Chicken vertebral chondrocytes, which normally grow in suspension, synthesize large amounts of cartilage extracellular matrix proteins, but little fibronectin. We have analyzed the effects of both substrate attachment and transformation with a temperature-sensitive mutant of Rous sarcoma virus on fibronectin gene expression in these cells. Our experiments show that viral transformation increases fibronectin synthesis to a greater extent than substrate attachment. Furthermore, transformed chondrocytes have lost the ability to decrease fibronectin synthesis in response to suspension culture, suggesting that transformation alters the normal attachment-responsive control of fibronectin gene expression. Finally, infected substrate-attached chondrocytes shifted to the nonpermissive temperature for transformation use fibronectin RNA more efficiently in protein synthesis than cells grown under the other conditions, suggesting for the first time a role for translational control of fibronectin gene ...
TY - JOUR. T1 - Regulation of fibronectin gene expression by cyclic AMP and phorbol myristate acetate in HT-1080 human fibrosarcoma cells. AU - Lee, Byung Heon. AU - Park, Rang Woon. AU - Kim, In San. PY - 1998/12/31. Y1 - 1998/12/31. N2 - We studied the regulation of fibronectin (FN) gene expression by cAMP and phorbol-12-myristate-13-acetate (PMA) in HT-1080 human fibrosarcoma cells. Dibutyryl cAMP increased FN synthesis and mRNA levels, while PMA inhibited the cAMP-induced FN synthesis. In transient transfection assays, cAMP increased FN promoter activity, while PMA paradoxically enhanced the cAMP-induced promoter activity. Stable transfection experiments, however, showed that neither cAMP or PMA alone nor together affected FN promoter activity. These results suggest that PMA antagonizes the cAMP-induced FN gene expression and that both the action of cAMP and the inhibition of its action by PMA may occur at the posttranscriptional level in HT-1080 cells.. AB - We studied the regulation of ...
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It has been well documented that the extracellular matrix components fibronectin and laminin promote or regulate morphogenesis of the myocardial cells in mammalian heart. However, their chronological change of expression (or localization) in the human heart remains elusive. In this study, fibronectin and laminin in the left ventricle of forty-two human fetuses aged from 8 to 26 weeks gestation and left ventricular tissues obtained from a 2-week old infant and two adults were investigated by Western blot analyses and indirect immunofluorescence technique with monoclonal antibodies. In the fetal heart, fibronectins were present along the endocardium, epicardium, and linings of larger blood vessels. In 14-16 weeks gestation, fibronectin immunofluorescence became stronger but not evenly dispersed in the interstitium. After 24 weeks gestation, they were strongly positive only in the relatively larger blood vessels, as well as those in the infant and adult cardiac tissues. Laminins were strongly positive
Cells interact with extracellular fibronectin (FN) via adhesive fibronectin receptors (FNRs) that are members of the very late antigens (VLAs) subgroup of the integrin family. In stationary fibroblasts, the FNR is highly organized and distributed identically to extracellular FN fibrils. However, in highly migratory neural crest cells and embryonic somatic fibroblasts, this organization is lost and the FNR appears diffuse. Similarly, oncogenic transformation typically leads to disorganization of the FN receptor and loss of matrix FN. Two models can account for these observations. First, the FN matrix may organize the FN receptor at extracellular matrix contacts on the cell surface. Motile cells not depositing FN matrices thus lack organized receptors. Alternatively, as the FNR is required for optimal FN matrix assembly, (McDonald, J. A., B. J. Quade, T. J. Broekelmann, R. LaChance, K. Forseman, K. Hasegawa, and S. Akiyama. 1987. J. Biol. Chem. 272:2957-2967; Roman, J. R. M. LaChance, T. J. ...
