Fibronectins: multifunctional modular glycoproteins.
Open Access
- 1 November 1982
- journal article
- review article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 95 (2), 369-377
- https://doi.org/10.1083/jcb.95.2.369
Abstract
Fibronectins are large glycoproteins that have been implicated in a wide variety of cellular properties, particularly those involving the interactions of cells with extracellular materials. These properties include cell adhesion, morphology, cytoskel- etal organization, migration, differentiation, oncogenic trans- formation, phagocytosis, and hemostasis. During the past sev- eral years, investigations in many laboratories have analyzed the expression, functions, and structure of fibronectins. These studies have revealed that fibronectins have a complex molec- ular structure consisting of multiple specific binding sites, and the complex biological phenomena in which fibronectins par- ticipate can now be considered in terms of this structure. In this brief article we will review the current understanding of the structure and properties of fibronectins. Because a number of comprehensive reviews on various aspects of fibro- nectins have been published (1-13), we shall focus on overall concepts, recent developments and promising future research directions in this rapidly expanding field. Sources of Fibronectins In vivo, fibronectins are found in body fluids (300 #g/ml in plasma, lesser amounts in other fluids), soft connective tissue matrices, and most basement membranes. Fibronectins are synthesized by a wide variety of cells in vitro (Table I). Fibroblasts and endothelial cells are major producers, but many other cell types, including some epithelial cells, synthe- size fibronectin at lower levels. There are at least two types of fibronectin, termed plasma and cellular fibronectins, although there may well be multiple forms of cellular fibronectin. Cel- lular and plasma fibronectins, although distinguishable, are very similar in structure and properties (see below). One major source of plasma fibronectin appears to be hepatocytes (14, 15) x although endothelial cells (16-18) and macrophages (19-22) could also contribute, given their close association with the bloodstream.Keywords
This publication has 99 references indexed in Scilit:
- Occurrence of Fibronectin on the Primary Mesenchyme Cell Surface During Migration in the Sea Urchin EmbryoDifferentiation, 1982
- Shapes, domain organizations and flexibility of laminin and fibronectin, two multifunctional proteins of the extracellular matrixJournal of Molecular Biology, 1981
- Primary cultures of rat hepatocytes synthesize fibronectinBiochemical and Biophysical Research Communications, 1979
- Fibronectin alters the phenotypic properties of cultured chick embryo chondroblastsCell, 1979
- Lack of correlation between the decreased expression of cell surface LETS protein and tumorigenicity in human cell hybridsCell, 1978
- TRANSMEMBRANE LINKAGE OF FIBRONECTIN TO INTRACELLULAR ACTIN‐CONTAINING FILAMENTS IN CULTURED HUMAN FIBROBLASTS*Annals of the New York Academy of Sciences, 1978
- A LARGE GLYCOPROTEIN LOST FROM THE SURFACES OF TRANSFORMED CELLS*Annals of the New York Academy of Sciences, 1978
- TRANSFORMATION‐SENSITIVE CELL SURFACE PROTEIN: ISOLATION, CHARACTERIZATION, AND ROLE IN CELLULAR MORPHOLOGY AND ADHESIONAnnals of the New York Academy of Sciences, 1978
- In vitro traits of adenovirus-transformed cell lines and their relevance to tumorigenicity in nude miceCell, 1977
- Dimeric character of fibronectin, a major cell surface-associated glycoproteinBiochemical and Biophysical Research Communications, 1977