Fibronectin (Cold-Insoluble Globulin), VI. Influence of Heparin and Hyaluronic Acid on the Binding of Native Collagen<sup />

Jilek, F.; Hörmann, Helmut

doi:10.1515/bchm2.1979.360.1.597

Cited by 161 publications

(33 citation statements)

References 8 publications

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“…Fibronectin is characterized by a high affinity to collagen, especially to collagen type III [19] and to fibrin [14] forming crosslinks under the influence of plasma-transglutaminase (activated factor XIII) [22,23]. Furthermore, it enhances the attachment of fibroblasts [12] and endothelial cells [9] in cell culture.…”

Section: Discussionmentioning

confidence: 99%

Immunohistochemical localization of fibronectin as a tool for the age determination of human skin wounds

et al. 1992

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Summary:We analyzed the distribution of fibronectin in routinely embedded tissue specimens from 53 skin wounds and 6 postmortem wounds. In postmortem wounds a faint but focal positive staining was exclusively found at the margin of the specimens which dit not extend into the adjacent stroma. Vital wounds were classified into 3 groups. The first comprising lesions with wound ages ranging from a few seconds to 30min, the second comprising those with wound ages upt to 3 weeks, and the third group with lesions more than 3 weeks old. Ten out of 17 lesions with a wound age up to 30 rain showed a clear positive reaction within the wound area. Three specimens in this group were completely negative, while in 4 additional cases the result was not significantly different from postmortem lesions. These 7 Cases were characterized by acute death with extremely short survival times (only seconds). In wounds up to 3 weeks old fibronectin formed a distinct network containing an increasing number of inflammatory cells corresponding to the wound age. In 2 cases with a survival time of 17 days and in all wounds older than 3 weeks fibronectin was restricted to the surface of fibroblasts and to parallel arranged fibers in the granulation tissue without any network structures. We present evidence that fibronectin is a useful marker for vital wounds with a survival time of more than a few minutes. Fibronectin appears before neutrophilic granulocytes migrate into the wound area. Since a faint positive fibronectin staining is seen in postmortem lesions and bleedings, we propose that only those wounds which show strong positive fibronectin staining also extending into the adjacent stroma should be regarded as vital.

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Section: Discussionmentioning

confidence: 99%

Immunohistochemical localization of fibronectin as a tool for the age determination of human skin wounds

et al. 1992

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“…The reason for the heparin dependence is obscure . Several studies have shown that fibronectin, gelatin, and heparin can participate in the formation of ternary aggregates (6,23,24,45) . However, aggregation is not a sufficient explanation for our results because (a) in the presence of F(ab')2 fragments of antifibronectin, aggregates of beads still formed but internalization was inhibited (Fig.…”

Section: Discussionmentioning

confidence: 99%

Phagocytosis of gelatin-latex particles by a murine macrophage line is dependent on fibronectin and heparin.

Water¹,

Schroeder²,

Crenshaw³

et al. 1981

The Journal of Cell Biology

116

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It has been suggested that fibronectin plays a role in clearing particles from the circulation by promoting binding to phagocytes of the reticuloendothelial system . By use of a well-defined system to investigate the possible opsonic role of fibronectin, we have studied the uptake of gelatin-coated latex particles by a murine macrophage cell line (P388D 1 ) .Fibronectin promotes binding of gelatin-coated beads to these cells in both suspension and monolayer cultures . In both cases there is a requirement for heparin as a cofactor . Other glycosaminoglycans (chondroitin sulfates A and C, dermatan sulfate, and keratan sulfate) were inactive, whereas heparan sulfate was somewhat active .Proof that beads were actually endocytosed was obtained by electron microscopy, which showed beads internalized in membrane-bounded vesicles, and by immunofluorescence analyses, using antibodies to fibronectin to stain external beads. Two rapid assays for the opsonic activity of fibronectin were developed based on differential centrifugation of cellassociated beads and on the immunofluorescence procedure . Binding and endocytosis were time-and temperature-dependent and varied with the amount of gelatin on the beads and with the concentrations of fibronectin and heparin added, and could be inhibited by F(ab') 2 antifibronectin . These studies provide a sound basis for a detailed analysis of the interaction of fibronectin with the cell surface and of its involvement in endocytosis.Phagocytosis is the process by which particles (bacteria, damaged cells, fibrin aggregates, etc .) are bound and endocytosed by phagocytic cells . Recognition of these particles by the cells is due to the presence of humoral factors (opsonins) such as immunoglobulins or complement, which coat the particles and promote their phagocytosis (44). Recently, an a-2-globulin from plasma has been shown to facilitate clearance of certain particles from the circulation (31,32,42) . It also promotes the binding of particles to liver slices (12,16,31,40) and the uptake of gelatin-coated particles by rat peritoneal macrophages (13,18) . This a-2-globulin has recently been purified from rat and human sera and found to be immunologically and functionally identical with plasma fibronectin (2, 33), a dimeric glycoprotein with subunits of 230,000 daltons (3) . Fibronectin is known to be involved in adhesion of cells to solid substrata and has specific binding sites for gelatin, glycosaminoglycans (i .e ., heparin), fibrinogen, and fibrin, and can be crosslinked to fibrin or collagen by Factor XIII (reviewed in references 17, 21, 35, 32 47, 49) . Fibronectin has also been shown to bind to bacteria' (27, 36), but has not been shown to promote phagocytosis of bacteria .To define the conditions necessary for endocytosis of fibronectin-coated particles, we have studied an established mouse macrophagelike cell line (P388D,) by using a centrifugation assay, as well as electron and immunofluorescence microscopy. We find that endocytosis of gelatin-conjugated latex beads...

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“…These subunits, which may have slight difTerences in sequence, are com monly linked as a dimer via interchain disul fide bonds near the C-terminus. The subunits contain distinct domains that mediate spe cific interactions with fibrin noncovalently and via factor XHIa [14][15]; with collagen, especially denatured collagen, gelatin [16][17][18]; with heparin and other anionic polymers [19][20][21][22]; and with certain cells [23][24][25][26], in cluding fibroblasts and macrophages. The in terdomain regions are relatively sensitive to proteolysis, and the separate domains can be isolated after mild enzymatic digestion by affinity chromatography using the appro priate ligand.…”

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confidence: 99%

Are the Biologic Activities of Fibronectin Controlled by Alterations in Its Molecular Form?

Colvin¹,

Kradin²

1983

Pathol Immunopathol Res

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Fibronectin (Cold-Insoluble Globulin), VI. Influence of Heparin and Hyaluronic Acid on the Binding of Native Collagen

Cited by 161 publications

References 8 publications

Immunohistochemical localization of fibronectin as a tool for the age determination of human skin wounds

Immunohistochemical localization of fibronectin as a tool for the age determination of human skin wounds

Phagocytosis of gelatin-latex particles by a murine macrophage line is dependent on fibronectin and heparin.

Are the Biologic Activities of Fibronectin Controlled by Alterations in Its Molecular Form?

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