Staphylococcus aureus cells have been shown to possess surface-associated proteins with affinity for soluble fibronectin. We have investigated the ability of these surface proteins to mediate attachment to immobilized fibronectin and collagen. Attachment was quantified by determination of bacterial ATP in a bioluminescence assay. The ability to attach to fibronectin- or collagen-coated plastic surfaces was investigated for four S. aureus strains: Cowan 1, Newman, SA113(83A), and Wood 46. Cells from the different strains varied in their attachment properties, but all cells except those of strain Wood 46 attached readily to substrates coated with fibronectin. Only cells from strain Cowan 1 attached reproducibly to collagen-coated substrates in the absence of fibronectin. The attachment of cells from strain SA113(83A) to fibronectin-coated surfaces was shown to be dependent on time, fibronectin concentration, and bacterial growth phase. Soluble fibronectin or NH2-terminal fibronectin fragment (Mr, ...
Carcinogenesis is a multistep process which involves interplay between the tumour cells and the matrix proteins. This occurs by adherence between the tumour cells and proteins in the extracellular matrix. VHL mutation affects through the hypoxia inducible factor (HIF) and causes changes in various tissue proteins like VEGF, PDGF, TGF, Fibronectin and others. As not much literature is available, we aim to quantify the changes of fibronectin protein in renal cell carcinoma (RCC) tissue. This Prospective unbalanced case control study was conducted over a period of 18 months from April 2016 to September 2017. The patients undergoing nephrectomy for the diagnosis of RCC were included in the study after obtaining written informed consent. Patients were excluded from study, if normal renal tissue could not be identified in the resected kidney and if the artery clamp time to retrieval of tissue was more than 30 min. Fibronectin protein is estimated in the tumour tissue by gel electrophoresis and western
Fibronectin is a large vertebrate glycoprotein that is found in soluble and insoluble forms and involved in diverse processes. Protomeric fibronectin is a dimer of subunits, each of which comprises 29-31 modules - 12 type I, two type II and 15-17 type III. Plasma fibronectin is secreted by hepatocytes and circulates in a compact conformation before it binds to cell surfaces, converts to an extended conformation and is assembled into fibronectin fibrils. Here we review biophysical and structural studies that have shed light on how plasma fibronectin transitions from the compact to the extended conformation. The three types of modules each have a well-organized secondary and tertiary structure as defined by NMR and crystallography and have been likened to beads on a string. There are flexible sequences in the N-terminal tail, between the fifth and sixth type I modules, between the first two and last two of the type III modules, and at the C-terminus. Several specific module-module interactions have been
An expression vector containing a cDNA complementary to 1.3 kb of the 5′ coding sequences of the fibronectin gene in the antisense orientation with respect to its promoter was introduced by electroporation into hybrids between melanoma cells and normal fibroblasts in which malignancy was suppressed. Immunofluorescence analysis of clones transfected with the antisense cDNA showed a dramatic decrease in the amount of fibronectin on the cell surface compared to that seen on the surface of the untransfected hybrid cells or of cells transfected with fibronectin cDNA in the sense orientation or with the expression vector alone. Four out of five clones transfected with the antisense cDNA were highly tumorigenic, whereas transfectants containing either the sense fibronectin construct or the expression vector alone remained non-tumorigenic. These results suggest that antisense RNA to fibronectin may be able to abrogate the suppression of malignancy imposed on the hybrid cells by the fibroblast parent. ...
Since the initial description in 1986,29 numerous authors have described TGFβs ability to upregulate fibronectin synthesis in a host of different cell types. We began our studies by reconfirming that TGFβ upregulates the level of both fibronectin protein and mRNA in A10 aortic SMCs. Our findings were in accordance with those of others who have shown that the induction of fibronectin is a general response of vascular SMCs to TGFβ.. Although Smad proteins are well established as signal mediators downstream of TGFβ receptors, whether TGFβ stimulates fibronectin expression through a Smad-dependent pathway is controversial. Using various mutants of TGFβ type I receptor, Itoh et al showed that TGFβ-induced fibronectin expression requires activation of Smad proteins.30 Moreover, the authors demonstrated that the TGFβ-mediated fibronectin induction is absent in a Smad4-deficient cell line, MDA-MB-468, and this TGFβ dysfunction can be rescued by ectopic Smad4 expression. Here, in VSMCs, we ...
