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Evolution of Cell Adhesion Systems: Evidence for Arg‐Gly‐Asp‐Mediated Adhesion in the Protozoan Neoparamoeba aestuarina
Author(s) -
CUSTODIO MARCIO R.,
IMSIECKE GEORG,
BOROJEVIC RADOVAN,
RINKEVICH BARUCH,
ROGERSON ANDREW,
MÜLLER WERNER E. G.
Publication year - 1995
Publication title -
journal of eukaryotic microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.067
H-Index - 77
eISSN - 1550-7408
pISSN - 1066-5234
DOI - 10.1111/j.1550-7408.1995.tb01623.x
Subject(s) - biology , amoeba (genus) , fibronectin , adhesion , extracellular matrix , cell adhesion , laminin , microbiology and biotechnology , cell adhesion molecule , protozoa , tetrahymena , cell , multicellular organism , biochemistry , chemistry , organic chemistry
. Developmental processes in multicellular organisms require structural elements, such as adhesion molecules, to stabilize cells at functional positions. In vertebrates, a series of extracellular matrix proteins, e.g. fibronectin and laminin are involved in cell adhesion. These proteins contain Arg‐Gly‐Asp [RGD] at their binding sites. Here we show that at concentrations above 2 mM the peptide GRG D SPK, comprising the tripeptide RGD (Arg‐Gly‐Asp), prevents the adhesiveness of cells of the marine amoeba Neopar‐amoeba aestuarina. In addition, elevated levels of GRG D SPK cause cells to alter their shapes from those with digitiform subpseudopodia to rounded cells with small lobed pseudopodia. These cells detach from the substratum. These results are specific for the RGD sequence, because incubation in GRG E SPK solution at the same concentrations had no effect on cell attachment or structure. From these data we suggest that the structural adhesion molecules identified in vertebrates shows amino acid homologies with those found in unicellular protozoa.