Fibronectin: a chromatin-associated protein?

Zardi, Luciano; Siri, Annalisa; Bárbara, Cristina; Santi, Leonardo; Gardner, William D.; Hoch, Sallie O.

doi:10.1016/0092-8674(79)90120-x

Cited by 92 publications

(31 citation statements)

References 39 publications

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“…It could originate from local synthesis by mammary epithelial cells (29,301 or macrophages known to be present in milk. Milk tibronectin could also originate from filtration of the blood.…”

Section: Discussionmentioning

confidence: 99%

Human milk fibronectin: identification of fibronectin fragments by transfer of milk proteins from polyarcrylamide gels to nitrocellulose sheets

et al. 1982

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“…It could originate from local synthesis by mammary epithelial cells (29,301 or macrophages known to be present in milk. Milk tibronectin could also originate from filtration of the blood.…”

Section: Discussionmentioning

confidence: 99%

Human milk fibronectin: identification of fibronectin fragments by transfer of milk proteins from polyarcrylamide gels to nitrocellulose sheets

et al. 1982

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“…The proteins known to be present in the nucleus include the homologue of targeting protein for Xenopus kinesin-like protein 2 (Xklp2) (TPX2, AF244547) (44 -46, 56 -58) and the p32cdc2-like PITSLRE protein kinase ␣ SV9 isoform (AF080683) (47,60). The other non-ribosomal proteins we identified are fibronectin (48,49), tubulin ␣1, putative (AK01960, ␤-tubulin isotype M-␤ 5), growth arrest specific 11 (50,51), putative (AK007869, eukaryotic translation elongation factor 1) (52,53,59), putative (AK010776), and GAJ (Supplementary Table III). All of these non-ribosomal proteins except GAJ and putative (AK010776) can be categorized coincidentally into protein factors participating or expected to be participating in microtubule assembly or nucleologenesis occurring during the M-phase of the cell cycle (Table II and Supplementary Table III).…”

Section: Resultsmentioning

confidence: 99%

Isolation and Proteomic Characterization of Human Parvulin-associating Preribosomal Ribonucleoprotein Complexes

Fujiyama

Yanagida²,

Hayano³

et al. 2002

Journal of Biological Chemistry

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Human parvulin (hParvulin; Par14/EPVH) belongs to the third family of peptidylprolyl cis-trans isomerases that exhibit an enzymatic activity of interconverting the cis-trans conformation of the prolyl peptide bond, and shows sequence similarity to the regulator enzyme for cell cycle transitions, human Pin1. However, the cellular function of hParvulin is entirely unknown. Here, we demonstrate that hParvulin associates with the preribosomal ribonucleoprotein (pre-rRNP) complexes, which contain preribosomal RNAs, at least 26 ribosomal proteins, and 26 trans-acting factors involved in rRNA processing and assembly at an early stage of ribosome biogenesis. Since an amino-terminal domain of hParvulin, which is proposed to be a putative DNA-binding domain, was alone sufficient to associate in principle with the pre-rRNP complexes, the association is probably through protein-RNA interaction. In addition, hParvulin co-precipitated at least 10 proteins not previously known to be involved in ribosome biogenesis. Coincidentally, most of these proteins are implicated in regulation of microtubule assembly or nucleolar reformation during the mitotic phase of the cell. Thus, these results, coupled with the preferential nuclear localization of hParvulin, suggest that hParvulin may be involved in ribosome biogenesis and/or nucleolar re-assembly of mammalian cells.

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“…Only clones showing a negative reaction for plFN and a positive reaction for cFN were selected for further characterization. The solid-phase double-antibody radioimmunoassay method was also used for the quantitative competition binding assay (3,36). It was carried out using the mAbs IST-9 and FN-3 (both specific for the ED sequence), and IST-4 (specific for a sequence common to all FN variants).…”

Section: Radioimmunoassaymentioning

confidence: 99%

Monoclonal antibodies in the analysis of fibronectin isoforms generated by alternative splicing of mRNA precursors in normal and transformed human cells.

Borsi¹,

Bárbara²,

Castellani³

et al. 1987

The Journal of Cell Biology

194

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Abstract. Recent results showing that a singlefibronectin gene can give rise to several different mRNAs by alternative splicing have offered an explanation for fibronectin polymorphism. Here we report on monoclonal antibodies that show specificity for a fibronectin segment (ED) that can be included or omitted from the molecule depending on the pattern of splicing of the mRNA precursors. Using these monoclonals, we have quantitatively analyzed the expression of the ED sequence in human fibronectin from different sources. The results demonstrated that, at the protein level, the ED segment is not expressed in plasma fibronectin and that, in fibronectin from the tissue culture medium of tumor-derived or simian virus-40-transformed human cells, the percentage of fibronectin molecules containing the ED segment is about 10 times higher than in fibronectin from normal human fibroblasts. These results suggest that in malignant cells the mechanisms that regulate the splicing of mRNA precursors are altered. F IBRONECT1NS (FNs) ~ are high-molecular-mass, adhesive glycoproteins present in the soluble form in plasma and other body fluids and in insoluble form in the extracellular matrices and basement membranes. FN molecules act as bridges between the cell surface and extracellular material. In fact, the FN molecules contain a cellbinding site and binding sites for collagen, heparin, gangliosides, and fibrin. Because of their multiple interactions, FNs play an important role in diverse biological phenomena, including cell adhesion, cell migration, hemostasis and thrombosis, wound healing and the ability to induce a more normal phenotype in transformed cells (for reviews on distribution, structure, and biological functions, see references 1,7,8,18,24).It has been demonstrated that FN polymorphism may be at least partially due to alternative splicing schemes in two regions (ED and IIICS) because as many as 10 different mRNAs may originate from the primary transcript of a single gene (9, 12-15, 25, 26, 29) localized on chromosome 2 (11, 34). In fact, Schwarzbauer et al. (25) have shown that an antiserum specific for the rat fibronectin IIICS sequence recognizes the larger subunit of rat plasma FN (plFN), but not the smaller one.Here we report the characterization of mAbs for the ED 1. Abbreviations used in this paper: cFN and plFN, fibronectin from cultured cell media and plasma, respectively. fragment of fibronectin. Using these mAbs in a quantitative assay, we have demonstrated that this sequence is not present in plFN and that tumor-derived and SV-40-transformed human cells release a population of FN molecules in which the percentage of subunits containing the ED sequence is about 10 times higher than in the FN released by normal human fibroblasts.

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Fibronectin: a chromatin-associated protein?

Cited by 92 publications

References 39 publications

Human milk fibronectin: identification of fibronectin fragments by transfer of milk proteins from polyarcrylamide gels to nitrocellulose sheets

Human milk fibronectin: identification of fibronectin fragments by transfer of milk proteins from polyarcrylamide gels to nitrocellulose sheets

Isolation and Proteomic Characterization of Human Parvulin-associating Preribosomal Ribonucleoprotein Complexes

Monoclonal antibodies in the analysis of fibronectin isoforms generated by alternative splicing of mRNA precursors in normal and transformed human cells.

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