The level of fibronectin (FN) gene transcription in resting rat 3Y1 cells is very high but decreases steeply after growth stimulation by serum or by the induction of E1A expression. To study the mechanism of this E1A-mediated down-regulation, the 5 flanking regions of the FN gene with various deletions and substitutions were fused to the Escherichia coli chloramphenicol acetyltransferase (CAT) gene and introduced into resting 3Y1 cells with E1A expression plasmids. The results indicate that the G10 stretch located from nucleotide position -239 to -230 and two GC boxes from position -105 to -95 and position -54 to -44 are the primary E1A-responsive elements for repression of the FN gene. Two GC boxes also contain a G10 stretch that is interrupted by the presence of an internal C residue. These sequences overlap with the Sp1 motif GGGCGG. Substitution of the sequence GGGG with ATCC or CTTA in these G-rich sequences, leaving the Sp1 motif intact, completely abolished the E1A sensitivity of the ...
Abstract. Recent studies have pointed to changes in tissue mechanics as a contributory element to the development of malignancies. Increased tissue rigidity is associated with the unfolding of the Type III domains of fibronectin within the extracellular matrix. The consequences of this unfolding on cellular functions within the lung are not well understood. In the present study, we evaluated the effect of a peptide representing a partially unfolded intermediate of the first Type III repeat of fibronectin (FnIII-1c) on inflammatory gene expression in adult human lung fibroblast cells. FnIII-1c induced expression of cytokines, CXCL1-3, IL-8 and TNF-α, by lung fibroblast cells. The increase in IL-8 expression was dependent on Toll-like receptor 2 and NFκB. Immunohistochemistry of tissue arrays representing squamous cell carcinoma of the lung revealed extensive stromal staining for IL-8 and fibronectin fibrils which were co-aligned with myofibroblasts. These data suggest a model in which unfolding ...
TY - JOUR. T1 - Proteolysis regulates exposure of the IIICS-1 adhesive sequence in plasma fibronectin. AU - Ugarova, Tatiana. AU - Ljubimov, Alexander V.. AU - Deng, Lynn. AU - Plow, Edward F.. PY - 1996. Y1 - 1996. N2 - The alternatively spliced type III connecting segment (IIICS) of fibronectin (Fn) contains an amino acid sequence, CS-1, which is recognized by the integrin receptor, α4β1. Plasma Fn inhibits α4β1-dependent binding of lymphocytes and monocytes to CS-1 containing Fn derivatives poorly, suggesting limited exposure of the CS-1 sequence in Fn. To test the availability of CS-1 in plasma Fn, an antibody was raised to the synthetic peptide CS-1. The CS-1 sequence was found to be minimally exposed in plasma Fn: and immobilization of Fn, a model of matrix deposition, caused only a modest increase in its exposure. Digestion of Fn with selected proteases, however, induced substantial expression of the CS-1 sequence. The acid protease cathepsin D generated fragments of 31-33.5 kDa from ...
Introduction: Atherosclerosis is an inflammatory disease that develops preferentially in regions of disturbed hemodynamic shear stress. The extracellular matrix protein fibronectin (FN) is deposited in the sub-endothelial layer of pre-atherosclerotic and advanced lesions. Atheroprone shear stress promotes FN deposition and inflammatory signaling pathways in endothelial cells (ECs). Platelet endothelial cell adhesion molecule (PECAM), a mechanosensory protein, is necessary for the production, secretion, and assembly of FN matrix by ECs. Similar to ECs, vascular smooth muscle cells (SMCs) also display a pro-inflammatory phenotype in regions of atherogenesis, and this phenotype is key to the progression of atherosclerosis.. Hypothesis: We hypothesize that endothelial PECAM and FN signaling promotes a pro-inflammatory smooth muscle cell phenotype in response to atheroprone shear stress patterns.. Methods: An in vitro cone-and-plate viscometer model was used to apply human-derived atheroprone or ...
