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PubMed1989

Effect of repetitive low-dose endotoxin on liver parenchymal and Kupffer cell fibronectin release.

Repetitive low-dose endotoxin, at a dose which will result in endotoxin tolerance, produces a marked but transient 2- to 3-day increase in plasma fibronectin. This elevation of fibronectin appears to contribute to increased hepatic Kupffer cell phagocytic function observed with repetitive low-dose endotoxin administration. Although numerous cell types synthesize fibronectin, hepatocytes are believed to be the major cell source of fibronectin in the plasma. Since Kupffer cells also synthesize fibronectin, we sought to determine the relative contribution of hepatic Kupffer cells, as compared to parenchymal cells, to the elevation of plasma fibronectin following repetitive low-dose endotoxin administration. Kupffer cells isolated from rats previously treated for 3 consecutive days with 100 micrograms Salmonella enteritidis endotoxin released greater (p less than 0.01) amounts of fibronectin over time in culture (3, 6, 12 and 24 hr) as compared to Kupffer cells isolated from normal rats. Experiments in which fibronectin was normalized to DNA content of the cells in culture also showed similar results for fibronectin release by Kupffer cells (normal: 2.9 +/- 0.5 ng per microgram DNA per 24 hr; endotoxin-treated: 53.3 +/- 1.3 ng per microgram DNA per 24 hr). Hepatocytes from endotoxin-treated rats released less (p less than 0.01) fibronectin over time than hepatocytes isolated from normal animals. As with Kupffer cells, results for fibronectin release by hepatocytes were similar when normalized to the DNA content (normal: 190.0 +/- 9.4 ng per microgram DNA per 24 hr; endotoxin-treated: 83.3 +/- 4.2 ng per microgram DNA per 24 hr).(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1982

Fibronectin is apparently not involved in species-specific reaggregation of cells from the marine sponge geodia cydonium.

Experiments were carried out to test the hypothesis that fibronectin is involved in reaggregation of dissociated sponge cells. Cells from the siliceous sponge Geodia cydonium were extracted with urea to solubilize fibronectin from cells of higher multicellular organisms. The crude extract was further fractionated by DNA, heparin, and collagen affinity chromatography; they were termed Geodia fibronectin like fractions. The fibronectin like fractions contained a series of proteins with molecular weights different from that of the genuine fibronectin. The Geodia fibronectin like fractions did not react with antiserum, produced against human fibronectin, under formation of a precipitin line. Using this antiserum the sponge cells could not be specifically labeled with FITC-anti-IgG antiserum. Radioimmunoprecipitation experiments revealed that the Geodia fractions contain--if at all--0.1% fibronectin or fibronectin like protein at the most. In the crucial experiments it was shown that the Geodia fibronectinlike fractions, human fibronectin, and antifibronectin antiserum exerted no influence on adhesion of Geodia cells either in the absence or in the presence of the soluble aggregation factor. Based on these findings, we conclude that fibronectin is apparently not present on Geodia cells and does not play a role in aggregation of this biological system.

Animals↗
PubMed1987

Fibronectin-associated transforming growth factor.

We have studied the ability of fibronectins to induce anchorage-independent growth of NRK-49F cells in serum-free medium. Cells were seeded in soft agar in the presence of various concentrations of plasma fibronectins, and colonies were counted after 10 days. It was found that, with some exceptions, human plasma fibronectins induced anchorage-independent growth at concentrations in 20-100 micrograms/ml range. The ability of exogenously supplied fibronectins to promote anchorage-independent growth of NRK cells is attributed to a transforming growth factor (TGF) activity associated with gelatin-agarose affinity purified plasma fibronectins. This TGF activity required epidermal growth factor (EGF) in our serum-free assay system. The TGF-like activity appears to either co-purify or to be associated with fibronectin at neutral pH during molecular sieve chromatography and during ultracentrifugation through sucrose density gradients. The TGF activity "dissociates" from fibronectin at extremes of pH, however, and can be separated from fibronectin by molecular sieve chromatography in 1 M acetic acid. Under these conditions, the TGF-like activity chromatographed as a single peak with an apparent molecular weight of approximately 30 kDa. The physical-chemical properties, chromatographic behavior, and biological activity of this TGF suggest that it is type-beta transforming growth factor/growth inhibitor (beta-TGF/GI). The TGF activity has been observed in fibronectin isolated from fresh human plasma as well as in fibronectins from several other species obtained from commercial suppliers. Our results would suggest that caution be applied in the interpretation of experiments in which gelatin affinity purified fibronectins are used at micrograms/ml concentrations.

