Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:Q07644 (polypeptide)
 72,197 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Fibronectin is a glycoprotein found in plasma (cold-insoluble globulin), connective tissues, and cultures of fibroblasts and astroglial cells. This paper describes the identification of fibronectin in human CSF. Fibronectin in CSF was immunologically indistinguishable from the plasma form, as shown by double-diffusion analysis and by radioimmunoassay specific for fibronectin. Fibronectin was isolated from human CSF by affinity chromatography on Sepharose-coupled gelatin and was further analyzed by SDS-polyacrylamide gel electrophoresis. It showed a polypeptide band similar to that of plasma fibronectin. The fibronectin concentration in CSF of 17 neurological outpatients without demonstrable organic lesion in the CNS was 3.0 +/- 1.6 microgram/ml (mean +/- S.D.) which is about 0.6% of total CSF protein. In CSF of 11 MS patients, the concentration was significantly (p less than 0.005) lower (1.6 +/- 0.2 microgram/ml). Of patients with brain tumors, seven had very low levels, three were normal, and two had very high levels. The cause for the low levels in MS and tumor patients is not known.
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PMID:Demonstration of fibronectin in human cerebrospinal fluid. 10 31

We have isolated a large noncollagenous glycoprotein, laminin, from a mouse tumor that produces basement membrane. The protein consists of at least two polypeptide chains (Mr = 220,000 and Mr = 440,000) joined to each other by disulfide bonds. Laminin and type IV collagen are major constituents of the tumor. Laminin is distinctly different from fibronectin, another component of basement membranes, in amino acid composition and immunological reactivity. Pepsin digestion of laminin releases a large, cystine-rich fragment which retains most of the antigenicity of the original protein. Immunological studies using purified antibody against laminin show that it is produced by a variety of cultured cells. In addition, these antibodies react with the basement membranes of normal tissues, suggesting that this protein or an immunologically related protein is a constituent of the basement membranes of these tissues.
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PMID:Laminin--a glycoprotein from basement membranes. 11 18

The proteins in cell layers of cultured normal diploid human skin (ES, ER) and lung (WI-38) fibroblasts were compared to those of SV40-transformed human fibroblasts (WI-38/VA-13), human rhabdomyosarcoma (RD) and fibrosarcoma (HT-1080) cells using metabolic amino acid and sugar labeling and surface labeling with tritiated sodium borohydride after oxidation with galactose oxidase. The labeled proteins were analysed by sodium dodecyl sulfate polyacrylamide gel electrophoresis and autoradiography (fluorography). A transformation-associated decrease in the pericellular glycoprotein fibronectin (subunit molecular weight, 220 000) and in the synthesis of a set of polypeptides in the 130 000--180 000 dalton region was seen. Synthesis of a glycosylated 160 000 dalton polypeptide was markedly reduced. In transformed cells distinct increases of several specific polypeptides was detected in both [35S]methionine and [3H] mannose incorporation experiments but not using the surface labeling method.
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PMID:Comparison of polypeptides from cultured human fibroblasts and sarcoma cells. 21 25

We have identified and purified a polypeptide region containing the collagen-binding site of the adhesive glycoprotein fibronectin. Chicken cellular fibronectin isolated from cultured embryonic fibroblasts was permitted to bind to gelatin coupled to agarose beads and was then digested extensively with chymotrypsin. A prominent 40,000-dalton fragment of fibronectin consisting of a single polypeptide chain was detected by sodium dodecyl sulfate/polyacrylamide gel electrophoresis of material remaining bound to the gelatin-agarose. This fragment appeared within 10 min after the digestion was initiated and persisted for more than 20 hr. This proteolytic fragment was isolated in electrophoretically pure form and retained its affinity for collagen. Plasma fibronectins from chicken and human blood also contained collagen-binding proteolytic fragments of similar size. This finding suggest that the collagen-binding sites of cellular and plasma fibronectins are homologous.
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PMID:Identification and isolation of a collagen-binding fragment of the adhesive glycoprotein fibronectin. 28 1

Fibronectin is synthesized as a monomeric polypeptide chain. As early as it can be detected inside the cell, it carries carbohydrate side chains. These chains are sensitive to endoglycosidase H, suggesting that they are asparagine linked and high mannose form. The monomeric chains quickly dimerize while still inside the cell. Newly synthesized fibronectin appears as a dimer, both at the cell surface and secreted into the culture medium, about 30 min after commencement of labeling. This exported fibronectin has endoglycosidase H-resistant carbohydrate side chains, indicating processing from the high mannose form to a complex form. Exit of fibronectin to the outside of the cell follows quickly on carbohydrate processing; no large pool of endoglycosidase H-resistant fibronectin exists inside the cell. The dimeric fibronectin at the cell surface is initially deoxycholate soluble but slowly becomes deoxycholate-insoluble and also slowly forms high molecular weight aggregates which require reduction of disulfide bonds for their dissociation.
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PMID:Biosynthesis and processing of fibronectin in NIL.8 hamster cells. 50 Jun 94

Fibronectin mRNA has been partially purified by guanidine extraction, oligo-(dT)-cellulose chromatography and sucrose density gradient centrifugation. We obtain a fraction which programs a wheat germ in vitro translation system to synthesize a polypeptide species which co-electrophoreses with fibronectin in SDS-polyacrylamide gels and which is immunoprecipitated with affinity purified fibronectin-specific IgG. Analysis of this RNA fraction by methyl mercury hydroxide-agarose gel electrophoresis reveals the presence of a band accounting for 30 percent to 50 percent of the ethidium bromide-staining material in the fraction. The RNA of this band has an estimated molecular weight of about 3 million daltons and is greatly reduced in the corresponding RNA fraction from RSV transformed CEF. This RNA has been tentatively identified as fibronectin mRNA.
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PMID:Partial purification and characterization of the messenger RNA for cell fibronectin. 57 88