Defining fibronectins cell adhesion synergy site by site-directed mutagenesis.s profile, publications, research topics, and co-authors
Improve cell attachment by using cell culture surfaces coated with Corning human fibronectin (HFN) surface. HFN is produced by a wide variety of mesenchymal and epithelial cells, and is present in both the ECM and plasma. Cell adhesion to fibronectin is mediated by the central cell-binding domain of FN through RGD (Arg-Gly-Asp) amino acid sequence. The principal functions of fibronectin appear to be in cellular migration during wound healing and development, regulation of cell growth and differentiation, and haemostasis/thrombosis.. The Corning Fibronectin mimetic surface is a pre-coated, synthetic, xeno-free, animal-free, and room temperature stable surface that mimics the natural cell environment. Fibronectin surface consists of the RGD amino acid sequence from the Fibronectin cell binding domain that facilitates cell attachment. It is coated on the surface in a manner that presents a functionally active orientation to the cells. For difficult-to-transduce and fastidious cell types, look to ...
Improve cell attachment by using cell culture surfaces coated with Corning human fibronectin (HFN) surface. HFN is produced by a wide variety of mesenchymal and epithelial cells, and is present in both the ECM and plasma. Cell adhesion to fibronectin is mediated by the central cell-binding domain of FN through RGD (Arg-Gly-Asp) amino acid sequence. The principal functions of fibronectin appear to be in cellular migration during wound healing and development, regulation of cell growth and differentiation, and haemostasis/thrombosis.. The Corning Fibronectin mimetic surface is a pre-coated, synthetic, xeno-free, animal-free, and room temperature stable surface that mimics the natural cell environment. Fibronectin surface consists of the RGD amino acid sequence from the Fibronectin cell binding domain that facilitates cell attachment. It is coated on the surface in a manner that presents a functionally active orientation to the cells. For difficult-to-transduce and fastidious cell types, look to ...
Litvinov, R.I., Izmailov, S.G., Zinkevich, O.D. et al. Tensometric study of the effect of exogenous fibronectin on skin wound healing. Bull Exp Biol Med 104, 1736-1738 (1987). https://doi.org/10.1007/BF00836015. Download ...
LAN576Hu71, Biotin-Linked Polyclonal Antibody to Fibronectin Type III Domain Containing Protein 5 (FNDC5), FRCP2; Irisin; Fibronectin type III repeat-containing protein 2 | Products for research use only!
EPN576Hu61, Eukaryotic Fibronectin Type III Domain Containing Protein 5 (FNDC5), FRCP2; Irisin; Fibronectin type III repeat-containing protein 2 | Products for research use only!
Health,A test for fetal fibronectin can predict whether a pregnant woman is a...The fFN test has been approved by the U.S. Food and Drug Administrat...,Laboratory,Testing,Can,Identify,Risk,of,Pre-Term,Labor,and,,,Delivery,,,,medicine,medical news today,latest medical news,medical newsletters,current medical news,latest medicine news
Rabbit Polyclonal Anti-Fibronectin Antibody [HRP]. Mesenchymal Cells Marker. Validated: WB, IHC, IHC-P. Tested Reactivity: Human, Mouse, Rat, and more. 100% Guaranteed.
Rabbit Polyclonal Anti-Fibronectin Antibody [FITC]. Mesenchymal Cells Marker. Validated: ICC/IF, IHC, IHC-P. Tested Reactivity: Human, Mouse, Rat, and more. 100% Guaranteed.
Biorobot paper accepted!! 4 new papers in print related to protein unfolding Welcome to the Lab to new PhD student Ana from Ecuador. Cyberplasm receives media attention, here is the original press release living microrobot Congratulations to Orr Yarkoni for passing his PhD viva for a thesis entitled "Engineering an inducible NO pathway to facilitate cell-electronics communication" Congratulations to Darman Nordin for passing his PhD viva for a thesis entitled "Interaction of the extracellular matrix protein fibronectin with model cell membranes" ...