Animals↗
PubMed1988

Extracellular matrix assembly of cell-derived and plasma-derived fibronectins by substrate-attached fibroblasts.

Using a previously described model system for the incorporation of plasma fibronectin into the extracellular matrix (McKeown-Longo, P.J. and Mosher, D.F., 1985. J. Cell Biol., 100:364-374), we compared the binding of cell-derived and plasma-derived fibronectins to human fibroblast cell layers. Binding was measured in time course experiments using metabolically labeled cell-derived, iodinated cell-derived, and iodinated plasma-derived fibronectins. The kinetics of matrix assembly of cell- and plasma-derived fibronectins were the same. Competitive binding curves using intact fibronectin or the 70-kD amino-terminal fragment of fibronectin suggested that cell surface binding sites have equal affinity for cell- and plasma-derived fibronectins. Iodinated fibronectins did not bind to isolated matrices containing collagen type I, fibronectin, and thrombospondin. These results suggest that fibroblasts do not distinguish between cell-derived and plasma-derived fibronectins when assembling exogenous fibronectin into extracellular matrix.

Binding Sites↗
PubMedDate not supplied

Changes in lung tissue fibronectin content and synthesis during postnatal lung growth.

We studied changes in lung tissue fibronectin content and synthesis during postnatal lung growth in rats. We reasoned that fibronectin, which is important in cell differentiation, migration, and adhesion, and in the organization of the extracellular matrix, might play a role in the rapid cell proliferation and alveolar septal formation that occurs postnatally in mammalian lungs. Newborn rats were sacrificed at 4, 7, 11, 14, and 21 days after birth. The lungs were perfused and lavaged, tissue fibronectin was extracted using urea and heparin (Bray et al, Science 1981; 214:793) and the extracted fibronectin was measured by enzyme-linked immunoassay. Tissue fibronectin synthesis was measured by the in vivo incorporation of 35S-methionine into fibronectin that was extracted from lung tissue and immunoprecipitated. Lavage fibronectin and albumin content and lung tissue collagen (hydroxyproline) content were also determined. Lung tissue fibronectin content per g dry lung almost doubled between days 4 and 7 after birth, was slightly higher at day 14 than at day 7, and decreased sharply between days 14 and 21. Lung tissue fibronectin synthesis per g dry lung increased steadily between days 4 and 14 to reach a peak value of about 2.5 times the 4-day value; it then decreased sharply between days 14 and 21. The period of increased fibronectin content and synthesis (4 to 14 days) coincided with the period during which lung cell proliferation and secondary alveolar septa formation are known to be the most active, and the sharp decrease in fibronectin content and synthesis (between 14 and 21 days) coincided with the period during which lung growth and remodeling markedly decrease.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1995

Mechanical properties of the extracellular matrix influence fibronectin fibril assembly in vitro.

