Elastin peptides prepared from piscine and mammalian elastic tissues inhibit collagen‐induced platelet aggregation and stimulate migration and proliferation of human skin fibroblasts

Sugawara, Eri; Ura, Megumi; Nakaba, Misako; Maeda, Isamu; Okamoto, Kouji

doi:10.1002/psc.1277

Cited by 23 publications

(20 citation statements)

References 30 publications

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“…(VPGVGVPGVGVPGKGVPGVGVPGVG) 10 Positive have biological activities conducive to fibroblast proliferation which is crucial for healing of different tissues. Elastin derived peptides that are prepared by proteolytic degradation of j-elastin or elastin based tissues have been shown to increase proliferation of arterial smooth muscle cells 24 and fibroblasts, 42 respectively. Since, these studies were done using a complex mixture of degradation products of elastin, the exact sequence or molecular weight of the species that induced proliferation could not be identified.…”

Section: Discussionmentioning

confidence: 99%

Proliferative activity of elastin‐like‐peptides depends on charge and phase transition

Yuan

Koria

2015

J Biomedical Materials Res

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Elastin-like-peptides (ELPs) are stimulus-responsive protein-based polymers and are attractive biomaterials due to their biocompatibility and unique properties. This study shows that in addition to their physical properties, ELPs have biological activities that are conducive to tissue regeneration. Specifically, we found that ELPs induce fibroblast proliferation via cell surface heparan sulfate proteoglycans (HSPG). Furthermore, our data suggests that ELP based materials with differential proliferative potential can be designed by controlling the interaction of ELPs with HSPGs by incorporating either hydrophobic or positively charged residues within the ELP sequence. Fibroblast proliferation is important for granulation tissue formation which is important in chronic wounds as well as in healing of other tissues. The customizable biological activity of ELPs coupled with their unique physical properties will enable us to design novel, sustainable and cost effective therapies for different tissue regeneration applications. © 2015 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 104A: 697-706, 2016.

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Section: Discussionmentioning

confidence: 99%

Proliferative activity of elastin‐like‐peptides depends on charge and phase transition

Yuan

Koria

2015

J Biomedical Materials Res

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“…Fragments of elastin, for example, are central in the progression of a mouse model of emphysema through chemotaxis of monocytes, a process which is blocked by administration of an anti-elastin antibody (Houghton et al, 2006). The elastin receptor (ELR) is a mediator of these molecular effects of elastin (Robert, 2005), which include chemotaxis of multiple inflammatory cells (Senior et al, 1980; Tajima et al, 1997) and changes in the activities of mesenchymal-derived cells including adhesion to elastic fibers (Hornebeck et al, 1986), increase of cellular proliferation (Tajima et al, 1997; Mochizuki et al, 2002), migration (Senior et al, 1982; Skeie and Mullins, 2008; Shiratsuchi et al, 2010) and increase in expression and secretion of various pro-matrix metalloproteinases (MMPs), especially -1, -2 and -3 (Cozlin et al, 2006; Brassart et al, 2001; Heinz et al, 2010), and a decrease in tissue inhibitor of metalloproteinases (TIMP)-1 and -2 (Cozlin et al, 2006). …”

Section: Introductionmentioning

confidence: 99%

Tropoelastin modulates TGF-β1-induced expression of VEGF and CTGF in airway smooth muscle cells

et al. 2013

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Elastin is predominantly comprised of crosslinked tropoelastin. For many years elastin was considered to serve a solely structural role but is now being increasingly identified as causal in cell signaling, development and repair. We introduced tropoelastin into an in vitro model in which airway smooth muscle cells (ASMCs) were stimulated with transforming growth factor (TGF)-β1 to examine the modulatory effect of this modular elastin sequence on release of angiogenic factors and matrix metalloproteinases (MMPs). Human ASMCs were presented to surfaces coated with tropoelastin or collagen and controls, then stimulated with TGF-β1. Transcript levels of vascular endothelial growth factor (VEGF) and connective tissue growth factor (CTGF) were quantified 4 and 24 h after TGF-β1 stimulation. Protein VEGF release from cells and CTGF sequestered at cell surfaces were measured by ELISA at 24 and 48 h. TGF-β1 increased VEGF mRNA 2.4 fold at 4 h and 5 fold at 24 h, accompanied by elevated cognate protein release 3 fold at 24 h and 2.5 fold at 48 h. TGF-β1 stimulation increased CTGF mRNA 6.9 fold at 4 h and 11.8 fold at 24 h, accompanied by increased sequestering of its protein counterpart 1.2 fold at 24 h and 1.4 fold at 48 h. Pre-incubation of cells with tropoelastin did not modulate VEGF or CTGF mRNA expression, but combined with TGF-β1 stimulation it led to enhanced VEGF release 5.1-fold at 24 h and 4.4-fold at 48 h.Pre-incubation with tropoelastin decreased CTGF sequestering 0.6-fold at 24 and 48 h, and increased MMP-2 production. Collagen pre-incubation under the same conditions displayed no effect on TGF-β1 stimulation apart from a slightly decreased (0.9 fold) sequestered CTGF at 48 h. As CTGF is known to anchor VEGF to the matrix and inhibit its angiogenic activity, a process which can be reversed by digestion with MMP-2, these findings reveal that elastin sequences can disrupt the balance of angiogenic factors, with implications for aberrant angiogenesis. The results suggest a model of molecular crosstalk and support an active role for elastin in vascular remodeling.

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“…They potentiate the migration and matrix invasion of tumor cells [8][9][10]36,37]. They stimulate the migration and proliferation of monocytes and skin fibroblasts [40,41]. They up-regulate MMP expression by fibroblasts inducing a remodeling program in favor of melanoma cell invasion [7].…”

Section: Resultsmentioning

confidence: 99%

Elastin molecular aging promotes MDA‐MB‐231 breast cancer cell invasiveness

et al. 2018

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Elastin is a long‐lived extracellular matrix protein responsible for the structural integrity and function of tissues. Breast cancer elastosis is a complex phenomenon resulting in both the deposition of elastotic masses and the local production of elastin fragments. In invasive human breast cancers, an increase in elastosis is correlated with severity of the disease and age of the patient. Elastin‐derived peptides ( EDP s) are a hallmark of aging and are matrikines – matrix fragments having the ability to regulate cell physiology. They are known to promote processes linked to tumor progression, but their effects on breast cancer cells remain unexplored. Our data show that EDP s enhance the invasiveness of MDA ‐ MB ‐231 breast cancer cells through the engagement of matrix metalloproteases 14 and 2. We therefore suggest that elastosis and/or an aged stroma could promote breast cancer cell invasiveness.

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Elastin peptides prepared from piscine and mammalian elastic tissues inhibit collagen‐induced platelet aggregation and stimulate migration and proliferation of human skin fibroblasts

Cited by 23 publications

References 30 publications

Proliferative activity of elastin‐like‐peptides depends on charge and phase transition

Proliferative activity of elastin‐like‐peptides depends on charge and phase transition

Tropoelastin modulates TGF-β1-induced expression of VEGF and CTGF in airway smooth muscle cells

Elastin molecular aging promotes MDA‐MB‐231 breast cancer cell invasiveness

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