Fibronectin Antibody - With BSA and Azide, Mouse Monoclonal Antibody [Clone SPM539 ] validated in IHC-P, IF, FC (AH10465-20), Abgent
anti-Extracellular Leucine-Rich Repeat and Fibronectin Type III Domain Containing 2 (ELFN2) antibody (Alexa Fluor 647) ABIN905174 from antibodies-online
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U937 cells attach to the RGDS-containing 80-kD fragment of fibronectin (Fn). The present report examined whether these cells recognize other domains of Fn. U937 cells attach to a 38-kD fragment derived from the A chain of Fn, which includes the Hep II domain and most of the alternatively spliced IIICS region. U937 did not bind to a 58-kD fragment derived from the B chain (which lacks IIICS) and has the Hep II site. They also did not bind to a 31-kD COOH-terminal fibrin-binding fragment or to a 29-kD fragment containing the Hep I domain. Cell adhesion to the 38-kD fragment was not inhibited by the 80-kD fragment, by GRGDSPC synthetic peptides, or by a mAb directed to the RGDS-containing domain of Fn. Attachment was completely inhibited by the 38-kD fragment and by the synthetic peptide CS-1, comprising the first 25 amino acid residues of IIICS. These results indicate that U937 cells interact with two sites of Fn, the RGDS-containing region, and the IIICS region. ...
in Developmental Biology (1984), 101(2), 373-381. The appearance and distribution of the extracellular material glycoprotein, fibronectin, was investigated in gastrulating chick embryos using affinity-purified anti-human plasma fibronectin antibodies ... [more ▼]. The appearance and distribution of the extracellular material glycoprotein, fibronectin, was investigated in gastrulating chick embryos using affinity-purified anti-human plasma fibronectin antibodies. Preservation of tissue structure and immunoreactivity was carried out by ethanol/acetic acid fixation or by formaldehyde/glutaraldehyde fixation. Using the former fixation method, fibronectin immunoreactivity was detected (1) at the ventral surface of the upper layer or epiblast, mainly anterior and lateral to Hensens node, in regions where middle-layer or mesoblast cells are not yet present, and (2) sparsely in extracellular spaces of the deep layer. Using the latter fixation method, fibronectin immunoreactivity was, moreover, found ...
The process by which fibronectin (FN), a soluble multidomain protein found in tissue fluids, forms insoluble fibrillar networks in the extracellular matrix is poorly understood. Cryptic sites found in FN type III domains have been hypothesized to function as nucleation points, thereby initiating fibrillogenesis. Exposure of these sites could occur upon tension-mediated mechanical rearrangement of type III domains. Here, we present the solution structures of the second type III domain of human FN ((2)FNIII), and that of an interaction complex between the first two type III domains ((1-2)FNIII). The two domains are connected through a long linker, flexible in solution. A weak but specific interdomain interaction maintains (1-2)FNIII in a closed conformation that associates weakly with the FN N-terminal 30 kDa fragment (FN30 kDa). Disruption of the interdomain interaction by amino-acid substitutions dramatically enhances association with FN30 kDa. Truncation analysis of (1-2)FNIII reveals that the
Metastatic growth is considered a rate limiting step in cancer progression, and upregulation of extracellular matrix (ECM) deposition and cell-ECM signaling are major drivers of this process. Mechanisms to reverse ECM upregulation in cancer could potentially facilitate its prevention and treatment but they are poorly understood. We previously reported that the adhesion G-protein coupled receptor GPR56/ADGRG1 is downregulated in melanoma metastases. Its re-expression inhibited melanoma growth and metastasis and reduced the deposition of fibronectin, a major ECM component. We hypothesize that its effect on fibronectin deposition contributes to its inhibitory role on metastatic growth. To test this, we investigated the function of GPR56 on cell-fibronectin adhesion and its relationship with metastatic growth in melanoma. Our results reveal that GPR56 inhibits melanoma metastatic growth by impeding the expansion of micrometastases to macrometastases. Meanwhile, we present evidence that GPR56 inhibits
Fibronectin (FN) is transactivated by human papillomavirus type 16 (HPV16) E6 via the induction of c-Jun-ATF-2 complexes binding to the cyclic AMP response element (CRE) in the FN promoter. The present study analyzed c-Jun regulation of FN gene expression. Northern and immunoblot analyses showed that c-Jun expression was enhanced in HPV16-E6-expressing cells. However, mouse 10T1/2 cell lines overexpressing c-Jun showed an inverse correlation between the expression levels of c-Jun and those of FN. Luciferase assays indicated that the FN promoter was strongly repressed in c-Jun-overexpressing mouse 10T1/2 cells. Deletion and mutation analyses of the FN promoter revealed that repression of the FN promoter by c-Jun depends on the CRE located at -160 relative to the start site of transcription. Supershift assays of CRE-bound complexes from HPV16-E6-expressing and c-Jun-overexpressing cells suggested that the presence of ATF-2 in the complexes binding to CRE was required for the transactivation of the ...
