1. The shift from unicellular life to multicellular, integrated organi
sms has been accompanied by the acquisition of adhesion proteins. Rece
ntly we succeeded in cloning some genes coding for such proteins from
the lowest multicellular animals, the marine sponges (model: the silic
eous sponge Geodia cydonium). 2. G. cydonium contains several lectins
and cDNA for two of them (termed LECT-1 and LECT-2) was cloned. Both l
ectins have a framework sequence of 38 conserved amino acids which are
characteristic for the carbohydrate-binding site of vertebrate S-type
lectins. Next, we have isolated and characterized a cDNA coding for a
receptor tyrosine kinase of class II (GCTK). The deduced amino acid s
equence shows two characteristic domains: i) the tyrosine kinase domai
n and ii) an immunoglobulin-like domain. The latter part shows high ho
mology to the vertebrate type immunoglobulin domain. This result, toge
ther with the lectin data, demonstrates that binding domains of such a
dhesion proteins are not recent achievements of higher animals but exi
st already in animals (sponges) which have diverged from other organis
ms about 800 million years ago. 3. Considering the fact that during em
bryogenesis of sponges a typical anteroposterior organization pattern
is seen, a ''homeotic'' organ-like transformation has been postulated.
The subsequent search for genes provided with the homeodomain sequenc
e was successful. The deduced amino acid sequence of G. cydonium showe
d high homology to chicken and to the Antennapedia sequence from Droso
phila melanogaster. 4. These data support the view that the kingdom An
imalia is of monophyletic origin.