Glycobiology vol 6 no 8 pp. 785-793, 1996
© 1996
research-article |
A galectin links the aggregation factor to cells in the sponge (Geodia cydonium) system
Institut für Physiologische Chemie, Universität Duesbergweg 6, D-55099 Mainz, Germany
1Departamento de Bioquimica, Instituto de Quimica, Centro de Tecnologia, Universidade Federal do Rio de Janeiro 21941-900 Rio de Janeiro, Brazil
2To whom correspondence should be addressed at: Institut für Physiologische Chemie, Universität, Duesbergweg 6, D-55099 Mainz, Germany
Received on March 13, 1996; revised on June 24, 1996; accepted on July 5, 1996
The cDNA for the full-length lectin from the marine sponge Geodia cydonium was cloned. Analysis of the deduced aa sequence revealed that this lectin belongs to the group of galectins. The full-length galectin, which was obtained also in a recombinant form, has an Mr of 20,877; in the processed form it is a 15 kDa polypeptide. The enriched aggregation factor from G.cydonium also was determined to contain, besides minimal amounts of the galectin, a 140 kDa polypeptide which is involved in cell-cell adhesion. Monoclonal antibodies have been raised against this protein; Fab' fragments prepared from them abolished cell-cell reaggregation. Cell reaggregation experiments revealed that the aggregation factor is an essential component in the aggregation process but it requires likewise the presence of the galectin. Antibodies against the galectin blocked the aggregation factor-mediated cell adhesion. A plasma membrane component was identified (a 29 kDa polypeptide) which interacted with the aggregation factor in the presence of galectin; binding could be blocked both by antibodies against the galectin as well as against the aggregation factor. Immunohistochemical analysis revealed that spherulous cells contain the galectin but not the aggregation factor. By laser scanning microscopy, it is shown that both the aggregation factor and the galectin are located at the rim of the cells. From these data we conclude that the G.cydonium aggregation factor binds to the cells via a galectin bridge.
galectin aggregation factor Geodia cydonium sponage cell adhesion
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