Mouse anti Human fibronectin antibody, clone EP5 recognizes fibronectin in human and mouse tissues, specifically connective tissues and ve
Reactivity of the mAb C6 with different FN fragments.A. Model of the domain structure of human FN subunit; the three different types of repeats and the specific
The fibronectin content of RMC cultures grown for 8-14 days in medium containing 30 mM (540 mg/dl) D-glucose was increased 30-60% relative to that of control cells cultured in 10 mM (180 mg/dl) glucose. Addition of equiosmolar concentrations (20 mM, 360 mg/dl) of L-glucose, 3-O-methylglucose, or mannitol to 10 mM glucose media did not alter fibronectin accumulation compared with values observed in 10 mM glucose alone. The basal phosphorylation of the 80,000-Mr MARCKS protein, which is a substrate for PKC, and the phosphorylation induced by acute (15-min) exposure of cells to 15% FCS or to 0.1 μM (50 ng/ml) PDBu were all increased in cells grown in 30 mM compared with 10 mM glucose. By contrast, phosphorylation of the 80,000-Mr protein in response to a maximal concentration of PDBu (1 μM, 500 ng/ml) was not different in cells grown in 30 mM compared with 10 mM glucose. The acute increases in phosphorylation of the 80,000-Mr protein were blocked by the PKC inhibitor calphostin C. Chronic (7-day) ...
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For immunofluorescence, 13-mm-diameter glass coverslips were derivatized for 30 min with 1 mM sulpho-m-maleimidobenzoyl-N-hydrosuccinimide ester (Perbio Science). For biochemical assays, 15-cm tissue culture-treated plastic dishes were coated directly with ligand. Coverslips or dishes were coated for 2 h at room temperature with 10 μg/ml fibronectin polypeptides in Dulbeccos PBS containing calcium and magnesium (Biowhittaker UK) and blocked with 10 mg/ml of heat-denatured BSA for 30 min at room temperature. Equivalent ligand coating between glass and plastic was tested by ELISA using the antifibronectin mAb 333 (Bass et al., 2007). For experiments on defined ligands, cells were treated with 25 μg/ml cycloheximide (Sigma-Aldrich) for 2 h before detachment to prevent de novo matrix synthesis and were then detached with 0.5 mg/ml trypsin. Cells were resuspended in DME/25 mM Hepes and 25 μg/ml cycloheximide, plated at a density of 1.25 × 104 cells per coverslip or 4 × 106 cells per dish, and ...
BACKGROUND: Titin is a huge protein ( approximately 3 MDa) that is present in the contractile unit (sarcomere) of striated muscle and has a key role in muscle assembly and elasticity. Titin is mainly composed of two types of module (type I and II). Type I modules are found exclusively in the region of titin localised in the A band, where they are arranged in a super-repeat pattern that correlates with the ultrastructure of the thick filament. No structure of a titin type I module has been reported so far. RESULTS: We have determined the structure of a representative type I module, A71, using nuclear magnetic resonance (NMR) spectroscopy. The structure has the predicted fibronectin type III fold. Titin-specific conserved residues are either located at the putative module-module interfaces or along one side of the protein surface. Several proline residues that contribute to two stretches in a polyproline II helix conformation are solvent-exposed and line up as a continuous ribbon extending over ...
