TY - JOUR
T1 - Tissue fibronectin is an endogenous ligand for galectin-1
AU - Ozeki, Yasuhiro
AU - Matsui, Taei
AU - Yamamoto, Yoshinobu
AU - Funahashi, Masanori
AU - Hamako, Jiharu
AU - Titani, Koiti
N1 - Funding Information:
We thank Dr Stephen Anderson (The Biomembrane Institute at Seattle) for scientific editing of the manuscript. This work was supported by a Grants-in-Aid for Scientific Research from the Ministry of Education, Science and Culture of Japan, and from the Fujita Health University.
PY - 1995/3
Y1 - 1995/3
N2 - A 14K β-galactoside-binding lecttn (galectin-1) is present in many animal tissues. In a search for endogenous ligands, we surveyed galectin-1-binding proteins in human placenta. Extract of human placenta with 2 M urea was applied to a Sepharose 4B column conjugated with galectin-1 purified from frog (Rana catesbeiana) eggs. Two major proteins eluted with 100 mM lactose from the column-bound fraction showed apparent molecular masses of 220 and 180 kDa on SDS-PAGE under reducing conditions. Western blotting analysis using monoclonal antibodies indicated that these proteins were fibronectin and laminin, respectively. Most placenta] and amniotic fibronectins bound strongly to the column, whereas almost all plasma fibronectin passed through the column. The galectin-1, fibronectin and laminin were immunohistochemically shown to be co-localized in the extracellular matrix of placental tissue. In a cell attachment assay, rhabdosarcoma cells adhered to a plate coated with placental fibronectin, even in the presence of GRGDS peptide, if galectin-1 were also present This adhesive effect of galectin-1 was inhibited by lactose. These results indicate that tissue fibronectin, as well as laminin, serve as endogenous ligands for galectin-1, suggesting that galectin-1 may play a role in assembly of the extracellular matrix, or in the control of cell adhesion based on lectin-extracellular matrix interaction.
AB - A 14K β-galactoside-binding lecttn (galectin-1) is present in many animal tissues. In a search for endogenous ligands, we surveyed galectin-1-binding proteins in human placenta. Extract of human placenta with 2 M urea was applied to a Sepharose 4B column conjugated with galectin-1 purified from frog (Rana catesbeiana) eggs. Two major proteins eluted with 100 mM lactose from the column-bound fraction showed apparent molecular masses of 220 and 180 kDa on SDS-PAGE under reducing conditions. Western blotting analysis using monoclonal antibodies indicated that these proteins were fibronectin and laminin, respectively. Most placenta] and amniotic fibronectins bound strongly to the column, whereas almost all plasma fibronectin passed through the column. The galectin-1, fibronectin and laminin were immunohistochemically shown to be co-localized in the extracellular matrix of placental tissue. In a cell attachment assay, rhabdosarcoma cells adhered to a plate coated with placental fibronectin, even in the presence of GRGDS peptide, if galectin-1 were also present This adhesive effect of galectin-1 was inhibited by lactose. These results indicate that tissue fibronectin, as well as laminin, serve as endogenous ligands for galectin-1, suggesting that galectin-1 may play a role in assembly of the extracellular matrix, or in the control of cell adhesion based on lectin-extracellular matrix interaction.
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U2 - 10.1093/glycob/5.2.255
DO - 10.1093/glycob/5.2.255
M3 - Article
C2 - 7780201
AN - SCOPUS:0028945453
SN - 0959-6658
VL - 5
SP - 255
EP - 261
JO - Glycobiology
JF - Glycobiology
IS - 2
ER -