Mechanical properties of the extracellular matrix (ECM) are proposed to influence cell behavior and biological activity. The influence of the mechanical environment on fibronectin fibril assembly was evaluated. Fibroblasts were cultured in hydrated collagen gels with two distinctly different mechanical properties. Cells cultured within a stabilized collagen gel generate stress that is transmitted throughout the matrix (stressed gel). In contrast, cells that are cultured within a collagen gel that is floating freely in media do not generate stress (relaxed gel). Fibroblasts in the stressed collagen gel develop large bundles of actin microfilaments and associated fibronectin fibrils, while fibroblasts within relaxed gels do not form stress fibers or assemble fibronectin into fibrils. In addition, we have evaluated the mechanism of fibronectin fibril assembly employed by fibroblasts cultured within a stressed three-dimensional collagen matrix and the role of fibronectin fibrils in transmission of cell-generated forces to the surrounding matrix. Fibronectin fragments (70-kDa amino terminal fragment, 110-kDa cell-adhesive fragment, and GRGDS peptide) and a monoclonal antibody body blocked fibronectin fibril assembly in stressed three-dimensional collagen gels. These results suggest that the features of fibronectin required for fibronectin fibril assembly by cells in collagen gels is similar to those required by cells cultured on a planar substratum. Although fibronectin fibril assembly was blocked by these inhibiting fragments and antibody, the cells displayed prominent actin bundles and developed isometric tension, indicating that stress fiber formation and contractile force transmission is not dependent on the presence of fibronectin fibrils.

Actins↗
PubMed1997

Endogenous fibronectin of blood polymorphonuclear leukocytes: immunochemical characterization and subcellular localization.

Fibronectin, a large dimeric glycoprotein synthesized and secreted by several cell types, mediates cell adherence to surfaces. In infections and inflammatory responses, blood polymorphonuclear leukocytes (PMNs) adhere to cells and matrix proteins during extravasation and accumulation at inflammatory sites. The presence of fibronectin in blood PMNs has been poorly studied, and the characteristics and subcellular localization of this endogenous adhesive molecule are practically unknown. By immunofluorescence flow cytometry, purified rabbit antibodies and a monoclonal antibody to plasma fibronectin reacted with isolated blood PMNs, only after permeabilization of the cells. By Western blot analysis, the antibodies recognized, under reducing conditions, a protein with an apparent molecular mass of 230 kDa in the cell lysate. Eleven monoclonal antibodies to common frame fibronectin epitopes, including the RGD-containing cell-binding domain, also reacted with PMN fibronectin by Western blotting. In contrast, two antibodies to ED-A, the alternatively spliced region characteristic of "cellular" fibronectin, were unreactive, but recognized platelet fibronectin. On average, 1 million PMNs contained 6.8 ng +/- 1.4 (SD) of fibronectin, as measured by sandwich ELISA. Immunogold labeling and electron microscopy studies indicated localization of most fibronectin in PMN granules. Moreover, double-immunofluorescence and digital image analysis demonstrated colocalization of fibronectin with lactoferrin, a marker of specific (secondary) granules. The results indicate that blood PMNs contain approximately 8000 molecules per cell of intact ED-A-negative fibronectin localized mainly in their specific granules.

Antibodies, Monoclonal↗
PubMed1997

Endogenous fibronectin of blood polymorphonuclear leukocytes: stimulus-induced secretion and proteolysis by cell surface-bound elastase.

In an accompanying study, we described the presence of intact fibronectin, a large adhesive molecule, in the specific granules of blood PMNs. Secretion of fibronectin by blood PMNs is poorly understood, and the fate of this fibronectin is practically unknown. In the present study we demonstrate that nanomolar concentrations of phorbol ester or the chemoattractants fMLP, PAF, and LTB4 induce fibronectin secretion from blood PMNs. Phorbol ester induced secretion of approximately 85% of the total fibronectin content, as well as expression of small amounts on the cell surface of the activated PMNs. Secreted fibronectin was proteolytically cleaved and, after 20 min, four major fragments of 150, 120, 90, and 80 kDa containing a midchain epitope were identified by Western blot analysis. Kinetic studies indicated that fibronectin was rapidly secreted as an intact molecule and that proteolysis started within minutes and proceeded for at least 1 h. If cells were removed after 5 min TPA treatment, no further proteolysis of the secreted fibronectin was observed, indicating participation of cell-bound proteinases. From a cocktail of proteinase inhibitors, PMSF was the most active in suppressing fibronectin proteolysis. Studies with specific peptidyl inhibitors of human leukocyte elastase and cathepsin G, major serine proteinases of PMNs, demonstrated some inhibition with the cathepsin G inhibitor, while the human leukocyte elastase inhibitor almost completely abolished fibronectin proteolysis. A monoclonal antibody to the elastase had a similar effect. The results indicate that intact fibronectin is a secretory product of blood PMNs and that this endogenous adhesive molecule is within minutes extracellularly processed by cell surface-bound elastase.

