Identification and isolation of a collagen-binding fragment of the adhesive glycoprotein fibronectin.

Hahn, Liang-Hsien E.; Yamada, Kenneth M.

doi:10.1073/pnas.76.3.1160

Cited by 110 publications

(38 citation statements)

References 30 publications

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“…A fragment of 40,000 daltons near the amino-terminus contains the collagen-binding site, whereas another fragment of -160,000 daltons binds to the cell surface (11,12,57,66,83,145,196,210) . The 160,000dalton fragment does not bind to collagen but can promote cell adhesion to plastic, whereas the collagen-binding fragment (40,000 daltons) lacks cell-attachment activity (83,84,196) . One report describes a 50,000-dalton peptide from fibronectin that can both bind to collagen and mediate cell adhesion (66) .…”

Section: Fibronectinmentioning

confidence: 99%

Role of collagenous matrices in the adhesion and growth of cells.

Kleinman¹,

Klebe²,

Martin³

1981

The Journal of Cell Biology

1,291

434

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It has long been appreciated that, for many types of cells, attachment to a substrate is required for their replication. Collagen substrates enhance the growth (64,70,109,238) as well as the differentiation (40,69,85,86,146,161,184), of many cells in culture above that observed with other substrates such as plastic and glass. As discussed in this report, many cultured cells including fibroblasts, myoblasts, hepatocytes, chondrocytes, and certain epithelial cells are thought not to bind directly to the collagen substrate or to the plastic surface of culture dishes (31,73,74,76,77,89,93,113,164,220) . Instead, extracellular glycoproteins bind the cells to the substrate. One of these attachment proteins, fibronectin, has been extensively studied (99,151,166,227,228,244) . Fibronectin is produced by fibroblasts (13,197,246) and endothelial cells (102, 140) as well as some other cell types . It is also present in high concentrations in blood and serum (152) . In culture, serum fibronectin, as well as that produced by the cells, can bind to both the collagen substrates and the tissue culture plastic surface and mediate the attachment of cells (73,113,164,242) . Circulating fibronectin participates in a variety of reactions important to wound healing, including the adhesion and spreading of platelets on collagen (10, 14, 75, 100, 204), binding to the fibrin clot (74,150,198) and to collagen (37,46,94,103,119), promoting opsonization reactions by phagocytic cells (18,94,201), and promoting fibroblast migration (6, 61) . Thus, fibronectin not only functions as an attachment protein, but also may play an important role in repair reactions .In the case of certain differentiated cells, such as chondrocytes (89) and epithelial cells (159, 220), glycoproteins different from fibronectin are active in attachment. The components of these extracellular matrices of fibroblasts, chondrocytes, and epithelial cells differ with the cell type, and they require separate attachment proteins to provide additional specificity to the interaction of the cell with its matrix. Alterations in cellsubstratum interactions are observed in differentiating cells and after spontaneous transformation of cells or exposure to oncogenic agents (99,228) . This review will briefly outline our current knowledge of the types of collagen and their distribution and biosynthesis. Then, the interaction of cells with col-REVIEW

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Section: Fibronectinmentioning

confidence: 99%

Role of collagenous matrices in the adhesion and growth of cells.

Kleinman¹,

Klebe²,

Martin³

1981

The Journal of Cell Biology

1,291

434

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“…Thus, a part of the labeling of the cell membrane with 3H-mannose may represent fibronectin. Fibronectin has specific high-affinity binding sites for a variety of macromolecules, including collagen, cell membrane components, fibrinogen, heparin, hyaluronic acid, actin, and transglutaminase (Hahn and Yamada, 1979;Keski-Oka et al, 1979;Ruoslahti and Engvall, 1980;Mosher et al, 1980).…”

Section: Discussionmentioning

confidence: 99%

³H‐mannose utilization by fibroblasts of the periodontal ligament

Cho¹,

Garant²

1987

Anat. Rec.

