F. Zito et al., Regulative specification of ectoderm in skeleton disrupted sea urchin embryos treated with monoclonal antibody to PI-nectin, DEVELOP GR, 42(5), 2000, pp. 499-506
PI-nectin is a glycoprotein first discovered in the extracellular matrix (E
CM) of Paracentrotus lividus sea urchin embryo, apically located on ectoder
m and endoderm cells, The molecule has been described as functioning as an
adhesive substrate for embryonic cells and its contact to ectoderm cells is
essential for correct skeletogenesis. The present study was undertaken to
elucidate the biochemical characteristics of PI-nectin and to extend knowle
dge on its in vivo biological function. Here it is shown that the binding o
f mesenchyme blastula cells to PI-nectin-coated substrates was calcium depe
ndent, and reached its optimum at 10mM Ca2+. Perturbation studies using mon
oclonal antibody (McAb) to PI-nectin, which prevent ectoderm cell-PI-nectin
contact, show that dorsoventral axis formation and ectoderm differentiatio
n were retarded. At later stages, embryos recovered and, even if growth and
patterning of the skeleton was greatly affected, the establishment of dors
oventral asymmetry was reached. Similarly, the expression of specific ectod
erm and endoderm territorial markers was achieved, although occurring with
some delay. Endoderm differentiation and patterning was not obviously affec
ted. These results suggest that both endoderm and ectoderm cells have regul
ative capacities and differentiation of territories is restored after a lag
period. On the contrary, failure of inductive differentiation of the skele
ton cannot be rescued, even though the ectoderm has recovered.