Antibodies, Monoclonal↗
PubMed1984

Spreading of explants of embryonic chick mesenchymes and epithelia on fibronectin and laminin.

Tissues from 2.5-day chick embryos were explanted onto glass coated with adsorbed fibronectin or laminin, or extracellular matrices (ECM) of deoxycholate-extracted chick embryo cells. Spreading of somitic and trunk neural-crest mesenchyme cells was equally rapid and extensive on fibronectin, laminin and on the fibronectin-rich, laminin-poor ECM produced by mesenchymal cells. No preference for fibronectin over laminin was displayed by these two mesenchymes when a choice of mutually exclusive alternating tracks was provided. Epithelial cells did not spread from explants of the neural tube on any substrate tested up to 24 h in vitro, but adhesion of the explant and outgrowth of axons was greatest on laminin. Explants of endodermal epithelium spread rapidly on or near ECM formed by endoderm cells. This ECM was deficient in laminin but contained dense fibronectin fibers. Spreading was less rapid on fibronectin, and even more retarded on laminin. Ectodermal epithelium explants spread rapidly on and near fibronectin-rich, laminin-poor ECM produced by ectoderm cells, and almost as rapidly on laminin, but spreading was strongly delayed and reduced on fibronectin. The observations suggest that the mesenchymal nature of somite and neural crest cells does not correspond to a lowered responsiveness to laminin relative to fibronectin, while the relationship between laminin and superior epithelial cell spreading should not be generalized. The spreading of the epithelia on complex ECM also indicates the presence of a component(s) other than fibronectin or laminin, which strongly promote(s) spreading. In addition, the methods used indicate that plasma fibronectin and laminin do not specifically bind to each other, and that bovine serum albumen may be inadequate in preventing the attachment of proteins, especially laminin, to cell culture substrates.

Animals↗
PubMed1987

Differential effects of soluble and immobilized fibronectins on aortic endothelial cell proliferation and attachment.

We studied the effects of soluble and immobilized forms of plasma fibronectin on bovine aortic endothelial cell (AEC) proliferation and attachment. Soluble fibronectin stimulated AEC growth at 10 micrograms/ml, but at higher concentrations of soluble fibronectin AEC growth was progressively inhibited. The growth rates of arterial smooth muscle cells (ASMC) and dermal fibroblasts (DF) were not altered by soluble fibronectin concentrations of 10 to 100 micrograms/ml. Plasma fibronectin, immobilized by attachment to culture dish surfaces, had no significant effects on the proliferation of any of the cell types examined. The attachment rates of AEC were decreased in the presence of 50 micrograms/ml soluble fibronectin. Immobilized fibronectin increased the rate of AEC attachment, but had no significant effects on ASMC or DF attachment; however, 12 h after plating there was nearly 100% attachment in all groups, whether or not fibronectin was present in the system. That soluble and immobilized fibronectins elicit disparate cellular responses is consistent with published reports of different cell surface receptors for different forms of the protein; in this manner, cells enmeshed in an interstitial matrix containing immobilized fibronectin could still respond to soluble fibronectin in the extracellular milieu.

Animals↗
PubMed2000

Differentiation of polymorphonuclear neutrophils in patients with systemic infections and chronic inflammatory diseases: evidence of prolonged life span and de novo synthesis of fibronectin.