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FNDC5 (fibronectin domain-containing [protein] 5) was initially discovered and characterized by two groups in 2002. In 2011 FNDC5 burst into prominence as the parent of irisin, a small protein containing the fibronectin type III domain. Irisin was proposed to be secreted by skeletal muscle cells in response to exercise, and to circulate to fat tissue where it induced a transition to brown fat. Since brown fat results in dissipation of energy, this pathway is of considerable interest for metabolism and obesity. Here I review the original discoveries of FNDC5 and the more recent discovery of irisin. I note in particular three problems in the characterization of irisin: the antibodies used to detect irisin in plasma lack validity; the recombinant protein used to demonstrate activity in cell culture was severely truncated; and the degree of shedding of soluble irisin from the cell surface has not been quantitated. The original discovery proposing that FNDC5 may be a transmembrane receptor may ...
Fig. 2 Integrin/BMP-2 receptor cosignaling drives MSC osteogenesis.. (A) Coimmunoprecipitation of integrin β1 and BMPRI occurred on BMP-2 sequestered by FN on PEA, and bands correspond to BMPRIa (60 kD) after precipitation with anti-integrin β1 antibodies. The graphs show quantification of bands relative to the absence of BMP-2. This colocalization can also be seen in individual cells with integrin β1 (stained red) and BMPRIa (stained green). (B) Smad signaling was drastically altered when BMP-2 was presented bound on FNIII12-14; blocking this GF-binding domain of FN (using the monoclonal antibody P5F3 at a molar ratio of 1 with FN to block the GF-binding site) reduces Smad signaling. GAPDH, glyceraldehyde-3-phosphate dehydrogenase. (C) Phosphorylation of extracellular signal-related kinase (ERK) 1/2 was significantly enhanced on PEA when BMP-2 was presented at the material interface, sequestered on FN, compared to the presence of the same doses of the soluble factor. (D) In-cell Western ...
The processes responsible for epithelial spreading during wound healing and embryonic morphogenesis were investigated in an organ culture model in which an epithelial tissue (chick embryo pigmented retinal epithelium) spread over the surface of an aggregate of mesenchyme cells (chick embryo cardiac mesenchyme). The heart mesenchyme aggregate is differentiated into a core of stellate cells associated with a fibronectin-poor matrix surrounded by a cortical zone, 2-5 cells in thickness, of flattened cells embedded in a fibronectin-rich extracellular matrix. Envelopment of the mesenchyme aggregate is accompanied by a movement of the cells and the fibronectin-rich extracellular matrix of the cortex over the core tissue in advance of the spreading pigmented retina tissue. Three distinct processes were identified as contributing to epithelial spreading in this system: (1) active migration of the pigmented retinal epithelium; (2) active contraction of the cortical cells of the mesenchyme aggregate to ...
This unit describes the purification of the multifunctional adhesive glycoprotein fibronectin from plasma or of cell‐derived fibronectin from cell surfaces and from conditioned medium
Quantikine® ELISA kit for human Fibronectin (Cat#DFBN10). 0.579 ng/mL detection sensitivity. View Fibronectin ELISA kit details.
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Results Without consideration of qfFN concentration, the number needed to treat (NNT) to successfully administer steroids to one woman who delivered within 1 week of presentation was 77 (1540 to prevent one case of respiratory distress syndrome (RDS)), and 3 women would have delivered before receiving a full course. Utilising fFN thresholds of 10, 50, 200 and 500ng/ml to guide steroid administration reduced the NNT to 58, 28, 9 and 5 respectively; only one extra case would have been missed at a threshold of ≥500 ng/ml. At ≥200 ng/ml, the NNT to prevent one RDS case reduces to 180.. ...
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PubMed comprises more than 30 million citations for biomedical literature from MEDLINE, life science journals, and online books. Citations may include links to full-text content from PubMed Central and publisher web sites.