Weg. Muller et al., Towards an understanding of the molecular basis of immune responses in sponges: The marine demosponge Geodia cydonium as a model, MICROSC RES, 44(4), 1999, pp. 219-236
The phylogenetic position of the phylum Porifera (sponges) is near the base
of the kingdom Metazoa. During the last few years, not only rRNA sequences
but, more importantly, cDNA/genes that code for proteins have been isolate
d and characterized from sponges, in particular from the marine demosponge
Geodia cydonium. The analysis of the deduced amino acid sequences of these
proteins allowed a molecular biological approach to the question of the mon
ophyly of the Metazoa. Molecules of the extracellular matrix/basal lamina,
with the integrin receptor, fibronectin, and galectin as prominent examples
, and of cell-surface receptors (tyrosine kinase receptor), elements of sen
sory systems (crystallin, metabotropic glutamate receptor) as well as homol
ogs/modules of an immune system (immunoglobulin-like molecules, scavenger r
eceptor cysteine-rich [SRCR]- and short consensus repeats [SCR]-repeats), c
lassify the Porifera as true Metazoa. As living fossils, provided with simp
le, primordial molecules allowing cell-cell and cell-matrix adhesion as wel
l as processes of signal transduction as known in a more complex manner fro
m higher Metazoa, sponges also show pecularities not known in later phyla.
In this paper, the adhesion molecules presumably involved in the sponge imm
une system are reviewed; these are the basic adhesion molecules (galectin,
integrin, fibronectin, and collagen) and especially the highly polymorphic
adhesion molecules, the receptor tyrosine kinase as well as the polypeptide
s comprising scavenger receptor cysteine-rich (SRCR) and short consensus re
peats (SCR) modules. In addition, it is reported that in the model sponge s
ystem of G. cydonium, allogeneic rejection involves an upregulation of phen
ylalanine hydroxylase, an enzyme initiating the pathway to melanin synthesi
s. Microsc. Res. Tech. 44:218-236, 1999. (C) 1999 Wiley-Liss, Inc.