Results 221 to 230 of about 8,122 (251)
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Journal of Oral Pathology & Medicine, 1981
Abstract The current knowledge of the structure, expression and functions of fibronectin is reviewed.Fibronectin is a high molecular weight glycoprotein present in the blood, connective tissue and at cell surfaces. It is synthesized by many types of differentiated cells and is believed to be involved in the attachment of cells to the surrounding ...
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Abstract The current knowledge of the structure, expression and functions of fibronectin is reviewed.Fibronectin is a high molecular weight glycoprotein present in the blood, connective tissue and at cell surfaces. It is synthesized by many types of differentiated cells and is believed to be involved in the attachment of cells to the surrounding ...
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Fibronectin and cryoprecipitation
La Ricerca in Clinica e in Laboratorio, 1986Fourteen patients with essential mixed cryoglobulinemia were studied. The relevance of fibronectin (FN) in cryoprecipitation seems to be of relative importance since only two thirds of the cryoprecipitates have a higher cryocrit level when FN is present. On the other hand, the other samples show a lower precipitating activity after plasma heating at 60
Pier Luigi Meroni +3 more
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Fibronectin and Atherosclerosis
Acta Medica Scandinavica, 1980ABSTRACT. Fibronectin is a polymorphic glycoprotein of plasma, other body fluids and connective tissue, and it occurs in an insoluble and a soluble form. Insoluble fibronectin is found associated with basement membranes and in loose connective tissue matrix as well as in the pericellular matrix formed around cultured adherent cells, such as ...
Karl von Smitten +2 more
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Annual Review of Medicine, 1984
Fibronectin is a major protein of blood and tissues. It has been intensively studied because of its many interactions with cells and other macromolecules. Fibronectin is a principal component of the extracellular matrix, and its most important function seems to be in tissue remodelling during embryogenesis and wound healing.
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Fibronectin is a major protein of blood and tissues. It has been intensively studied because of its many interactions with cells and other macromolecules. Fibronectin is a principal component of the extracellular matrix, and its most important function seems to be in tissue remodelling during embryogenesis and wound healing.
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Current Protocols in Cell Biology, 1999
AbstractThis unit describes the purification of the multifunctional adhesive glycoprotein fibronectin from plasma or of cell‐derived fibronectin from cell surfaces and from conditioned medium. Fibronectin can be used in cell adhesion and migration assays, and can be obtained in relatively high purity using simple affinity chromatography techniques ...
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AbstractThis unit describes the purification of the multifunctional adhesive glycoprotein fibronectin from plasma or of cell‐derived fibronectin from cell surfaces and from conditioned medium. Fibronectin can be used in cell adhesion and migration assays, and can be obtained in relatively high purity using simple affinity chromatography techniques ...
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Steroids, 1989
The fibronectin (FN) levels in human follicular fluids have been shown to correlate well with follicular size and oocyte maturity, suggesting a role of FN in oocyte maturation. When added to the culture medium, the synthetic peptide Gly-Arg-Gly-Asp-Ser (GRGDS), which specifically inhibits the cell-binding of FN, has been shown to inhibit both ...
Akira Tsuiki +2 more
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The fibronectin (FN) levels in human follicular fluids have been shown to correlate well with follicular size and oocyte maturity, suggesting a role of FN in oocyte maturation. When added to the culture medium, the synthetic peptide Gly-Arg-Gly-Asp-Ser (GRGDS), which specifically inhibits the cell-binding of FN, has been shown to inhibit both ...
Akira Tsuiki +2 more
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Journal of Cell Science, 2002
Fibronectin (FN) mediates a wide variety of cellular interactions with the extracellular matrix (ECM) and plays important roles in cell adhesion, migration, growth and differentiation ( [Mosher, 1989][1]; [Carsons, 1989][2]; [Hynes, 1990][3]; [Yamada and Clark, 1996][4]).
Kenneth M. Yamada, Roumen Pankov
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Fibronectin (FN) mediates a wide variety of cellular interactions with the extracellular matrix (ECM) and plays important roles in cell adhesion, migration, growth and differentiation ( [Mosher, 1989][1]; [Carsons, 1989][2]; [Hynes, 1990][3]; [Yamada and Clark, 1996][4]).
Kenneth M. Yamada, Roumen Pankov
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Dermatology, 1987
In the skin organ culture model of pemphigus, fibronectin concentrations of 300 and 500 μg/ml inhibited pemphigus plasma-induced acantholysis and intraepidermal binding of the pemphigus antibodies examined by direct immunofluorescence. A direct interaction of fibronectin with pemphigus antibodies could not be demonstrated by chromatography of pemphigus
Jean-Jacques Morgenthaler +2 more
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In the skin organ culture model of pemphigus, fibronectin concentrations of 300 and 500 μg/ml inhibited pemphigus plasma-induced acantholysis and intraepidermal binding of the pemphigus antibodies examined by direct immunofluorescence. A direct interaction of fibronectin with pemphigus antibodies could not be demonstrated by chromatography of pemphigus
Jean-Jacques Morgenthaler +2 more
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Expression of Fibronectin and Adhesion to Fibronectin in Myeloma Cell Lines
Acta Haematologica, 1993Fibronectin (FN) expression in six myeloma, two mature B-cell lines, and four T-cell lines was analyzed. All myeloma cell lines expressed FN at various levels, while mature B- and T-cell lines apparently had less FN. Moreover, an extramedullary plasmacytoma-derived myeloma cell line, KHM7, was found to secrete FN into the culture medium.
Hiromitsu Matsuzaki +6 more
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Seminars in Cancer Biology, 2002
Fibronectin (Fn) was the first 'structural' glycoprotein intensively studied as an ubiquitous matrix component of early phylogenetic appearance. Its age-dependent increase in plasma and tissues may be accompanied in pathological states, especially in tumor growth, by its proteolytic breakdown by a number of neutral proteases.
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Fibronectin (Fn) was the first 'structural' glycoprotein intensively studied as an ubiquitous matrix component of early phylogenetic appearance. Its age-dependent increase in plasma and tissues may be accompanied in pathological states, especially in tumor growth, by its proteolytic breakdown by a number of neutral proteases.
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