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PubMed1984

Temporal and spatial regulation of fibronectin in early Xenopus development.

Pattern formation and temporal control of gene expression in Xenopus development were investigated using fibronectin as a biochemical marker. We determined the spatial localization of fibronectin in the embryo by immunofluorescence and the temporal program of its expression by biosynthesis studies and Western blotting techniques. At the start of gastrulation, fibronectin is localized on the roof of the blastocoel which serves as the surface upon which mesodermal cells will migrate. However, since we find fibronectin secreted by all parts of the embryo, localization is probably achieved through spatially localized receptors that bind secreted fibronectin. Fibronectin levels and fibronectin synthesis rates increase following the midblastula stage. This increase is independent of transcription and therefore involves activation of maternal RNA for fibronectin. Since this message mobilization also occurs in activated but unfertilized eggs, this event must be regulated separately from the midblastula transition.

Animals↗
PubMed1982

Fibronectin interacts with Clq, a subcomponent of the first component of complement.

Human Clq, a subcomponent of the first component of complement interacts with human fibronectin. Using ELISA methodology fixation of Clq to solid phase fibronectin, as well as fibronectin to solid phase Clq has been demonstrated. Cl in its native macromolecular form displays little reactivity for fibronectin, nor does Cl reconstituted from Clq, Clr and Cls in the presence of Ca2+ ions. Heating of Clq above its thermal transition temperature (51 degrees C) induces an increased binding capacity for fibronectin. On the other hand, a mixture of the dissociated A, B and C chains of Clq is less active than native Clq. The binding of fibronectin appears to be mediated by the A chain. Studies with Clq deprived of its globular parts by peptic digestion indicate that the collagen-like regions of Clq are involved in fibronectin binding. In contrast, collagenase treatment of Clq abrogates its fibronectin binding capacity.

Animals↗
PubMed1988

Interaction between cell-binding domain and extracellular matrix-binding domain of fibronectin determined by fluorescence depolarization.

Interaction of domains in fibronectin was observed by photometry of fluorescence polarization of three kinds of dye; [N-(1-anilinonaphthyl-4)]maleimide (ANM tau = 5 ns), [N-(3-fluoranthyl)]maleimide (FAM tau = 20 ns), and [N-(3-pyrene)]maleimide (PRM tau = 100 ns). Each dye was labeled at a free sulfhydryl group in the cell-binding domain. Neither fluorescence of ANM with short fluorescent lifetime, FAM with long lifetime, nor PRM with longer fluorescent lifetime on fibronectin depolarized as much as the free dye. It was found that each dye was firmly fixed in the cell-binding domain. When heparin or gelatin was added in the solution of PRM-fibronectin complex, the fluorescence polarization tended to increase principally by combining heparin or gelatin to fibronectin. It was found that the rotation of whole or partial fibronectin containing the cell-binding domain through fluorescent lifetime of 100 ns was suppressed by combining of heparin or gelatin to fibronectin. When heparin or gelatin was added in the solution of ANM- or FAM-fibronectin complex, on the contrary, the fluorescence polarization tended to decrease, that is, slightly depolarize through the fluorescent lifetime of 5 or 20 ns, respectively. It was found that the rotation of the cell-binding domain, or of part of the fibronectin molecule containing the domain, was slightly promoted by combining heparin or gelatin to its domain. These results indicate that an interaction of the heparin- or gelatin-binding domain with the cell-binding domain was induced by the combining of heparin or gelatin to the respective domains.

Animals↗
PubMed1984

Modifications of fibronectin in age-related diseases: diabetes and cancer.

Fibronectin is present in tissues and also in body fluids (plasma). Both forms were studied in normal controls, diabetics and cancer patients; both of these diseases show an age-dependent increasing trend. Age-dependent variations were shown to occur for both forms of fibronectin. Plasma fibronectin increases exponentially with age in a normal population. This increase is strongly attenuated or absent in diabetics and in mammary cancer patients. On the contrary, tissue fibronectin increases in diabetic skin. In mammary cancer fibronectin disappears from the tumor cell membranes but increases in the peritumoral stroma. The above modifications may be attributed to increased protease activity in tumour tissue and also to the possibility of an increased retention of plasma fibronectin in diabetic skin and peritumoral stroma, both tissues exhibiting a modification of intercellular matrix biosynthesis which does involve the increased production of retention sites of fibronectin. An increased local synthesis in both tissues may also occur. The above results are confronted with those reported by other authors and support the contention that plasma and tissue fibronectins undergo age-dependent modifications which may be seriously perturbed in diabetes and cancer.

