Adherence of synovial cells on EDA‐containing fibronectin

Hino, Kazuo; Maeda, Tatsuya; Sekiguchi, Kiyotoshi; Shiozawa, Kazuko; Hirano, Hiroto; Sakashita, Eiji; Shiozawa, Shunichi

doi:10.1002/art.1780391011

Cited by 20 publications

(10 citation statements)

References 32 publications

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“…33) Our present result, showing that ACC-FN is more potent than pFN for adhesion of ACC3 cells, is consistent with these data. On the other hand, the immunohistochemical findings suggested that ED-B(+) FNs are associated with angiogenesis.…”

Section: Discussionsupporting

confidence: 93%

High‐molecular‐weight Fibronectin Synthesized by Adenoid Cystic Carcinoma Cells of Salivary Gland Origin

Toyoshima

Kimura

Cheng

et al. 1999

Japanese Journal of Cancer Research

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Section: Discussionsupporting

confidence: 93%

High‐molecular‐weight Fibronectin Synthesized by Adenoid Cystic Carcinoma Cells of Salivary Gland Origin

Toyoshima

Kimura

Cheng

et al. 1999

Japanese Journal of Cancer Research

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“…In a previous study, 1 mg/ml heparin inhibited by 35% the adherence of cultured synovial cells onto plasma-fibronectin-coated substratum [Hino et al, 1996]. Co-coating of plastic surface with 10 mg/ml plasma-fibronectin and 0.1-5 mg/ml heparin resulted in significant inhibition in the adherence of rat smooth muscle cells, the occurrence of which was maximal at 1 mg/ml heparin [Lundmark et al, 2001].…”

Section: Discussionmentioning

confidence: 96%

Heparin modulates the growth and adherence and augments the growth‐inhibitory action of TNF‐α on cultured human keratinocytes

Harvima

Lappalainen

Hirvonen³

et al. 2004

J of Cellular Biochemistry

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Previous works suggest the involvement of mast cells in the epithelialization of chronic wounds. Since heparin is a major mediator stored in the secretory granules of mast cells, the purpose of this work was to elucidate the function of heparin in epithelialization using in vitro culture models. For this, low- and high-calcium media in monolayer and epithelium cultures of keratinocytes were used. Also, an assay based on keratinocyte adherence onto plastic surface was used as well. Heparin (0.02-200 microg/ml) inhibited keratinocyte growth in a non-cytotoxic and dose-dependent manner in low- and high-calcium media, Keratinocyte-SFM and DMEM, in the absence of growth factors and serum. Also, heparin inhibited the growth of keratinocyte epithelium in the presence of 10% fetal calf serum and DMEM. Instead, in the presence of Keratinocyte-SFM and growth factors, heparin at 2 microg/ml inhibited the growth by 18% but at higher heparin concentrations the inhibition was reversed to baseline. TNF-alpha is another preformed mediator in mast cell granules and it inhibited keratinocyte growth in monolayer and epithelium cultures. Interestingly, heparin at 2-20 microg/ml augmented or even potentiated this growth-inhibitory effect of TNF-alpha. The association of TNF-alpha with heparin was shown by demonstrating that TNF-alpha bound tightly to heparin-Sepharose chromatographic material. However, heparin could not augment TNF-alpha-induced cell cycle arrest at G0/G1 phase or intercellular adhesion molecule-1 expression in keratinocytes. In the cell adherence assay, heparin at 2 microg/ml inhibited significantly by 12-13% or 33% the adherence of keratinocytes onto the plastic surface coated with fibronectin or collagen, respectively, but this inhibition was reversed back to baseline at 20 or 200 microg/ml heparin. Also, heparin affected the cell membrane rather than the protein coat on the plastic surface. In conclusion, heparin not only inhibits or modulates keratinocyte growth and adherence but it also binds and potentiates the growth-inhibitory function of TNF-alpha.

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“…Inclusion of the alternatively spliced A domain is known to augment fibronectin's adhesion to integrin and its cell binding and spreading activity (20,35). The increased activity was not due to the binding of A to cells.…”

Section: Discussionmentioning

confidence: 99%

The Compact Conformation of Fibronectin Is Determined by Intramolecular Ionic Interactions

Johnson¹,

Sage²,

Briscoe³

et al. 1999

Journal of Biological Chemistry

170

215

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Fibronectin exists in a compact or extended conformation, depending upon environmental pH and salt concentration. Using recombinant fragments expressed in bacteria and baculovirus, we determined the domains responsible for producing fibronectin's compact conformation. Our velocity and equilibrium sedimentation data show that FN2-14 (a protein containing FN-III domains 2 through 14) forms dimers in low salt. Experiments with smaller fragments indicates that the compact conformation is produced by binding of FN12-14 of one subunit to FN2-3 of the other subunit in the dimer. The binding is weakened at higher salt concentrations, implying an electrostatic interaction. Furthermore, segment FN7-14؉A, which contains the alternatively spliced A domain between FN11 and 12, forms dimers, whereas FN7-14 without A does not. Segment FN12-14؉A also forms dimers, but the isolated A domain does not. These data imply an association of domain A with FN12-14, and the presence of A may favor an open conformation by competing with FN2-3 for binding to FN12-14.

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Adherence of synovial cells on EDA‐containing fibronectin

Cited by 20 publications

References 32 publications

High‐molecular‐weight Fibronectin Synthesized by Adenoid Cystic Carcinoma Cells of Salivary Gland Origin

High‐molecular‐weight Fibronectin Synthesized by Adenoid Cystic Carcinoma Cells of Salivary Gland Origin

Heparin modulates the growth and adherence and augments the growth‐inhibitory action of TNF‐α on cultured human keratinocytes

The Compact Conformation of Fibronectin Is Determined by Intramolecular Ionic Interactions

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