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BioMed research international2020; 2020; 6093974; doi: 10.1155/2020/6093974

Type I Collagen Suspension Induces Neocollagenesis and Myodifferentiation in Fibroblasts In Vitro.

Abstract: The ability of a collagen-based matrix to support cell proliferation, migration, and infiltration has been reported; however, the direct effect of an aqueous collagen suspension on cell cultures has not been studied yet. In this work, the effects of a high-concentration aqueous suspension of a micronized type I equine collagen (EC-I) have been evaluated on a normal mouse fibroblast cell line. Immunofluorescence analysis showed the ability of EC-I to induce a significant increase of type I and III collagen levels, parallel with overexpression of crucial proteins in collagen biosynthesis, maturation, and secretion, prolyl 4-hydroxylase (P4H) and heat shock protein 47 (HSP47), as demonstrated by western blot experiments. The treatment led, also, to an increase of α-smooth muscle actin (α-SMA) expression, evaluated through western blot analysis, and cytoskeletal reorganization, as assessed by phalloidin staining. Moreover, scanning electron microscopy analysis highlighted the appearance of plasma membrane extensions and blebbing of extracellular vesicles. Altogether, these results strongly suggest that an aqueous collagen type I suspension is able to induce fibroblast myodifferentiation. Moreover, our findings also support in vitro models as a useful tool to evaluate the effects of a collagen suspension and understand the molecular signaling pathways possibly involved in the effects observed following collagen treatment in vivo.
Copyright © 2020 Francesca Lombardi et al.
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Publication Date: 2020-06-26 PubMed ID: 34368344PubMed Central: PMC8337109DOI: 10.1155/2020/6093974Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

The research investigated the impact of an aqueous suspension of a specific type of collagen (EC-I) on a normal mouse fibroblast cell line and revealed that it can promote increased collagen levels and the expression of certain proteins, which implies that this suspension could trigger myodifferentiation in fibroblasts.

Specific Findings

  • This study focused on understanding how an aqueous suspension of micronized type I equine collagen (EC-I) directly impacts normal mouse fibroblast cells, to which previous research has not significantly contributed.
  • Immunofluorescence analysis in the research disclosed that EC-I could cause a considerable upsurge in the levels of type I and III collagen, which play roles in maintaining the health and healing of the skin, blood vessels, and connective tissues.
  • The effect of EC-I also paralleled an overexpression of key proteins in collagen biosynthesis, secretion, and maturation, namely, Prolyl 4-Hydroxylase (P4H) and Heat Shock Protein 47 (HSP47).
  • This increase in protein expression was demonstrated using western blot experiments, a commonly used method in molecular biology for detecting specific proteins in a sample of tissue homogenate or extract.

Additional Observations

  • The research noticed an enhancement in the expression of a protein named ‘smooth muscle actin (-SMA)’ following the implementation of the collagen treatment. This protein is often upregulated during the differentiation of fibroblasts into myofibroblasts, which are cells that help wounds heal.
  • The researchers also recorded a change in cytoskeletal organization, observed via a technique known as phalloidin staining, which is used to visualize the arrangements of actin filaments.
  • Utilizing scanning electron microscopy, the study noted the emergence of extensions in the plasma membrane and the blebbing of extracellular vesicles, which are small bubble-like particles that exist in and around cells.

Conclusions and Implications

  • Collectively, these findings imply that the use of an aqueous suspension of type I collagen could spur myodifferentiation in fibroblasts, a process by which fibroblasts evolve into muscle cells. This could have applications in wound healing or tissue regeneration.
  • This study provides backing to the use of in vitro models—where biological processes are studied in a controlled laboratory setting, such as a test tube or petri dish—for evaluating the impact of collagen treatment and understanding the molecular signaling pathway which could be involved.

Cite This Article

APA
Lombardi F, Palumbo P, Augello FR, Giusti I, Dolo V, Guerrini L, Cifone MG, Giuliani M, Cinque B. (2020). Type I Collagen Suspension Induces Neocollagenesis and Myodifferentiation in Fibroblasts In Vitro. Biomed Res Int, 2020, 6093974. https://doi.org/10.1155/2020/6093974

Publication

BioMed research international
ISSN: 2314-6141
NlmUniqueID: 101600173
Country: United States
Language: English
Volume: 2020
Pages: 6093974

Researcher Affiliations

Lombardi, Francesca
  • Department of Life, Health & Environmental Sciences, University of L'Aquila, L'Aquila 67100, Italy.
Palumbo, Paola
  • Department of Life, Health & Environmental Sciences, University of L'Aquila, L'Aquila 67100, Italy.
Augello, Francesca Rosaria
  • Department of Life, Health & Environmental Sciences, University of L'Aquila, L'Aquila 67100, Italy.
Giusti, Ilaria
  • Department of Life, Health & Environmental Sciences, University of L'Aquila, L'Aquila 67100, Italy.
Dolo, Vincenza
  • Department of Life, Health & Environmental Sciences, University of L'Aquila, L'Aquila 67100, Italy.
Guerrini, Luca
  • Department of Life, Health & Environmental Sciences, University of L'Aquila, L'Aquila 67100, Italy.
Cifone, Maria Grazia
  • Department of Life, Health & Environmental Sciences, University of L'Aquila, L'Aquila 67100, Italy.
Giuliani, Maurizio
  • Department of Life, Health & Environmental Sciences, University of L'Aquila, L'Aquila 67100, Italy.
  • Unit of Plastic and Reconstructive Surgery, Casa di Cura "Di Lorenzo" SrL, Via Vittorio Veneto 37, Avezzano, 67051 L'Aquila, Italy.
Cinque, Benedetta
  • Department of Life, Health & Environmental Sciences, University of L'Aquila, L'Aquila 67100, Italy.

MeSH Terms

  • Actins / biosynthesis
  • Animals
  • Antigens, Differentiation / biosynthesis
  • Cell Differentiation
  • Collagen Type I / chemistry
  • Fibroblasts / metabolism
  • HSP47 Heat-Shock Proteins / biosynthesis
  • Horses
  • Mice
  • Models, Biological
  • NIH 3T3 Cells
  • Prolyl Hydroxylases / biosynthesis

Conflict of Interest Statement

The authors declare no conflict of interest.

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