Adolescent↗
PubMed1996

Specific sequences of fibronectin activate the protein kinase C signal transduction pathway in invasive bladder cancer.

The mechanism of human bladder cancer cell invasion is not clear, but it appears that extracellular matrix components, such as fibronectin, may be involved. To investigate the role of fibronectin in tumor cell invasion and progression, we used an in vitro invasion assay to define the motility stimulating fragment of fibronectin for invasive human bladder cancer T24 cells. Using a modified Boyden chamber assay and purified fragments of fibronectin, we demonstrated that both the 120 kDa chymotrypsin generated fragment of fibronectin (containing the cell attachment RGD motif and additional sequences towards the carboxyl-terminal heparin binding domain), as well as the trypsin generated 60 kDa fragment of fibronectin (containing the carboxyl-terminal heparin binding domain and additional sequences towards the cell attachment RGD motif), were able to stimulate the migration of invasive human bladder cancer T24 cells. Control fragments containing only the amino-terminal gelatin binding region of fibronectin did not stimulate the motility of the human bladder cancer T24 cells. To determine the molecular mechanism in which these fragments may stimulate the migration of the T24 cells, we assayed for intracellular signal transduction pathway protein kinase C (PKC). We demonstrated that both the 120 kDa and the 60 kDa fragments were able to stimulate the activation of protein kinase C. Non-motility stimulating fragments of fibronectin were not able to activate protein kinase C. We conclude that the PKC signal transduction pathway may be involved in matrix mediated motility, and suggest that the inhibition of such pathway(s) may alter the malignant phenotype of human bladder cancer.

Amino Acid Sequence↗
PubMed1980

Biosynthetic processing of the oligosaccharide chains of cellular fibronectin.

We have examined the maturation or processing of the oligosaccharides of cellular fibronectin in cultured chick embryo fibroblasts. Fibronectin was pulse-labeled with [2-3H]mannose of [35S]methionine, and the turnover rates of carbohydrate and polypeptide portions of immunoprecipitated fibronectin were compared. The oligosaccharides on fibronectin were analyzed by gel electrophoresis for alterations in sensitivity to the enzyme endo-beta-N-acetylgluosaminidase H, which specifically cleaves the 'high-mannose' class of asparagine-linked oligosaccharide. Incorporated mannose was removed only at early time points, suggesting that the structure of fibronectin oligosaccharides was altered due to processing. This possibility was confirmed by the analysis of glycopeptides generated by exhaustive pronase digestion. Two major glycopeptide structures were detected; their properties correspond to a 'high-mannose' oligosaccharide precursor and a 'complex' carbohydrate product. The precursor-product relationship of these two forms of oligosaccharide chains was demonstrated by pulse-chase labeling experiments. The precursor glycopeptide had an apparent size (Mr 2100) comparable to (Man)9GlcNAc (Mr 2080), and was sensitive to endo-beta-N-acetylglucosaminidase H; nearly all of the labeled mannose incorporated in a 10 min pulse was released from fibronectin glycopeptides by this enzyme. During a 90 min chase period, the glycopeptides became larger and increasingly resistant to endo-beta-N-acetylglucosaminidase H cleavage. The final 'complex' or processed oligosaccharide structure contained approximately two-thirds less [3H]mannose, was insensitive to endo-beta-N-acetylglucosaminidase H and had an apparent Mr of 2300 as estimated by gel filtration. We conclude that the carbohydrate portion of fibronectin is synthesized as a 'high-mannose' intermediate and is subsequently processed to give the characteristic 'complex' oligosaccharide chains of fibronectin.

Acetylglucosaminidase↗
PubMed1984

Fibronectin mediated human gingival fibroblasts attachment to bone.