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The synthesis, intracellular translocation, and secretion of mannose-containing glycoproteins(s) by periodontal ligament fibroblasts have been investigated by means of electron microscopic radioautography. Tritiated mannose was administered to young mice via jugular vein, and radioautographs were prepared at 5, 10, 20, and 35 minutes, 4 and 8 hours after injection. Analysis of electron microscopic radioautographs revealed a maximum labeling (94%) with 3H-mannose of the rough endoplasmic reticulum at 5 minutes. Labeling of the Golgi components started to increase from 10 minutes (14%) and reached a maximum level at 20 minutes (31.2%). At 35 minutes, secretion granules, dense bodies, profiles of intracellular collagen, and the cell surface were labeled. At 8 hours, most labelling (79.2%) was extracellular, and associated either with the collagenous matrix (43.7%) or the cell surface (35.5%). Cytoplasmic vesicles containing dense materials around collagen fibrils were also labeled at 8 hours. It is concluded that mannose is directly incorporated into the rough endoplasmic reticulum (RER), and that mannose-containing glycoprotein(s) are packaged in the Golgi apparatus into secretory granules. Mannose-containing glycoprotein(s) become distributed on the periodontal ligament (PDL) fibroblast cell surface, cytoplasmic dense bodies, and the extracellular matrix.

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“…The A and B chains are very similar but not identical polypeptides [48] which are organized into discrete functional domains. These domains have been characterized as specific protease-resistant fragments that bind to gelatin 17, 42,[49][50][51][52][53][55][56][57][58][59][60][61][62], heparin [42,57,63,641, actin [42,621,DNA [42], S aureus [42, 431, fibrin [66], transglutaminase [43,58,671, and the plasma membrane [56-581; they also have characteristic carbohydrates and free sulfhydryl groups. These domains, isolated or identified mainly by affinity chromatography of proteolytic fragments, are summarized in Table I.…”

Section: Domain Structure Of Fibronectinmentioning

confidence: 99%

The structure of fibronectin and its role in cellular adhesion

Akiyama

Yamada

Hayashi

1981

J. Supramol. Struct. Cell. Biochem.

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Fibronectin is a large, adhesive glycoprotein which is found in a number of locations, most notably on cell surfaces, in extracellular matrixes, and in blood. Fibronectin had been detected in all vertebrates tested and in many invertebrates. Its presence in sponges is significant because this suggests that fibronectin may have appeared very early in evolution, possibly with the most primitive multicellular organisms. Cellular and plasma fibronectins have many striking similarities. However, the locations of the polypeptide chain differences between these two proteins indicate that plasma fibronectin cannot be derived from cellular fibronectin by means of simple post-translational proteolysis. Instead, these different types of fibronectin may be products of different genes or of differentially spliced messenger RNA molecules. Amniotic fluid fibronectin is possibly a third form of the protein. Cellular and plasma fibronectins are composed of at least six protease-resistant domains which contain specific binding sites for actin, gelatin, heparin, Staphylococcus aureus, transglutaminase, fibrin, DNA, and a cell surface receptor. The relative locations of these domains have been mapped in the primary structure of fibronectin. The cell surface receptor for fibronectin has not been positively identified, but may be a glycoprotein, a glycolipid, or a complex of the two. Although cell-substratum adhesion is mediated by fibronectin, the locations of the areas of closest approach of the cell to the substratum (the adhesion plaques) and fibronectin are not coincident under conditions of active cell growth. Under conditions of cell growth arrest in low serum concentrations, some fibronectin may become localized at the adhesion plaques. Models describing the domain structure of fibronectin and the molecular organization of the adhesion plaque area are presented.

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Identification and isolation of a collagen-binding fragment of the adhesive glycoprotein fibronectin.

Cited by 110 publications

References 30 publications

Role of collagenous matrices in the adhesion and growth of cells.

Role of collagenous matrices in the adhesion and growth of cells.

³H‐mannose utilization by fibroblasts of the periodontal ligament

The structure of fibronectin and its role in cellular adhesion

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Identification and isolation of a collagen-binding fragment of the adhesive glycoprotein fibronectin.

Cited by 110 publications

References 30 publications

Role of collagenous matrices in the adhesion and growth of cells.

Role of collagenous matrices in the adhesion and growth of cells.

3H‐mannose utilization by fibroblasts of the periodontal ligament

The structure of fibronectin and its role in cellular adhesion

Contact Info

Product

Resources

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³H‐mannose utilization by fibroblasts of the periodontal ligament