Polymorphonuclear neutrophils (PMN) are considered to be short-lived, terminally differentiated cells undergoing spontaneous apoptosis if not appropriately stimulated. In patients with systemic infections and inflammatory disease, however, PMN have an extended life span and acquire new surface receptors and functions. Expression of CD64, the high-affinity receptor for immunoglobulin, has been found, and functionally active elastase and surface-associated fibronectin as well. The latter is of particular interest since fibronectin is known as a multifunctional, multimodal extracellular matrix protein, participating in cell adherence, cell signaling, and cell cycle control. To study the surface-associated fibronectin further, PMN of healthy donors were cultivated to induce de novo synthesis of fibronectin. PMN produced fibronectin, which remained associated with the cell surface, where it was partially cleaved. PMN derived fibronectin exhibited a rare splice pattern: predominantly fibronectin containing the extradomain B (EDB) was generated, but evidently no IIICS domain; the latter is known as a receptor for beta1 integrins. How the presence of EDB affects the properties of fibronectin is not yet understood. Studies with recombinant EDB have failed to show a membrane-binding site or a direct participation of EDB in the adhesion process. The function of PMN-associated fibronectin is still under investigation. The rapid cleavage by surface-associated proteases suggests that fibronectin acts as a tightly regulated adhesion protein, and probably also as a precursor molecule for fibronectin-derived biologically active mediators.

Alternative Splicing↗
PubMed1997

Plasma fibronectin levels in meningococcal disease.

UNLABELLED: Fibronectin (a glycoprotein which modulates inflammation) may decrease mortality in systemic infection. Children with meningococcal disease (MCD) may have low fibronectin levels. We aimed to compare plasma fibronectin levels in children with MCD and controls, correlate fibronectin levels with interleukin-6 (IL-6), shock and death, and assess fibronectin as an aid to early diagnosis in MCD. Samples were taken on admission from 99 children with MCD and 49 controls. Plasma fibronectin was measured using a turbidimetric immunoassay. Plasma fibronectin was significantly lower in MCD compared to controls (57 micrograms/ml vs 105 micrograms/ml; P < 0.005). Children who died had significantly lower levels than survivors (29 micrograms/ml vs 62 micrograms/ml; P = 0.01). Fibronectin levels were negatively correlated with IL-6 levels. Fibronectin was a poor predictor of MCD. CONCLUSION: Plasma fibronectin levels are decreased in children with MCD, especially in shock and death. This decrease is associated with high IL-6 levels. Fibronectin could be a novel therapy in severe MCD.

Biomarkers↗
PubMed1985

Decreased plasma fibronectin levels in children with hemolytic-uremic syndrome.

Fibronectin is a normal plasma glycoprotein thought to have an important role in platelet aggregation and clot formation. Because of the participation of the coagulation system in hemolytic-uremic syndrome, the present study sought to determine if fibronectin plays a role in the pathogenesis of this disease. With this purpose in mind, plasma fibronectin levels were measured in 17 children with the clinical diagnosis of hemolytic-uremic syndrome and in 22 age-matched control subjects. Fibronectin levels were significantly depressed in 13 of 17 (76 percent) patients with hemolytic-uremic syndrome during the acute phase of their illness. The levels did not correlate with age, sex, serum creatinine level, platelet count, or hemoglobin concentration. Serial plasma samples were available in eight of these patients: fibronectin remained depressed from two to 10 days and then returned toward the normal range concomitant with increasing platelet counts and improvement in renal function. During remission, fibronectin levels were normal in all nine patients tested. To try to determine if fibronectin is deposited in the kidney during hemolytic-uremic syndrome, kidney biopsy specimens from six patients with hemolytic-uremic syndrome were examined by immunofluorescence for the presence of fibronectin, fibrinogen, and platelet antigens. Extensive deposition of all three antigens was demonstrated along the glomerular capillary wall in all biopsy specimens. In conclusion, plasma fibronectin levels are decreased during the acute phases of hemolytic-uremic syndrome in the majority of patients. Kidney biopsy findings suggest that fibronectin is intimately involved in the activation of the coagulation system in this disease and that decreased plasma fibronectin levels in hemolytic-uremic syndrome may be due, at least in part, to accelerated consumption of the protein at the sites of injury.