Experiments were undertaken to examine the effects of acid and fibronectin treatments on the human gingival fibroblast attachment to bone in vitro. The binding of [125I]fibronectin to bone powders was dependent on concentration of fibronectin and incubation time. The optimum pH of [125I]fibronectin attachment to bone powders was 6.0 using phosphate buffer. Acid treatment on bone powders in low concentration such as 10 mM of citric acid enhanced [125I]fibronectin binding. The attachment of [3H]thymidine labelled human gingival fibroblasts to bone was enhanced 1.5, 2.0 and 2.5-fold by citric acid, fibronectin and citric acid + fibronectin treatment, respectively. Scanning electron microscopic observations confirm that citric acid and/or fibronectin treatment enhanced the cell number and rapidity of fibroblast attachment to bone surfaces.

Animals↗
PubMed1992

Role of fibronectin in the adherence of Staphylococcus aureus to dermal tissues.

Staphylococcus aureus has a fibronectin receptor on its surface. Fibronectin seems to play a role in the initiation and modification of infection with S. aureus. We studied the role of fibronectin in the binding of S. aureus (clinical isolates) to dermal tissues in mice, and the relationship between the fibronectin binding ability of S. aureus and clinical features of S. aureus skin infections. Mice were inoculated with S. aureus incubated with gold-particles bound fibronectin and skin specimens were taken for electron microscopic examination. The number of gold particles surrounding the S. aureus cells decreased with time, with none detected 4 h after inoculation. At both 5 min and 1 h after inoculation, gold particles were only found on the free surface of S. aureus cells and not in the interface between S. aureus cells and fibroblasts. Fibronectin-bound gold particles were bound more extensively to S. aureus strains isolated from furunculosis or furuncle than to those from bullous impetigo. These results suggest that the matrix fibronectin on the surface of the fibroblasts of mice contributes to the adherence of S. aureus to the fibroblasts, and that the number of fibronectin binding sites on S. aureus cells is related to the degree of local invasiveness.

Animals↗
PubMed1992

Mycobacterium paratuberculosis binds fibronectin.

Fibronectin, an adhesive glycoprotein which is present in plasma and on many host cell surfaces of many host organisms, binds to certain bacterial pathogens. This study demonstrates the ability of Mycobacterium paratuberculosis (M.ptb) to interact with 125I-labelled fibronectin purified from bovine and ovine plasma. Two M.ptb strains were tested: a clinical isolate and a commercially available vaccine strain. Both strains showed significant fibronectin-binding activities of 22 and 41%, respectively, whereas non-pathogenic M.phlei had almost no affinity for fibronectin. Binding activities were similar for ovine and bovine fibronectin. We found that fibronectin binding by M.ptb was (1) time-dependent, reaching saturation within 90 min, (2) specific, since it was inhibited by an excess of unlabelled fibronectin but not by albumin, (3) saturable, with an apparent dissociation constant of 1.25 x 10(-9) M and a maximal number of 1,600 binding sites per bacterium, and (4) sensitive to detergents, proteases and heat treatments, indicating the protein nature of the responsible binding component(s). Scatchard plot analysis gave a straight line suggesting the presence of a single type of fibronectin receptor on M.ptb.

Animals↗
PubMed2004

Immunolocalization of integrins and fibronectin in tubal pregnancy.

Integrins are a large family of cell adhesion molecules that serve as receptors involved in cell-to-cell and cell-to-matrix interactions during implantation. We studied immunohistochemical staining of integrins (alpha 3, alpha V, beta 1, and alpha 2 beta 1) and fibronectin in ectopic tubal pregnancy. Thirty fallopian tube samples with ectopic pregnancies and five normal tubal segments were obtained during ligation operations; the latter specimens served as controls in the study. Formalin-fixed paraffin-embedded tissue sections were stained with hematoxylin-eosin or primary antibodies against alpha 3, beta 1, alpha V, and alpha 2 beta 1 integrins and fibronectin, using the avidin-biotin-peroxidase method. A semi-quantitative grading system was used to compare staining intensities. In the control samples, immunostaining of all integrins was found in a single layer of tall columnar epithelial cells, the lamina propria (Lp) and the muscular layer. Fibronectin staining was detected in the Lp and the muscular layer. Staining intensities of alpha 3 and beta 1 integrins and fibronectin were increased in the normal part of fallopian tubes with ectopic pregnancies. Staining of beta 1 integrin was more intense than staining of alpha 3 and fibronectin, whereas there was no difference in alpha V and alpha 2 beta 1 integrin expression between normal tubal tissue in the ectopic pregnancy group and control tubal tissue. In the tubal pregnancy group at the site of implantation, staining intensity of alpha 3 and beta 1 integrins and fibronectin was strong in decidual cells, supporting tissue and placental villi, whereas alpha V and alpha 2 beta 1 staining was mild. We concluded that integrins, especially beta 1 and alpha 3, and fibronectin may play a role in progression of tubal implantation. Although the role of integrins has not yet been clearly defined, these molecules may function as markers of normal and abnormal states of receptivity. We like to suggest that integrins and fibronectin, which are needed in utero implantation, are expressed in tubal tissues during ectopic pregnancy and are involved in ectopic implantation.

