Fibronectin-plasma membrane interaction in the adhesion of hemopoietic cells.
Open Access
- 31 July 1986
- journal article
- research article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 103 (2) , 429-437
- https://doi.org/10.1083/jcb.103.2.429
Abstract
Many hemopoietic cell lines were examined for their ability to adhere to culture dishes coated with extracellular matrix proteins. Adhesion assay was performed with murine and human leukemic cell lines representative of different stages of differentiation along both erythroid and myeloid lineages. All the hemopoietic cell lines tested adhered to fibronectin but not to laminin, types I, III, and IV collagen, serum-spreading factor, and cartilage proteoglycans. In addition to immortalized cell lines, immature erythroid and myeloid mouse bone marrow cells adhered to fibronectin. To define the fibronectin region involved in hemopoietic cell adhesion, proteolytic fragments, monoclonal antibodies, and synthetic peptides were used. Among different fibronectin fragments tested, only a 110-kD polypeptide, corresponding to the fibroblast attachment domain, was active in promoting adhesion. Moreover, a monoclonal antibody to the cell binding site located within this domain prevented hemopoietic cell adhesion. Finally, the tetrapeptide Arg-Gly-Asp-Ser, which corresponds to the fibronectin sequence recognized by fibroblastic cells, specifically and competitively inhibited attachment of hemopoietic cells to this molecule. The cell surface molecule involved in the interaction of mouse hemopoietic cells with fibronectin was identified as a 145,000-D membrane glycoprotein by adhesion-blocking antibodies. This glycoprotein was found to be antigenically and functionally related to the GP135 membrane glycoprotein involved in the adhesion of fibroblasts to fibronectin (Giancotti, F. G., P. M. Comoglio, and G. Tarone, 1986, Exp. Cell Res., 163:47-62). On the basis of these data, we conclude that interaction of hemopoietic cells with fibronectin involves a specific fibronectin sequence and a 145,000-D cell surface glycoprotein. We speculate that this property might be relevant for the interaction of hemopoietic cells with the bone marrow stroma, which represents the natural site of hemopoiesis.This publication has 41 references indexed in Scilit:
- A 135000 molecular weight plasma membrane glycoprotein involved in fibronectin-mediated cell adhesionExperimental Cell Research, 1986
- Selective Inhibition of Fibronectin-Mediated Cell Adhesion by Monoclonal Antibodies to a Cell-Surface GlycoproteinScience, 1985
- Elution of fibronectin proteolytic fragments from a hydroxyapatite chromatography column. A simple procedure for the purification of fibronectin domainsEuropean Journal of Biochemistry, 1985
- Loss of Adhesion of Murine Erythroleukemia Cells to Fibronectin During Erythroid DifferentiationScience, 1984
- Role of anchorin CII, a 31,000-mol-wt membrane protein, in the interaction of chondrocytes with type II collagen.The Journal of cell biology, 1984
- Collagen synthesis by bone marrow stromal cells: a quantitative studyBritish Journal of Haematology, 1982
- Monoclonal Antibodies Which Alter the Morphology of Cultured Chick Myogenic CellsJournal of Cellular Biochemistry, 1982
- Identification and partial characterization of five major membrane glycoproteins of BHK fibroblastsThe Journal of Membrane Biology, 1980
- Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications.Proceedings of the National Academy of Sciences, 1979
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970