Adolescent↗
PubMed1995

Monoclonal antibody X18A4 identifies an oncofetal fibronectin epitope distinct from the FDC-6 binding site.

OBJECTIVE: Oncofetal fibronectin reactive with antibody FDC-6 has been associated with trophoblastic implantation and chorion structural stability. Abnormal release of this fibronectin into cervical and vaginal secretions has identified patients at risk for preterm labor and delivery. The aim of this study was to determine whether trophoblast-derived oncofetal fibronectin contains other novel epitopes distinct from the FDC-6 binding site. STUDY DESIGN: Antitrophoblast fibronectin hybridomas were generated and screened by comparative immunoassays. One specific monoclonal antibody, X18A4, was identified and compared with antibody FDC-6 by immunocytochemical and immunoblot analyses. Both antibodies were also evaluated in "sandwich"-type double monoclonal immunosorbent assays. RESULTS: X18A4 and FDC-6 bind avidly and noncompetitively to distinct epitopes within oncofetal fibronectin. They exhibit similar immunohistochemical staining of the extracellular matrix within placental tissue, ovarian epithelial tumors, and cultured trophoblasts. However, in contrast to FDC-6, X18A4 has no detectable binding activity to human plasma fibronectin, and its binding to oncofetal fibronectin was unaffected by enzymatic deglycosylation. Immunoblot analyses of oncofetal fibronectin proteolytic digests suggest that X18A4 binds near or within the alternatively spliced type III connecting segment domain. CONCLUSIONS: X18A4 identifies and binds with high affinity to a new epitope within oncofetal fibronectin, distinct from the FDC-6 binding site. Because X18A4 displays no detectable binding to plasma fibronectin, it could be used as an important adjunctive antibody for enhancing the specificity of clinically based oncofetal fibronectin diagnostic assays.

Animals↗
PubMed1987

Fibronectin is stored but not synthesized in mature human peripheral blood granulocytes.

To investigate whether peripheral blood granulocytes can synthesize the adhesive glycoprotein, fibronectin, we sought to demonstrate the presence of messenger RNA coding for fibronectin within mature circulating granulocytes. Polyadenylated-enriched RNA was isolated from human peripheral blood granulocytes, human skin fibroblasts (synthesize fibronectin) and HeLa cells (lack fibronectin) and probed with a cDNA clone coding for the cell attachment domain of fibronectin. Hybridization of a fibronectin cDNA fragment occurred with fibroblast RNA but did not occur with granulocyte RNA despite a 100 fold excess granulocyte RNA. Incubation of granulocytes with n-formyl methionyl leucyl phenylalanine, a chemotactic peptide known to augment the release of fibronectin from granulocytes, failed to induce detectable levels of mRNA for fibronectin in granulocytes. There was no difference in the quantity of fibronectin released from chemotactic peptide-stimulated granulocytes pre-incubated in the presence or absence of the protein synthesis inhibitor, cycloheximide, suggesting that fibronectin exists in a stored form in granulocytes. These data suggest that fibronectin in mature granulocytes is the product of synthesis during early myeloid maturation.

Cells, Cultured↗
PubMed1992

Synthesis of cellular fibronectin by rat liver fat-storing (Ito) cells: regulation by cytokines.

