Elastin as a matrikine

Duca, Laurent; Floquet, Nicolas; Alix, Alain J. P.; Haye, Bernard; Debelle, Laurent

doi:10.1016/j.critrevonc.2003.09.007

Cited by 188 publications

(125 citation statements)

References 81 publications

Supporting

Mentioning

122

Contrasting

Unclassified

Order By: Relevance

“…In contrast to other data, regions encoded by the N-terminal exons (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18), the central exons (18 -27), and the C-terminal exons (18 -36) all supported human umbilical vein endothelial cell attachment.…”

mentioning

confidence: 66%

See 1 more Smart Citation

Cell Adhesion to Tropoelastin Is Mediated via the C-terminal GRKRK Motif and Integrin αVβ3

Bax

Rodgers

Bilek

et al. 2009

Journal of Biological Chemistry

155

181

View full text Add to dashboard Cite

Elastin fibers are predominantly composed of the secreted monomer tropoelastin. This protein assembly confers elasticity to all vertebrate elastic tissues including arteries, lung, skin, vocal folds, and elastic cartilage. In this study we examined the mechanism of cell interactions with recombinant human tropoelastin. Cell adhesion to human tropoelastin was divalent cation-dependent, and the inhibitory anti-integrin ␣ V ␤ 3 antibody LM609 inhibited cell spreading on tropoelastin, identifying integrin ␣ V ␤ 3 as the major fibroblast cell surface receptor for human tropoelastin. Cell adhesion was unaffected by lactose and heparin sulfate, indicating that the elastin-binding protein and cell surface glycosaminoglycans are not involved. The C-terminal GRKRK motif of tropoelastin can bind to cells in a divalent cation-dependent manner, identifying this as an integrin binding motif required for cell adhesion.

show abstract

mentioning

confidence: 66%

“…Members of the serine, aspartate, cysteine, and matrix metalloproteinase families of proteases can degrade elastin (8). The resulting elastin peptides have effects on ECM synthesis and cell attachment, migration, and proliferation (9).…”

mentioning

confidence: 99%

Cell Adhesion to Tropoelastin Is Mediated via the C-terminal GRKRK Motif and Integrin αVβ3

Bax

Rodgers

Bilek

et al. 2009

Journal of Biological Chemistry

155

181

View full text Add to dashboard Cite

show abstract

“…Injuries to the basement membrane can result in the release of these pro-invasive compounds. Furthermore, fragmentation of matrix proteins by free radicals or limited proteolysis can generate biologically active peptides, that is, the matrikines (Vartio 1989;Monboisse and Borel 1992;Raats et al, 1997;Duca et al, 2004). Once released, these matrikines, such as elastin peptides, can increase the expression of MMP-2, MT1-MMP and TIMP-2 in fibrosarcoma HT-1080 cells (Brassart et al, 1998).…”

mentioning

confidence: 99%

In vitro irradiation of basement membrane enhances the invasiveness of breast cancer cells

et al. 2007

View full text Add to dashboard Cite

Following removal of the primary breast tumour by conservative surgery, patients may still have additional malignant foci scattered throughout the breast. Radiation treatments are not designed to eliminate all these residual cancer cells. Rather, the radiation dose is calculated to optimise long-term results with minimal complications. In a tumour, cancer cells are surrounded by a basement membrane, which plays an important role in the regulation of gene expression. Using an invasion chamber, we have shown that irradiation before cell plating of a reconstituted basement membrane (Matrigel; Becton Dickinson, Bedford, MA, USA) increased the invasiveness of the breast cancer cells MDA-MB-231. This radiation enhancement of invasion was associated with the upregulation of the pro-invasive gene matrix metalloproteinase (MMP)-2. The expression of membrane type 1 matrix metalloproteinase (MT1-MMP) and tissue inhibitor of metalloproteinase-2 (TIMP), which are required to activate the MMP-2, were also increased. Confirming the role of MMP-2 and MT1-MMP, radiation enhancement of cancer cell invasion was prevented by an MMP-2 inhibitor and an anti-MT1-MMP antibody. This study also demonstrated that radiation can potentially enhance the invasion ability by inducing the release of pro-invasive factors stored in the Matrigel. Conversely, no enhancement of invasiveness was observed with the low metastatic cell line MCF-7. This lack of invasiveness correlated with the absence of the MMP-2 activator MT1-MMP in the MCF-7 cells. Radiotherapy is an efficient modality to treat breast cancer which could be further improved by inhibiting the pro-invasive gene upregulated by radiation.

show abstract

“…Elastin peptides are the result of elastin wear and tear due to mechanical fatigue or degradation by elastases during specific pathophysiological processes (12)(13)(14). Elastin peptide concentration in the blood flow is usually low, but it can reach high values in aged subjects, notably in those developing pathologies where elastin is massively degraded such as aneurysms (15,16).…”

mentioning

confidence: 99%

Interaction between the Elastin Peptide VGVAPG and Human Elastin Binding Protein

Blanchevoye

Floquet

Scandolera

et al. 2013

Journal of Biological Chemistry

Self Cite

View full text Add to dashboard Cite

Background:The interaction of the peptide VGVAPG with the elastin binding protein is critically involved in aneurysm progression.Results: A molecular model of this interaction is proposed and explored using a site-directed mutagenesis strategy. Conclusion: Three residues, Leu-103, Arg-107, and Glu-137, of elastin binding protein are critical players in this interaction. Significance: Our data now allow the design of antagonists of VGVAPG.

show abstract

Elastin as a matrikine

Cited by 188 publications

References 81 publications

Cell Adhesion to Tropoelastin Is Mediated via the C-terminal GRKRK Motif and Integrin αVβ3

Cell Adhesion to Tropoelastin Is Mediated via the C-terminal GRKRK Motif and Integrin αVβ3

In vitro irradiation of basement membrane enhances the invasiveness of breast cancer cells

Interaction between the Elastin Peptide VGVAPG and Human Elastin Binding Protein

Contact Info

Product

Resources

About