwill
R P
RP
D000595:Amino Acid Sequence; D000818:Animals; D015153:Blotting, Western; D002465:Cell Movement; D002846:Chromatography, Affinity; D005109:Extracellular Matrix / Q000378:metabolism*; D005353:Fibronectins / Q000037:antagonists & inhibitors / Q000378:metabolism*; D006829:Hydra; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000378:metabolism*; D017469:Receptors, Fibronectin / Q000302:isolation & purification / Q000378:metabolism*
D005353:Fibronectins; D009842:Oligopeptides; D017469:Receptors, Fibronectin; C047981:arginyl-glycyl-aspartic acid