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Isolation of an amino-terminal fibronectin-binding protein on human U937 cells and rat peritoneal macrophages

BLYSTONE, SD ; KAPLAN, JE

The Journal of biological chemistry, 1992-02, Vol.267 (6), p.3968-3975 [Periódico revisado por pares]

BETHESDA: American Society for Biochemistry and Molecular Biology

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Título:
Isolation of an amino-terminal fibronectin-binding protein on human U937 cells and rat peritoneal macrophages
Autor: BLYSTONE, SD ; KAPLAN, JE
Assuntos: Albumins - metabolism ; Analytical, structural and metabolic biochemistry ; Animals ; Binding and carrier proteins ; Biochemistry & Molecular Biology ; Biological and medical sciences ; Cells, Cultured ; Chromatography, Affinity ; Cross Reactions ; Electrophoresis, Polyacrylamide Gel ; Fibrinogen - metabolism ; fibronectin-binding protein ; Fibronectins - metabolism ; Fundamental and applied biological sciences. Psychology ; Gelatin - metabolism ; Humans ; Isoelectric Focusing ; isolation ; Life Sciences & Biomedicine ; macrophages ; Macrophages - chemistry ; Macrophages - metabolism ; man ; N-terminus ; Peritoneal Cavity - cytology ; Precipitin Tests ; Proteins ; Rats ; Receptors, Fibronectin ; Receptors, Immunologic - isolation & purification ; Receptors, Immunologic - metabolism ; Science & Technology ; Trypsin - metabolism ; U937 cells
É parte de: The Journal of biological chemistry, 1992-02, Vol.267 (6), p.3968-3975
Notas: Medline
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Descrição: Several cell-mediated activities for the amino terminus of fibronectin have been documented. In the present study we describe a macrophage surface protein with binding activity directed to the amino terminus of the fibronectin molecule. The binding of a 29-kDa amino-terminal fibronectin fragment to macrophages reached steady state by 30 min and was half-maximal at approximately 2 x 10(-8) M. This binding was specifically inhibited by excess unlabeled 29-kDa fragment or intact fibronectin but not by a 180-kDa fibronectin fragment which lacks the amino terminus. Competitive binding studies of the 70-kDa amino-terminal fibronectin fragment to macrophages revealed a single binding site with KD = 7.14 x 10(-8) M and approximately 8 x 10(4) binding sites/cell. Radiolabeled surface proteins extracted from rat peritoneal macrophages and from the human U937 cell line were applied to an affinity column comprised of the 70-kDa amino-terminal fragment of fibronectin coupled to a solid support. A single trypsin-sensitive radiolabeled protein of 67 kDa, from either cell type, was eluted from this column with urea. This protein showed no immunologic identity with fibronectin, fibrin(ogen), or albumin. The 67-kDa protein exhibited identical apparent molecular weight under reducing and nonreducing conditions, as assessed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis analysis. We have localized the fibronectin binding activity of this protein to within the 29-kDa amino-terminal domain of fibronectin. The 67-kDa protein eluted from the 70-kDa column failed to bind to a column comprised of the 45-kDa gelatin-binding fragment of fibronectin. Additionally, the 67-kDa protein was specifically eluted from the 70-kDa column by the 29-kDa amino-terminal fragment but not by the 45-kDa gelatin-binding fragment. These data suggest that this 67-kDa protein is a macrophage cell surface binding protein for the amino terminus of fibronectin.
Editor: BETHESDA: American Society for Biochemistry and Molecular Biology
Idioma: Inglês

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Isolation of an amino-terminal fibronectin-binding protein on human U937 cells and rat peritoneal macrophages

BLYSTONE, SD ; KAPLAN, JE

BETHESDA: American Society for Biochemistry and Molecular Biology

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