P. Marschal et al., XENOPUS-LAEVIS L-14 LECTIN IS EXPRESSED IN A TYPICAL PATTERN IN THE ADULT, BUT IS ABSENT FROM EMBRYONIC-TISSUES, Glycobiology, 4(3), 1994, pp. 297-305
Soluble, dimeric, lactose-binding lectins with subunit Mr of similar t
o 14-16 x 10(3), here called L-14s, are expressed in multiple tissues
in all vertebrates that have been examined. L-14s have particular affi
nity for polylactosamine chains on laminin, co-localize with laminin i
n some basement membranes, and influence adhesion to laminin and proli
feration for some cultured cells. In previous studies of mammals and c
hickens, L-14s have been found at high levels in a variety of adult ti
ssues, such as muscle and peripheral nerve, but at much higher levels
in many embryonic tissues, suggesting a special role in development. T
o further explore possible roles of L-14 in embryogenesis, we have stu
died the expression of L-14 in embryonic and adult Xenopus laevis tiss
ues. Except for the abundant L-14 in poison glands in adult Xenopus sk
in, we find that Xenopus L-14 is expressed in the same general distrib
ution as its mammalian homologues. However, we could detect no express
ion of L-14 in Xenopus embryos using either a sensitive immunoassay fo
r the protein or a sensitive RNase protection assay for its mRNA. Furt
hermore, use of affinity chromatography to identify other lactose-bind
ing lectins in embryonic tissue revealed only scarce proteins with hig
her subunit molecular weights. These results suggest that in X.laevis
L-14 functions in adult tissues and is not involved in embryogenesis.