Fibronectins are multifunctional extracellular matrix glycoproteins that seem to play a pacemaker role in liver fibrogenesis. The expression of cellular fibronectin by rat liver fat-storing cells in primary culture and their modulation by cytokines was studied. Cellular fibronectin was localized in the cytoplasm and on the surface of cultured fat-storing cells as well as in extracellular matrix fibrils by indirect immunofluorescence. Immunoprecipitation of endogenously labeled fibronectin using type specific antibodies showed the synthesis and secretion of cellular fibronectin by fat-storing cells in vitro. ED1 positive sequences specific for cellular fibronectin and absent in plasma fibronectin were detected within the total RNA of fat-storing cells. Cellular fibronectin synthesis was severalfold enhanced in "activated" vs. "resting" fat-storing cells. Treatment of fat-storing cells with transforming growth factor beta 1 resulted in a dose dependent increase of fibronectin synthesis. In contrast, interferon gamma inhibited the synthesis of fibronectin. The stimulation of fibronectin synthesis by transforming growth factor beta 1 and the inhibition by interferon gamma might be of importance for pathophysiology and therapy of liver fibrogenesis.

Animals↗
PubMed1992

Characterization of the interaction between human plasma fibronectin and collagen by means of affinity electrophoresis.

The interaction between human plasma fibronectin and different types and forms of collagen were analysed by affinity electrophoresis at different pH values. The fibronectin bound tightly to collagen type I, III and IV, but not to type V. The fibronectin interacted better with the denatured form of collagen type I (gelatin) than with the native form. At pH less than 5.5 the fibronectin exhibited much lower affinity to gelatin than at pH greater than 8.0. The interaction between the fibronectin and gelatin was further analysed by affinity electrophoresis in which apparent dissociation constants (Kd) of the fibronectin for gelatin were calculated, and effects of urea, 2-mercaptoethanol and temperature on the interaction were examined. The fibronectin markedly diminished its affinity to gelatin at 3 M urea to give Kd = 2.5 x 10(-6) M, which was 1000 times larger than the value without urea. The fibronectin dissociated into its monomers and the monomers diminished their affinity to gelatin in a stepwise fashion with increase in concentration of 2-mercaptoethanol. The fibronectin diminished the affinity to gelatin by elevating temperature, and van't Hoff plots of log Kd values against the reciprocal of absolute temperature (T) showed that log Kd was inversely proportional to 1/T in the range 15-50 degrees C, and the thermodynamic parameters of the standard enthalpy change, the standard free energy change and the entropy change at 37 degrees C for association of fibronectin and gelatin were all negative. At 60 degrees C the affinity of fibronectin to gelatin was not detectable.(ABSTRACT TRUNCATED AT 250 WORDS)

Collagen↗
PubMed1992

Effect of glow discharge surface modification of plasma TFE vascular graft material on fibronectin and laminin retention and endothelial cell adhesion.

The effects of glow discharge surface modification of plasma TFE vascular graft material (plasma TFE, Atrium Medical Corp., Hollis, NH) on the binding and retention of fibronectin and laminin as well as endothelial adherence were examined. The binding of both fibronectin and laminin to plasma TFE increased as a function of protein concentration in the range of 0.02 to 200 micrograms/ml. Binding to plasma TFE was not saturable in this range of protein concentrations. Fibronectin and laminin binding to plasma TFE was time-dependent, reaching a maximal level (1.8 and 3.2 micrograms/cm2 of bound fibronectin and laminin, respectively) after 30 min (fibronectin) and 4 hr (laminin). Binding was not the result of an accumulation of unbound protein in graft interstices since graft prewetting did not alter the amount of either fibronectin or laminin associated with plasma TFE. In addition, binding was not the result of protein modification during radiolabeling, since unlabeled fibronectin and laminin could compete effectively with their iodinated counterparts for binding to plasma TFE. Dissociation of bound fibronectin and laminin from plasma TFE was rapid, and less than 12% remained bound 60 min after washing. Plasma TFE subjected to glow discharge in O2 and carrying negatively charged functional groups on graft surfaces, exhibited a fivefold increase in fibronectin and laminin binding. In addition, more than 85% of the bound fibronectin and laminin was retained 24 hr after washing. The enhanced retention of fibronectin or laminin by these grafts was associated with an increase in endothelial cell adhesion.(ABSTRACT TRUNCATED AT 250 WORDS)

Ammonia↗