A study of actin—fibronectin interaction

Koteliansky, Victor; Glukhova, Marina A.; Morozkin, A.D.; Musatov, Andrej; Shirinsky, Vladimir P.; Tskhovrebov, L.A.; Smirnov, V.N.

doi:10.1016/0014-5793(81)80464-4

Cited by 12 publications

(2 citation statements)

References 23 publications

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“…In capillaries, specific staining for actin localized it to the basement membrane surrounding the endothelial cells and pericytes (7). Moreover, actin has been reported to bind to fibronectin (35,36). Thus, it was suggested that the association between actin, fibronectin, and other extracellular proteins could be functional-i.e., actin might participate in the control of cell adhesion and cell movement (7).…”

Section: Discussionmentioning

confidence: 99%

Actin is a surface component of calf pulmonary artery endothelial cells in culture.

Moroianu

Fett

Riordan

et al. 1993

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

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An angiogenin binding protein isolated previously from endothelial cells has been shown to be a member of the actin family. Calf pulmonary artery endothelial (CPAE) cells were investigated for the presence of surface actin by inmmunoblotting of isolated surface proteins and by immunofluorescence. CPAE cell surface proteins were isolated by selective apical biotinylation and recovery of biotinylated proteins by avidin affinity chromatography. Immunoblotting with a specific smooth muscle a-actin antibody detected the presence of this type of actin among the isolated cell surface proteins. Immunofluorescence confirmed that smooth muscle a-actin is localized at the surface of nonpermeabilized CPAE cells. Exposure of CPAE cells to angiogenin prior to cell surface immunostaining diminished the signal. When CPAE and rat aortic smooth muscle cells were made permeable before staining, stress fibers could be recognized by the antibody in smooth muscle cells but not CPAE cells. The results indicate that a smooth muscle type of a-actin is localized specifically on the surface of cultured CPAE cells where it might interact with angiogenin and other actin binding proteins present in the extracellular environment.Actin is an abundant, highly conserved protein that polymerizes into filaments that are essential for cellular motility and cell division as well as for the structure and mechanical properties ofthe cytoplasmic matrix. Whereas the majority of actin is found in the intracellular compartment, the protein has also been reported to be present on the cell surface of brain endothelial cells (1) and lymphocytes (2, 3), in the extracellular matrix of bovine aorta (4), cultured chicken embryo fibroblasts (5), or cultured rat smooth muscle cells (6), and in the basement membrane of endothelial cells, pericytes, and smooth muscle cells of arteries and arterioles (7).Angiogenin, a potent angiogenic molecule present in tumor cell conditioned medium (8), plasma (9), and milk (10), binds a 42-kDa dissociable cell surface component of calf pulmonary artery endothelial (CPAE) cells and GM7373 cells, a transformed bovine endothelial cell line (11). The angiogenin binding protein (AngBP) can be released from endothelial cells by exposure to heparin, heparan sulfate, or angiogenin (11,12). Tryptic peptide mapping and amino acid sequence analyses have indicated that AngBP is a member of the muscle-type actin family (12).The present study was undertaken to establish that actin is associated with the surface of endothelial cells in culture.Two different approaches were used: (i) immunoblotting of proteins isolated specifically from the cell surface and (ii) immunofluorescence with nonpermeabilized cells. The results indicate that a smooth muscle type of a-actin is present on the surface of endothelial cells in culture where it may function as an AngBP involved in the process of angiogenesis. MATERIALS AND METHODSMaterials. Bovine muscle actin and monoclonal antibodies to amoeba actin and to smooth muscle a-actin were from Sigma; flu...

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Section: Discussionmentioning

confidence: 99%

Actin is a surface component of calf pulmonary artery endothelial cells in culture.