Decidua↗
PubMed2004

Vaginal fetal fibronectin as a predictor of spontaneous preterm delivery after multifetal pregnancy reduction.

OBJECTIVE: The study was undertaken to assess the validity of vaginal fetal fibronectin assay as a screening test for spontaneous preterm delivery in asymptomatic patients who have undergone multifetal pregnancy reduction (MFPR). STUDY DESIGN: A historic cohort of 63 patients who underwent MFPR between 10 and 14 weeks of gestation was identified. All patients underwent serial vaginal fetal fibronectin sampling every 2 to 3 weeks from 22 weeks of gestation until delivery or 32 weeks of gestation. The fetal fibronectin concentration was measured by enzyme-linked immunosorbent assay, with 50 ng/mL or greater indicating a positive result. Charts were reviewed for fetal fibronectin results and pregnancy outcome data. Groups were compared by use of Fisher exact test. RESULTS: There were 13 singleton and 50 twin gestations after MFPR. A median of 4 fetal fibronectin assays were performed per patient. A total of 234 fetal fibronectin assays were performed with 222 (94.9%) negative results and 12 (5.1%) positive results. Overall, 41.3% of gestations were delivered spontaneously before 37 weeks; 7.9% were delivered before 34 weeks. The mean interval between tests was 17.8 days (+/-7.2 days). For delivery within 2 and 3 weeks of a single test, fetal fibronectin had a sensitivity of 66.7% and 50%, a specificity of 95.7% and 96.1%, a positive predictive value of 16.7% and 25%, and a negative predictive value of 99.5% and 98.6%, respectively. CONCLUSION: The fetal fibronectin test has similar validity to predict spontaneous preterm delivery in these high-risk pregnancies as in previously published cohorts.

Enzyme-Linked Immunosorbent Assay↗
PubMed2004

Identification and characterization of bacterial-binding property in the type III repeat domain of fibronectin.

To characterize fibronectin binding with Granulicatella adiacens, a causative agent of infective endocarditis, monoclonal antibodies were generated against human fibronectin and selected for their capacity to inhibit the fibronectin binding of the organism. Thermolysin and lysyl-endopeptidase digests of fibronectin were characterized by Western blot. The epitope of inhibitory monoclonal antibody was found in the central portion of fibronectin known as the cell-binding domain, and not in the N-terminal portion known to be the binding region of most microbial species, e.g., Staphylococcus aureus and Streptococcus pyogenes. While these two species could bind to both the N-terminal and central portion, Escherichia coli and G. adiacens bind only to the latter. Excess amounts of free fibronectin in the solution inhibited the bacterial adherence to the N-terminal fibronectin fragment, but not to the central region, thereby suggesting the central region plays a significant role for in vivo bacterial colonization in the presence of high concentrations of soluble fibronectin.

Animals↗
PubMed2006

Selective control of liver and kidney cells migration during organotypic cocultures inside fibronectin-coated rectangular silicone microchannels.

