TY - JOUR
T1 - Involvement of blood-group-B-active trisaccharides in Ca2+-dependent cell-cell adhesion in the Xenopus blastula
AU - Nomura, Kazuko H.
AU - Kobayashi, Ryuji
AU - Hirabayashi, Yoshio
AU - Fujisue-Sakai, Megumi
AU - Mizuguchi, Souhei
AU - Nomura, Kazuya
N1 - Funding Information:
&p.2: wledgements We thank H. Nomura, N. Nakajo and J. Iwa-shita for their help in an earlier phase of our study; M. Murata and K. Yamana for helpful discussion; A. P. Turner, J. Heasman and C.C. Wylie for introducing us to glycobiology; K. Yamamoto for giving us A-and B-substance and A. Suzuki for the generous gift of anti-GM1 antibody. This work was supported by Sasakawa Scientific Research Grant to K. H. N., by Grants-in-Aid for Scientific Research from the Ministry of Education, Science, Sports and Culture, and by The Cosmetology Research Foundation Grant to K. N.
PY - 1998
Y1 - 1998
N2 - Despite their wide distribution in various organisms, no physiological roles have been proposed for the human blood-group-ABO (ABH)-active trisaccharides. Here we show that monoclonal antibodies against human blood-group-B-active trisaccharides (B-substance) completely block the Ca2+-dependent cell-cell adhesion system of frog (Xenopus laevis) embryonic cells. Synthetic B-substance or B-active glycopeptides also disrupt the Ca2+-dependent cell-cell adhesion. These results suggest that blood-group-B-active substances play a role in cell-cell adhesion. Blood-group-B-active substances were found as glycoproteins and as glycosphingolipids. In order to identify B-active glycoproteins active in cell-cell adhesion, we purified B-active membrane glycoproteins by two-dimensional electrophoresis and found that they are 45- to 58-kDa proteins with pI(s) ranging from 4.0 to 5.3. They are glycosylphosphatidyl inositol (GPI) anchored. Amino acid sequence analysis showed that the purified B-active GPI-anchored proteins are homologues of soluble Xenopus cortical granule lectins (CGL). The results suggest that the B-active membrane glycoproteins are GPI-anchored forms of the lectin and are directly involved in frog Ca2+-dependent cell-cell adhesion.
AB - Despite their wide distribution in various organisms, no physiological roles have been proposed for the human blood-group-ABO (ABH)-active trisaccharides. Here we show that monoclonal antibodies against human blood-group-B-active trisaccharides (B-substance) completely block the Ca2+-dependent cell-cell adhesion system of frog (Xenopus laevis) embryonic cells. Synthetic B-substance or B-active glycopeptides also disrupt the Ca2+-dependent cell-cell adhesion. These results suggest that blood-group-B-active substances play a role in cell-cell adhesion. Blood-group-B-active substances were found as glycoproteins and as glycosphingolipids. In order to identify B-active glycoproteins active in cell-cell adhesion, we purified B-active membrane glycoproteins by two-dimensional electrophoresis and found that they are 45- to 58-kDa proteins with pI(s) ranging from 4.0 to 5.3. They are glycosylphosphatidyl inositol (GPI) anchored. Amino acid sequence analysis showed that the purified B-active GPI-anchored proteins are homologues of soluble Xenopus cortical granule lectins (CGL). The results suggest that the B-active membrane glycoproteins are GPI-anchored forms of the lectin and are directly involved in frog Ca2+-dependent cell-cell adhesion.
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U2 - 10.1007/s004270050148
DO - 10.1007/s004270050148
M3 - Article
C2 - 9518520
AN - SCOPUS:0031961065
SN - 0949-944X
VL - 208
SP - 9
EP - 18
JO - Development Genes and Evolution
JF - Development Genes and Evolution
IS - 1
ER -