Moroianu

Fett

Riordan

et al. 1993

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

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“…Thus denatured collagen binds more strongly to fibronectin than does native collagen (Engvall & Ruoslahti, 1977;Jilek & H6rmann, 1978). The same is true for actin (Koteliansky et al, 1981). Binding of fibronectin to fibrin monomers, which are proteolytic derivatives of fibrinogen, is also more effective than binding to fibrinogen (Stemberger & Hormann, 1976).…”

Section: Effect Of Bivalent Cationsmentioning

confidence: 60%

Association of fibronectin with carboxy-group-modified proteins in vitro

Vuento

Korkolainen

Stenman

1982

Biochemical Journal

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Treatment of human immunoglobulin G, albumin and fibronectin with water-soluble carbodi-imide at pH4.75 in the presence of glycine ethyl ester resulted in an avid binding of (125)I-labelled native fibrinectin to the modified proteins. Succinoylation, reduction and alkylation or heat-denaturation had no such effect. In affinity chromatography under physiological conditions, serum was depleted of fibronectin when run through columns of the carbodi-imide-treated proteins coupled to agarose. Fractions eluted from such columns with urea were enriched in fibronectin. The binding of radiolabelled fibronectin to the carbodi-imide-treated proteins was inhibited by unlabelled fibronectin in relatively low concentrations, but also by albumin in higher concentrations. Heat-denatured albumin inhibited at concentrations approx. 10-30 times lower than native albumin. The binding reaction had a pH optimum of 6-8. It was inhibited at high ionic strength and in the presence of urea. Anionic detergents inhibited at millimolar concentrations, but non-ionic detergents did not inhibit the binding reaction. The results were interpreted as showing that: (1) fibronectin is capable of binding to itself, to immunoglobulin G and to albumin after a reduction of the negative surface charge of these proteins, and may have a general ability to bind such modified proteins; (2) this binding can take place under physiological conditions; (3) carboxy-group-modified proteins selectively bind fibronectin from serum. This novel binding phenomenon could be important in terms of the opsonin function of circulatory fibronectin. We propose that fibronectin may recognize modified (denatured) proteins and mediate their uptake by the reticuloendothelial system.

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Interaction of Plasma Fibronectin (pFN) With Membranous Constituents of Peritoneal Exudate Cells and Pulmonary Macrophages

Rovin

Molnár

Chevalier

et al. 1984

Journal of Leukocyte Biology

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The prominent role of plasma fibronectin (pFN) in the host defense system as an opsonin for gelatin (collagen)-coated colloids has been established. In the present study we investigated the interaction of pFN and membrane isolates from cells devoid of collagen, as well as several tissues. In a liver slice assay system it was shown that subcellular membrane fractions from lung macrophages, peritoneal exudate cells, spleen, tests, and liver were able to competitively inhibit the pFN-mediated uptake of 125I-gelatin coated latex beads (gLtx) at low concentrations. Endocytosis of 125I-labeled membrane isolates by macrophage monolayers was also promoted by addition of pFN. In an attempt to characterize the membrane component(s) interacting with pFN, it was found that mild extraction procedure with 1 M KBr could release a significant amount of this inhibitory activity. Further studies demonstrated that the agent(s) responsible for inhibition of gLtx uptake was heat sensitive, not altered by trypsin treatment, and did not contain actin, a protein known to interact with pFN. This work indicates that pFN interacts specifically with an as yet unknown membrane component(s) and that such interaction will promote clearance of cellular debris by macrophages. This suggests that pFN may be an important opsonin for the reticuloendothelial system in clearance of collagenous and noncollagenous cellular debris once they are exposed to interact with it.

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A study of actin—fibronectin interaction

Cited by 12 publications

References 23 publications

Actin is a surface component of calf pulmonary artery endothelial cells in culture.

Actin is a surface component of calf pulmonary artery endothelial cells in culture.

Association of fibronectin with carboxy-group-modified proteins in vitro

Interaction of Plasma Fibronectin (pFN) With Membranous Constituents of Peritoneal Exudate Cells and Pulmonary Macrophages

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