In this work, the behaviors of embryonic liver and kidney explants were studied inside rectangular polydimethylsiloxane (PDMS) microchannels. The organs were cultured under monoculture and coculture conditions on PDMS coated with or without fibronectin. The results demonstrated that the migration of cells from both organs is dependent on culture conditions and thus can be selectively controlled. In liver monocultures without fibronectin, cell migration in the microchannels resulted in the formation of a dense 3D tissue. Fibronectin reduced liver cell migration and enhanced the emergence of cells demonstrating typical hepatocyte phenotypes at the vicinity of the explant. The migration rate in liver-liver cocultures, with and without fibronectin, was roughly twice the rate of cells under monoculture conditions. In cocultures, both livers merged to form a large tissue in which the two initial organs could not be identified. In kidney monocultures, with and without fibronectin, we did not observe any migration inside the microchannels. Contrary to liver cells, kidney cell migration was triggered when both fibronectin coating and coculture with liver or another kidney explant were used. The migration was more largely observed in coculture with liver when compared to kidney-kidney cocultures. In the case of liver-kidney coculture with fibronectin, the progression of the kidney cells inside the microchannels appears as a displacement of the entire kidney explant in the direction of the liver. The liver cells did not move in those cases. After contact, we observed a complete merging of both liver and kidney explants. In contrast, for liver-kidney cocultures without fibronectin, only the liver moved toward the kidney.

Animals↗
PubMed2004

Trabecular cell expression of fibronectin and MMP-3 is modulated by aqueous humor growth factors.

We investigated the mRNA and protein expression of fibronectin and stromelysin-1 (matrix metalloproteinase-3, MMP-3) by trabecular cells treated with growth factors present in primary and secondary aqueous humors. Serum-deprived trabecular cells were incubated for 48 hr or 7 days in medium containing either primary or secondary aqueous humor growth factors or in serum-free medium. We extracted total RNA, performed reverse transcription-polymerase chain reaction using primer pairs for fibronectin, stromelysin-1 and glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and quantified the products. We utilized Western blotting to detect and quantify fibronectin and stromelysin-1 protein. Compared to controls, expression of fibronectin mRNA by trabecular cells was increased by 50 and 100% after incubation in primary aqueous humor growth factors for 48 hr or 7 days, respectively, and 50 and 130% after incubation in secondary aqueous humor growth factors. Stromelysin-1 mRNA expression was decreased by 25 and 50% after incubation in primary aqueous humor growth factors for 48 hr or 7 days, respectively, and 80 and 85% after incubation for 48 hr or 7 days, respectively, in secondary aqueous humor growth factors. Fibronectin protein increased 3.5-fold and 6-fold after incubation for 48 hr with primary or secondary aqueous humor growth factors, respectively; after 7 days, the level increased 4- and 7-folds, respectively. Stromelysin-1 protein was not detectable by western blotting. The up-regulation of fibronectin mRNA by trabecular cells exposed to growth factors present in secondary aqueous humor augmented by the down-regulation of stromelysin-1 mRNA contributed to the accumulation of fibronectin. Our findings open the possibility that induction of stromelysin-1 gene expression in the trabecular meshwork of glaucomatous eyes could effectively reduce buildup of fibronectin in the aqueous outflow pathway to decrease outflow resistance in glaucomatous states of the eye.

Animals↗
PubMed2005

Fibronectin fibrillogenesis, a cell-mediated matrix assembly process.

The extracellular matrix provides a framework for cell adhesion, supports cell movement, and serves to compartmentalize tissues into functional units. Fibronectin is a core component of many extracellular matrices where it regulates a variety of cell activities through direct interactions with cell surface integrin receptors. Fibronectin is synthesized by many adherent cells which then assemble it into a fibrillar network. The assembly process is integrin-dependent and fibronectin-integrin interactions initiate a step-wise process involving conformational activation of fibronectin outside and organization of the actin cytoskeleton inside. During assembly, fibronectin undergoes conformational changes that expose fibronectin-binding sites and promote intermolecular interactions needed for fibril formation. In this review, the main steps of fibronectin assembly are described and recent studies on fibronectin conformational changes are discussed.

Actins↗
PubMedDate not supplied

Bacteria-associated fibronectin does not enhance Chlamydia trachomatis infectivity in vitro.

