Abstract

The synthetic peptide Gly-Arg-Gly-Asp-Ser (GRGDS) (which corresponds to a fragment of fibronectin and contains its cell adhesion sequence RGD) caused degranulation and spreading of monolayers of isolated granular haemocytes of the crayfish Pacifastacus leniusculus in vitro. When coated on glass coverslips, this RGD-containing peptide could mediate cell attachment of granular cells in vitro. A control peptide, Gly-Arg-Gly-Glu-Ser (GRGES), did not have these activities. Thus, GRGDS imitates the biological activities in vitro of the cell adhesion factor recently purified from crayfish haemocytes. This suggests that the sequence Arg-Gly-Asp (RGD), which is responsible for the cell adhesion activities of a number of vertebrate proteins, may also be involved in degranulation and cell adhesion of arthropod haemocytes. This is the first report describing direct activities by an RGD-containing peptide towards invertebrate cells in vitro, and the first indication of the presence of an RGD-recognizing receptor on invertebrate haemocytes.

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