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BioMed research international
2020;2020 6093974.

Type I Collagen Suspension Induces Neocollagenesis and Myodifferentiation in Fibroblasts .

Francesca Lombardi, Paola Palumbo, Francesca Rosaria Augello, Ilaria Giusti, Vincenza Dolo, Luca Guerrini, Maria Grazia Cifone, Maurizio Giuliani, Benedetta Cinque
Author Information
  1. Francesca Lombardi: Department of Life, Health & Environmental Sciences, University of L'Aquila, L'Aquila 67100, Italy. ORCID
  2. Paola Palumbo: Department of Life, Health & Environmental Sciences, University of L'Aquila, L'Aquila 67100, Italy. ORCID
  3. Francesca Rosaria Augello: Department of Life, Health & Environmental Sciences, University of L'Aquila, L'Aquila 67100, Italy. ORCID
  4. Ilaria Giusti: Department of Life, Health & Environmental Sciences, University of L'Aquila, L'Aquila 67100, Italy. ORCID
  5. Vincenza Dolo: Department of Life, Health & Environmental Sciences, University of L'Aquila, L'Aquila 67100, Italy. ORCID
  6. Luca Guerrini: Department of Life, Health & Environmental Sciences, University of L'Aquila, L'Aquila 67100, Italy. ORCID
  7. Maria Grazia Cifone: Department of Life, Health & Environmental Sciences, University of L'Aquila, L'Aquila 67100, Italy. ORCID
  8. Maurizio Giuliani: Department of Life, Health & Environmental Sciences, University of L'Aquila, L'Aquila 67100, Italy. ORCID
  9. Benedetta Cinque: Department of Life, Health & Environmental Sciences, University of L'Aquila, L'Aquila 67100, Italy. ORCID
PMID: 34368344 DOI: 10.1155/2020/6093974

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 -smooth muscle actin (-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 .

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MeSH Term

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

Chemicals

Actins
Antigens, Differentiation
Collagen Type I
HSP47 Heat-Shock Proteins
Serpinh1 protein, mouse
Prolyl Hydroxylases
Journal Article

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