The molecules responsible for mediating attachment of pathogenic bacteria to their host cells are essential determinants of the pathogen's success. Staphylococci, streptococci, and gonococci are known to utilize fibronectin to mediate adhesion and/or entry into eukaryotic cells. It has been shown that Chlamydia trachomatis binds fibronectin via a heparan sulfate-lyase sensitive molecule on the surface of the bacteria. Because heparan sulfate-lyase treated Chlamydia are markedly reduced in infectivity, we hypothesized that fibronectin might be acting as an intermediate to form a molecular bridge between heparan sulfate-like molecules on the surface of Chlamydia and integrins on the host cell. To test this question, fibronectin-deficient C. trachomatis were used in a series of infectivity assays whereby exogenous fibronectin was added to the inoculum. At concentrations up to 100 ug/ml fibronectin did not modulate C. trachomatis infectivity. However, at high fibronectin concentrations (1 mg/ml) bacterial infectivity was reduced. These data suggest that, unlike several other microbial pathogens, C. trachomatis does not utilize fibronectin to mediate infectivity in vitro.

Animals↗
PubMed1997

Effect of aprotinin on plasma fibronectin levels during cardiopulmonary bypass.

BACKGROUND: Acute depletion of plasma fibronectin levels has been reported during and after cardiopulmonary bypass; degradation of fibronectin by proteolytic enzymes has been suggested as one of the causes. This study was designed to assess the possible preservation of fibronectin levels by aprotinin during cardiopulmonary bypass. METHODS: Plasma fibronectin levels were evaluated in 19 patients undergoing either elective coronary artery bypass grafting or a valvular heart operation. The study was conducted prospectively in a controlled, randomized, double-blinded manner. Nine test patients (group A) received intraoperative, intravenous administration of aprotinin; 10 control patients (group B) received equivalent volume of normal saline solution. Fibronectin levels were measured immediately after induction of anesthesia (as the baseline for the study) and at the following times: after 5 minutes on bypass, after 30 minutes on bypass, immediately before the start of rewarming, and after being off bypass for 5 minutes, but before protamine administration. RESULTS: Both groups' basic characteristics were very similar. Group A patients were found to have significantly greater fibronectin levels than group B during and immediately after cardiopulmonary bypass (p < 0.002). CONCLUSIONS: Administration of aprotinin intraoperatively appears to result in better preservation of fibronectin levels during cardiopulmonary bypass. Although the mechanism of action of aprotinin as a proteolytic inhibitor remains unclear, it has been suggested that it exerts an inhibiting effect on proteolytic enzymes by forming an aprotinin-proteinase complex. The clinical implications of the greater level of fibronectin achieved by the intraoperative use of aprotinin during cardiopulmonary bypass need further evaluation.

Aprotinin↗
PubMed1986

Tracheal lavage and plasma fibronectin: relationship to respiratory distress syndrome and development of bronchopulmonary dysplasia.

Plasma for fibronectin determinations was obtained from 39 neonates with uncomplicated respiratory distress syndrome (RDS) and from 15 infants with RDS who developed bronchopulmonary dysplasia (BPD). Tracheal lavage fibronectin and albumin concentrations were measured in 15 infants with RDS and 15 with BPD. Control plasma fibronectin values were obtained from 20 healthy preterm infants on days 1, 2, 3, 14, and 30 of life. Control tracheal lavage fibronectin and albumin concentrations were measured in 17 neonates of various gestational ages who required tracheal intubation for nonpulmonary indications. Mean plasma fibronectin concentrations from patients with RDS was 121 +/- 11 micrograms/ml on days 1, 2, and 3, versus control level of 163 +/- 12 micrograms/ml (P less than 0.01). Mean tracheal lavage fibronectin/albumin ratio was 3.8 +/- 0.6 ng per microgram of albumin on days 1 to 5 for infants with RDS, versus control level of 5.6 +/- 3.6 (P = NS). Tracheal lavage fibronectin/albumin ratio from patients with BPD was elevated at 16.3 +/- 5.0 ng fibronectin per microgram of albumin on days 14 to 21, and 23.6 +/- 7.4 on day 30 (P less than 0.05 versus control and and versus RDS days 1 to 10). Low plasma fibronectin concentrations early in RDS may contribute to the development of pulmonary capillary leak. High tracheal lavage fibronectin levels may foster the development of pulmonary fibrosis in patients with BPD.

Albumins↗