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Rat hepatocytes attach to laminin present in liver biomatrix proteins by an Mg ++ ‐dependent mechanism
Author(s) -
De Lourdes Ponce Maria,
Rojkind Marcos
Publication year - 1995
Publication title -
hepatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.488
H-Index - 361
eISSN - 1527-3350
pISSN - 0270-9139
DOI - 10.1002/hep.1840220236
Subject(s) - laminin , fibronectin , extracellular matrix , cell adhesion , adhesion , integrin , chemistry , cell adhesion molecule , biochemistry , extracellular , cell , microbiology and biotechnology , biology , organic chemistry
Laminin belongs to a family of proteins that contains at least seven variants. Together with fibronectin, it is the most important cell‐adhesion protein. Recent data from various laboratories have suggested that liver sinusoidal laminins differ from Engelbert‐Holmes‐Swarm tumor laminin (laminin 1), because the former contain α2 instead of α1 chains. Therefore, we compared the adhesion of hepatocytes to laminin 1 and a matrix extracted with dilute acetic acid from liver biomatrix (LBP). We show that LBP contains laminin and that this extracellular matrix protein is the main adhesion protern. Close to 70% of the hepatocytes attach to LBP after 15 minutes of incubation at 37°C. Cell adhesion was Mg ++ and Mn ++ ‐dependent and Ca ++ ‐ and insulin‐independent. Ethylenediaminetetraacetic acid prevented cell adhesion in the presence of divalent cations. We show that synthetic cell‐adhesion peptide sequences present in laminin 1 (RGD and YIGSR) or an antibody to the cellbinding domain (SIKVAV) of the α chain do not prevent hepatocyte adhesion to LBP. We also show that LBP has cell specificity; hepatocytes adhere to it preferentially when compared with other epithelial and mesenchymal cell lines. We suggest that because of the differences in chain composition of laminin 1 and liver sinusoidal laminins as well as the described differences in cell adhesion to the two substrata, further studies are needed to determine the actual composition of liver laminin and establish the chains and domains to which hepatocytes adhere. (Hepatology 1995;22:620–628.)