The molecular properties of cold-insoluble globulin have been investigated by velocity centrifugation, circular dichroism, and fluorescence at neutral and alkaline pH. The stability of the protein to thermal and guanidine hydrochloride has been evaluated under both conditions. The close parallelism between the properties of cold-insoluble globulin and those of the cell surface protein (fibronectin) serve to establish the essential identity of the structures of the two proteins derived from different sources. It is suggested that the cold-insoluble globulin is composed of several domains connected by flexible polypeptide segments. The large increase in the frictional ratio observed between pH 7.0 and 11.0 can be explained by an expansion of the flexible segments without significant change in the domains. These domains are stable to about 55 degrees C at pH 7.0 but only to about 40 degrees C at pH 11.0.
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PMID:The structure and stability of human plasma cold-insoluble globulin. 76 48

Incubation of cultured human fibroblasts with blood coagulation factor XIIIa (plasma transglutaminase, fibrinoligase) and the fluorescent primary amine, N-(5-aminopentyl)-5-dimethylaminonaphthalene-1-sulfonamide, resulted in fluorescent labeling of three cellular polypeptides. The molecular weights of the labeled polypeptides, estimated by polyacrylamide gel electrophoresis in sodium dodecyl sulfate after reduction, were: greater than 1.2-10(6), 2.2-10(5), and 1.3-10(5). The labeled 2.2-10(5) dalton polypeptide was susceptible to mild trypsinization and not present in cultures of SV-40 transformed fibroblasts, indicating that it is the subunit of cell-surface fibronectin and identical with the external transformation-sensitive polypeptide of similar molecular weight described by others. Upon coelectrophoresis, the labeled 2.2-10(5) dalton polypeptide migrated slightly behind the subunit of plasma fibronectin (cold-insoluble globulin), indicating that the immunologically cross-reactive forms of fibronectin in human plasma and cultured human fibroblasts differ slightly in molecular weight. The identities of the labeled greater than 1.2-10(6) and 1.3-10(5) dalton polypeptides are not known. The XIIa-reactive glutamine residues of fibroblast cell-surface proteins are potential sites for intermolecular cross-linking (by xi-(gamma-glutamyl)lysyl linkages) to other proteins of connective tissue.
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PMID:Labeling of a major fibroblast surface protein (fibronectin) catalyzed by blood coagulation factor XIIa. 84 57

The leukocyte integrin alpha 4 beta 1 (VLA-4, CD49d/CD29) is a receptor for the extracellular matrix protein fibronectin and the endothelial adhesion protein VCAM-1. We have analyzed the biosynthesis and post-translational modifications of the two subunits of this receptor complex. The alpha 4 subunit was initially synthesized as a single-chain polypeptide that underwent the formation of complex endoglycosidase H-resistant oligosaccharide side chains and which could be proteolytically cleaved into two noncovalently associated fragments. The level and rate of alpha 4 subunit cleavage was dependent on the cell studied. The T cell tumor line HPB-ALL expressed both intact and fragmented alpha 4 on the cell surface. The interleukin-2-dependent natural killer line NK 3.3 and long term interleukin-2-dependent activated T lymphocytes cleaved the alpha 4 polypeptide earlier and more efficiently than did HPB-ALL cells and did not have detectable levels of intact alpha 4 on the cell surface. The proteolysis of alpha 4 was blocked by treating cells with either the lysosomotrophic amine NH4Cl or the carboxylic ionophore monensin. The presence of complex N-linked oligosaccharides did not seem to be necessary for alpha 4 cleavage or for binding of the alpha 4 beta 1 complex to a synthetic peptide corresponding to the binding site for this receptor on fibronectin.
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PMID:Post-translational processing of the leukocyte integrin alpha 4 beta 1. 128 Nov 55

Axonin-1 is an axon-associated cell adhesion molecule (AxCAM) of the chicken, which promotes neurite outgrowth by interaction with the AxCAM L1(G4) of the neuritic membrane. Here we report the cloning and sequence determination of a cDNA encoding axonin-1. Peptides generated by enzymatic cleavage showed similarity to the AxCAM F11. Degenerated polymerase chain reaction (PCR) primers were designed and an axonin-1 fragment was amplified from mRNA of embryonic retina. Screening of a cDNA library from embryonic brain resulted in the isolation of a 4.0-kb cDNA insert with an open reading frame of 3108 nucleotides. The deduced polypeptide of 1036 amino acids includes a putative hydrophobic N-terminal signal sequence of 23 or 25 amino acids and a C-terminal hydrophobic sequence of 29 amino acids which is suggestive of sequences serving as signal for the attachment of a glycosyl-phosphatidylinositol (glycosyl-PtdIns) anchor. The putative mature form of axonin-1 comprises six immunoglobulin-like repeats, followed by four fibronectin-type III repeats. Axonin-1 exhibits 75% amino acid identity with the AxCAM TAG-1 of the rat, suggesting that it is the chicken homologue of TAG-1. Like TAG-1, axonin-1 is glycosyl-PtdIns-anchored to the neuronal membrane; in contrast to TAG-1, it does not exhibit an Arg-Gly-Asp sequence.
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PMID:The axonally secreted cell adhesion molecule, axonin-1. Primary structure, immunoglobulin-like and fibronectin-type-III-like domains and glycosyl-phosphatidylinositol anchorage. 131 75


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