A new pro-migratory activity on human myogenic precursor cells for a synthetic peptide within the E domain of the mechano growth factor

Mills, Philippe; Lafrenière, Jean-François; Benabdallah, Basma; Fahime, Elmostafa El; Tremblay, Jacques P.

doi:10.1016/j.yexcr.2006.10.032

Cited by 68 publications

(72 citation statements)

References 48 publications

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“…However, all the synthetic fragments that contained the last 4 amino acids (aa) of the hEC's C-terminal end stimulated the growth of human PC-3 cells. In addition, the synthetic fragments, hEc (13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23)(24) and hEc (21)(22)(23)(24), activated ERK1/2 (D, E), while the synthetic hEc (1-12) did not affect the phosphorylation of ERK1/2 in human PC-3 cells (C).…”

Section: Discussionmentioning

confidence: 99%

“…In the first series of experiments, the cells were seeded for 24hrs after plating and the media continued to be supplemented with 10% FBS during the experimental procedure. We then added various doses of the scrambled peptide (negative control), mature IGF-1 peptide (positive control), hEc, mE and the synthetic hEc fragments, hEc (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12), hEc (13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23)(24), hEc, [21][22][23][24] for 48 hrs. In the second type of experiments, after the cell plating, the culture media were changed to contain 0.5% FBS for 48 hrs.…”

Section: Cell Culturesmentioning

confidence: 99%

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The human Ec peptide: the active core of a progression growth factor with species-specific mode of action

Papageorgiou

Philippou

Armakolas

et al. 2016

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ObJECTIvE: preferential IgF-1Ec expression has been firmly associated with skeletal muscle repair mechanisms, post-infarction remodeling of the myocardium, the pathophysiology of endometriosis and prostate cancer biology. Therefore, we have studied the possible biological significance of synthetic Ec peptide, a putative cleavage product of IgF-1Ec in pC-3 cells and C2C12 myoblasts. DESIgN: We had previously designed and synthesized commercially peptides corresponding to the human Ec and its mouse igf1 counterpart as well as synthetic peptides that correspond to parts of the hEc. Using proliferation and mitogenic signaling assays, we tested their effect on pC-3 cells and C2C12 myoblasts at different doses and in different culture conditions. RESUlTS: human Ec, hEc, was documented as exerting progression but not competence growth factor actions, activating ERK1/2 without affecting akt phosphorylation in pC-3 cells. a narrow concentration range of hEc (5-50nm) stimulated the growth of pC-3 cells grown in culture media supplemented with 10% FbS. hEc did not stimulate the growth of pC-3 cells cultured with media containing 0.5% FbS or in mouse C2C12 myoblasts under any culture conditions. The activity of hEc was blocked by a neutralizing anti-human IgF-1Ec antibody but not by a neutralizing anti-human IgF-1 receptor antibody. The synthetic mouse Ec was inactive in human pC-3 cells; however, it stimulated significantly the proliferation of mouse C2C12. by analyzing the bioactivity of synthetic hEc fragments, we documented that hEc's active core is located in the last 4aa of its C-terminal end. CONClUSION: The hEc peptide is an important progression factor for human pC-3 prostate cancer cells.

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Section: Discussionmentioning

confidence: 99%

Section: Cell Culturesmentioning

confidence: 99%

The human Ec peptide: the active core of a progression growth factor with species-specific mode of action

Papageorgiou

Philippou

Armakolas

et al. 2016

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“…For example, increased MMP-2 activity in muscles improves the transplantation efficiency of injected myoblasts (28). Furthermore, MMP-7, a matrilysin, enhances the migration of myoblasts and their engraftment when the myoblasts themselves express high levels of MMP-7 (6) or when the myoblasts are treated with the COOH-terminal extension of IGF-I, called the E-peptide, which in turn upregulates MMP-7 (22). Because the ECM has a multitude of different proteins, it is reasonable to assume that many different proteases, including the MMPs, are required to degrade the variety of protein substrates.…”

Section: Discussionmentioning

confidence: 99%

Matrix metalloproteinase 13 is a new contributor to skeletal muscle regeneration and critical for myoblast migration

Lei

Leong

Smith

et al. 2013

American Journal of Physiology-Cell Physiology

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Lei H, Leong D, Smith LR, Barton ER. Matrix metalloproteinase 13 is a new contributor to skeletal muscle regeneration and critical for myoblast migration. Am J Physiol Cell Physiol 305: C529-C538, 2013. First published June 12, 2013 doi:10.1152/ajpcell.00051.2013.-Efficient skeletal muscle repair and regeneration require coordinated remodeling of the extracellular matrix (ECM). Previous reports have indicated that matrix metalloproteinases (MMPs) play the pivotal role in ECM remodeling during muscle regeneration. The goal of the current study was to determine if the interstitial collagenase MMP-13 was involved in the muscle repair process. Using intramuscular cardiotoxin injections to induce acute muscle injury, we found that MMP-13 expression and activity transiently increased during the regeneration process. In addition, in muscles from mdx mice, which exhibit chronic injury, MMP-13 expression and protein levels were elevated. In differentiating C2C12 cells, a murine myoblast cell line, Mmp13 expression was most pronounced after myoblast fusion and during myotube formation. Using pharmacological inhibition of MMP-13 to test whether MMP-13 activity is necessary for the proliferation, differentiation, migration, and fusion of C2C12 cells, we found a dramatic blockade of myoblast migration, as well as a delay in differentiation. In contrast, C2C12 cells with stable overexpression of MMP-13 showed enhanced migration, without affecting myoblast maturation. Taken together, these results support a primary role for MMP-13 in myoblast migration that leads to secondary effects on differentiation.collagenase; matrix metalloproteinase; muscle repair; myoblast maturation

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“…[32][33][34] Two issues, poor cell survival and migration of grafted cells outside the injection site following transplantation have significantly hindered the overall application of this technology. 35,36 The cell death has been well studied and significantly improved by the prevention of an immune-response (rejection). 1,37,38 The donor cell migration ability also plays a key role in effectively introducing the dystophin gene to the diseased muscles.…”

Section: Discussionmentioning

confidence: 99%

MMP1 gene expression enhances myoblast migration and engraftment following implanting into mdx/SCID mice

Pan¹,

Vojnits²,

Liu

et al. 2015

Cell Adhesion & Migration

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Myoblast transplantation (MT) is a method to introduce healthy genes into abnormal skeletal muscle. It has been considered as a therapeutic modality in the last few decades for diseases such as Duchenne Muscular Dystrophy (DMD). However, challenges including cell death and poor graft engraftment have limited its application. The current experiment utilizes MMP1 gene transfer to improve the efficacy of myoblast transplantation into the diseased dystrophic skeletal muscle of mdx mice. Our results indicated that MMP1 expression can promote myogenic differentiation and fusion capacities, increase migration of MMP1 expressing myoblasts in vitro, as well as improve engraftment of dystrophin positive myofibers in vivo. Taken together, our observation suggests that the addition of MMP1 can overcome limitations in MT and improve its clinical efficacy.

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A new pro-migratory activity on human myogenic precursor cells for a synthetic peptide within the E domain of the mechano growth factor

Cited by 68 publications

References 48 publications

The human Ec peptide: the active core of a progression growth factor with species-specific mode of action

The human Ec peptide: the active core of a progression growth factor with species-specific mode of action

Matrix metalloproteinase 13 is a new contributor to skeletal muscle regeneration and critical for myoblast migration

MMP1 gene expression enhances myoblast migration and engraftment following implanting into mdx/SCID mice

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