The structure and biologic activities of plasma fibronectin

Mosesson, MW; Amrani, David L.

doi:10.1182/blood.v56.2.145.145

Cited by 344 publications

(83 citation statements)

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“…Several binding activities have been located in different domains of the FN molecule. Indeed, FN has affinities for collagen, heparin and other glycosaminoglycans, fibrin, cell surfaces, bacteria and itself (for reviews, see Mosesson and Amrani, 1980;Hynes and Yamada, 1982;Yamada, 1983).…”

Section: Introductionmentioning

confidence: 99%

Human fibronectin: molecular cloning evidence for two mRNA species differing by an internal segment coding for a structural domain.

Kornblihtt¹,

Vibe-Pedersen²,

Baralle³

1984

The EMBO Journal

219

108

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Two different fibronectin (FN) mRNA species were detected in the human cell line Hs578T. One species, mRNA I, contains an additional 270 nucleotide long insert (ED) that encodes exactly one of the internally repeated structural domains of the protein. The 90 amino acid extra domain belongs to the so‐called type III homology and it is located in the carboxy‐terminal half of FN, in between the cell attachment and the heparin binding sites of the protein. The evidence of two mRNAs is provided by the isolation and characterisation of four independent cDNA clones from a library prepared with a synthetic oligonucleotide primer, and it was confirmed by S1 nuclease analysis of cDNA/mRNA hybrids. This kind of analysis also showed that in the human cell line, mRNA I is present at a lower level than mRNA II (the mRNA species without the ED), whilst in human liver, mRNA I is virtually undetectable. Since liver tissue has recently been reported to be the source of plasma FN, our results indicate that the presence of the ED insert could be a particular feature of cellular FN.

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Section: Introductionmentioning

confidence: 99%

Human fibronectin: molecular cloning evidence for two mRNA species differing by an internal segment coding for a structural domain.

Kornblihtt¹,

Vibe-Pedersen²,

Baralle³

1984

The EMBO Journal

219

108

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“…Fibronectin is another adhesive glycoprotein that may function as an attachment protein and possibly as a promoter of cell-cell adhesion (Hynes, 1981;Kleinman et al, 1981;Mosesson and Amrani, 1980;Mosher, 1980;Pearlstein et al, 1980;Ruoslahti et al, 1981;Saba and Jaffe, 1980;Vaheri and Mosher, 1978;Yamada, 1983;Yamada and Olden, 1978). Laminin is at least as effective as fibronectin as an agglutinin (compare Fig.…”

Section: Laminin Compared With Fibronectinmentioning

confidence: 99%

The adhesive glycoprotein laminin is an agglutinin

Kennedy

Rohrbach

Martin

et al. 1983

Journal Cellular Physiology

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The glycoprotein laminin appears to function in the attachment of various epithelial cells to basement membranes. We examined whether its putative cell-adhesive activity could be analyzed in a simple, one-component model system--the agglutination of erythrocytes. Laminin is a potent agglutinin of aldehyde-fixed sheep and human erythrocytes, with half-maximal agglutination at 0.8 micrograms/ml in a standard hemagglutination assay. Inhibitors of this hemagglutinating activity include gangliosides and certain charged phospholipids. The spectrum of molecules is similar but not identical to inhibitors of the hemagglutinating activity of the adhesive glycoprotein fibronectin. Laminin is much less biologically active in three other assays for fibronectin biological activity involving cell spreading on tissue culture substrates, attachment of fibroblastic cells to type I collagen, and restoration of normal morphology to transformed fibroblasts. The adhesive glycoproteins laminin and fibronectin therefore differ markedly in biological activities in several specific adhesion assays; however, they resemble one another in binding to heparin, collagen, and cell surfaces and in their agglutinin activity.

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“…wt. glycoproteins that are present in vertebrates in both the soluble and insoluble forms (Mosesson and Amrani, 1980;Ruoslahti etal., 1981;Yamada and Olden, 1978;Vaheri and Alitalo, 1981;Mosher, 1980;Vaheri and Mosher, 1978;Hynes, 1976;Grinnel, 1978). The soluble form has been observed in many different biological fluids including plasma, urine, cerebrospinal, and amniotic fluids.…”

Section: Introductionmentioning

confidence: 99%

Species-specific monoclonal antibodies in the assignment of the gene for human fibronectin to chromosome 2.

Zardi¹,

Cianfriglia²,

Balza

et al. 1982

The EMBO Journal

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Using three different species‐specific monoclonal antibodies we have studied, in human‐mouse and human‐hamster somatic cell hybrids, the correlation between the presence of different human chromosomes and the ability to release human fibronectin into the tissue culture medium. Presence of human fibronectin was determined by an affinity‐radioimmunoassay. In addition, tissue culture media of the different hybrids were separated on SDS‐polyacrylamide gels, the proteins were blotted onto a nitrocellulose sheet and human fibronectin visualized by an immunoenzymatic technique. Karyology and determination of isoenzyme markers of specific human chromosomes show that the ability to produce human fibronectin segregated with the presence of human chromosome 2.

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The structure and biologic activities of plasma fibronectin

Cited by 344 publications

References 0 publications

Human fibronectin: molecular cloning evidence for two mRNA species differing by an internal segment coding for a structural domain.

Human fibronectin: molecular cloning evidence for two mRNA species differing by an internal segment coding for a structural domain.

The adhesive glycoprotein laminin is an agglutinin

Species-specific monoclonal antibodies in the assignment of the gene for human fibronectin to chromosome 2.

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