Plasma membrane glycoprotein which mediates adhesion of fibroblasts to collagen

Pearlstein, Edward

doi:10.1038/262497a0

Cited by 371 publications

(117 citation statements)

References 16 publications

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“…The physiologic role of FN in tissues has been inferred from its effects on cultured cells. FN is necessary for the attachment of tissue culture cells to culture vessels (19)(20)(21)(22). FN also increases the strength of attachment of transformed cells to culture vessels and thus changes their morphology (though not their growth characteristics and malignant potential) (24,25).…”

Section: Discussionmentioning

confidence: 99%

Synthesis of fibronectin by cultured human endothelial cells.

Jaffe¹,

Mosher²

1978

The Journal of Experimental Medicine

448

113

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Plasma fibronectin is probably the major nonimmune particulate opsonin in blood and is cross-linked to fibrin during the final stage of blood coagulation. Fibronectin also occurs in an insoluble form in basement membranes especially those underlying endothelial cells and in loose connective tissue. Fibronectin was demonstrated in cultured human endothelial cells and in the surrounding extracellular matrix by immunofluorescence microscopy by using antibody to human plasma fibronectin. Cultured human endothelial cells released fibronectin into the culture medium which was immunologically identical to the fibronectin in human plasma. Cultured human endothelial cells were labeled with [3H] leucine. The radioactive fibronectin present in the endothelial postculture medium and in urea extracts of cellular monolayers was isolated with either anti-fibronectin coupled to Protein A-Sepharose or double antibody immunoprecipitation and characterized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. When reduced, the [3H] fibronectin synthesized by cultured endothelial cells had the same mol wt (approximately 200,000) as plasma fibronectin. Unreduced, the [3H] fibronectin synthesized by endothelial cells migrated as a dimer, as did plasma fibronectin. Fibronectin accounted for approximately 15% of the protein synthesized and released by endothelial cells into the culture medium. Thus, cultured endothelial cells synthesize fibronectin, secrete it into the culture medium, and incorporate it into extracellular matrix. The results suggest that the endothelial cell is potentially a major site of synthesis of circulating plasma fibronectin. In addition, fibronectin derived from endothelial cells may be an important structural component of the subendothelium.

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Section: Discussionmentioning

confidence: 99%

Synthesis of fibronectin by cultured human endothelial cells.

Jaffe¹,

Mosher²

1978

The Journal of Experimental Medicine

448

113

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“…Third, the appearance of fibronectin on cells in.culture is dependent on cell-cell contact (18). Fourth, fibronectin mediates the adhesion of fibroblasts in culture to collagen (19,20 showed that fibronectin appears underneath the cells (35,36), but fibronectin also appears in a fibrillar network over the cell surface (18,30,35,36 (15)(16)(17)(18). For vascular endothelial cells, our results also suggest that fibronectin is involved in cell-substrate adhesion and, furthermore, the large amount of fibronectin in the extracellular matrix of these cells may be responsible for their flattened and contact-inhibited morphology.…”

Section: Methodsmentioning

confidence: 99%

“…in cell-cell and cell-substrate adhesion (15)(16)(17)(18), possibly by interacting with collagen (19,20), we have been studying the association of fibronectin with the extracellular matrix of vascular endothelial cells. In this paper we report on the formation of basement membrane-like material (extracellular matrix) in a cloned line of adult bovine aortic endothelial (ABAE) cells that we have recently characterized (21), and we also show that fibronectin is a major component of the extracellular matrix produced by ABAE cells.…”

mentioning

confidence: 99%

Identification, localization, and role of fibronectin in cultured bovine endothelial cells.

Birdwell¹,

Gospodarowicz²,

Nicolson³

1978

Proc. Natl. Acad. Sci. U.S.A.

235

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We have examined bovine aortic endothelial cell cultures for the presence of fibronectin, a high molecular weight cell-surface glycoprotein. Sparse cultures contain fibronectin only on dorsal cell surfaces at regions of cell-cell contact, as detected by immunofluorescence. In contrast, when the endothelial cells reached confluence as a highly contactinhibited monolayer, fibronectin was detected in an extracellular matrix underneath the cell monolayer but not on top of the monolayer. Sodium dodecyl sulfate/polyacrylamide gel electrophoresis of isolated extracellular matrix revealed that a predominant component of the matrix is a protein of approximately 2.3 X 105 molecular weight,.which has been identified as fibronectin.The vascular endothelium exists as a monolayer of highly flattened and contact-inhibited cells; because of their location at the interface between blood and tissue, endothelial cells are the chief elements involved in the permeability of blood vessels (1, 2). Although the side of the vascular endothelium exposed to the bloodstream is nonthrombogenic, the subendothelial matrix on which the cells rest is very thrombogenic (3,4). Thus, a disruption of the vascular endothelium can expose the underlying basement membrane, resulting.in the aggregation of platelets and thrombus formation. Therefore, factors that are involved in the attachment of endothelial cells to the basement membrane are very important for the proper functioning of the vascular endothelium.Biochemical analyses have established that basement membranes possess a highly cross-linked form of collagen (5), rendering basement membranes completely insoluble under physiological conditions. Although most biochemical studies of basement membranes have dealt with the structure and synthesis of collagen, noncollagenous matrix glycoproteins have also been found in some basement membranes (6). Recent studies indicate that one of these glycoproteins may be identical to fibronectin (7), a major cell-surface glycoprotein that is immunologically identical to cold-insoluble globulin (8), a plasma protein which is presumably the plasma form of fibronectin that is shed from cells into the blood. Fibronectin appears to be similar, if not identical, to the large external transformationsensitive (LETS) protein, which exists on the surface of certain untransformed cells, but not on the surface of transformed cells (9)(10)(11) (21), and we also show that fibronectin is a major component of the extracellular matrix produced by ABAE cells. METHODSCell Culture. The cloning, culturing, and characterization of ABAE cells have been described (21). ABAE cells are identified as endothelial cells on the basis of their morphology and ultrastructure and on their ability to synthesize Factor VIII (antihemophilic factor antigen), a marker for endothelial cells (22). These cells are routinely maintained in fibroblast growth factor (23).Electron Microscopy. Cells were prepared for electron microscopy by described methods (24), and then examined in a Hitachi S-500 ...

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“…It binds to collagen [3] and mediates adhesion of cells to collagen-coated surfaces [4][5][6][7]. The abundance of fibronectin in basement membrane structures [8] has led to the suggestion iLhat its in vivo function may be to attach cells to the extracellular matrix.…”

Section: Introductionmentioning

confidence: 99%