In vitro myogenesis induced by human recombinant elastin-like proteins. (October 2015)
- Record Type:
- Journal Article
- Title:
- In vitro myogenesis induced by human recombinant elastin-like proteins. (October 2015)
- Main Title:
- In vitro myogenesis induced by human recombinant elastin-like proteins
- Authors:
- D'Andrea, Paola
Scaini, Denis
Severino, Luisa Ulloa
Borelli, Violetta
Passamonti, Sabina
Lorenzon, Paola
Bandiera, Antonella - Abstract:
- Abstract: Mammalian adult skeletal muscle has a limited ability to regenerate after injury, usage or trauma. A promising strategy for successful regenerative technology is the engineering of bio interfaces that mimic the characteristics of the extracellular matrix. Human elastin-like polypeptides (HELPs) have been synthesized as biomimetic materials that maintain some peculiar properties of the native protein. We developed a novel Human Elastin Like Polypeptide obtained by fusing the elastin-like backbone to a domain present in the α2 chain of type IV collagen, containing two RGD motives. We employed this peptide as adhesion substrate for C2C12 myoblasts and compared its effects to those induced by two other polypeptides of the HELP series. Myoblast adhered to all HELPs coatings, where they assumed morphology and cytoarchitecture that depended on the polypeptide structure. Adhesion to HELPs stimulated at a different extent cell proliferation and differentiation, the expression of Myosin Heavy Chain and the fusion of aligned fibers into multinucleated myotubes. Adhesion substrates significantly altered myotubes stiffness, measured by Atomic Force Microscopy, and differently affected the cells Ca 2+ handling capacity and the maturation of excitation-contraction coupling machinery, evaluated by Ca 2+ imaging. Overall, our findings indicate that the properties of HELP biopolymers can be exploited for dissecting the molecular connections underlying myogenic differentiation andAbstract: Mammalian adult skeletal muscle has a limited ability to regenerate after injury, usage or trauma. A promising strategy for successful regenerative technology is the engineering of bio interfaces that mimic the characteristics of the extracellular matrix. Human elastin-like polypeptides (HELPs) have been synthesized as biomimetic materials that maintain some peculiar properties of the native protein. We developed a novel Human Elastin Like Polypeptide obtained by fusing the elastin-like backbone to a domain present in the α2 chain of type IV collagen, containing two RGD motives. We employed this peptide as adhesion substrate for C2C12 myoblasts and compared its effects to those induced by two other polypeptides of the HELP series. Myoblast adhered to all HELPs coatings, where they assumed morphology and cytoarchitecture that depended on the polypeptide structure. Adhesion to HELPs stimulated at a different extent cell proliferation and differentiation, the expression of Myosin Heavy Chain and the fusion of aligned fibers into multinucleated myotubes. Adhesion substrates significantly altered myotubes stiffness, measured by Atomic Force Microscopy, and differently affected the cells Ca 2+ handling capacity and the maturation of excitation-contraction coupling machinery, evaluated by Ca 2+ imaging. Overall, our findings indicate that the properties of HELP biopolymers can be exploited for dissecting the molecular connections underlying myogenic differentiation and for designing novel substrates for skeletal muscle regeneration. … (more)
- Is Part Of:
- Biomaterials. Volume 67(2015)
- Journal:
- Biomaterials
- Issue:
- Volume 67(2015)
- Issue Display:
- Volume 67, Issue 2015 (2015)
- Year:
- 2015
- Volume:
- 67
- Issue:
- 2015
- Issue Sort Value:
- 2015-0067-2015-0000
- Page Start:
- 240
- Page End:
- 253
- Publication Date:
- 2015-10
- Subjects:
- Elastin-like polypeptides -- Biomimetic materials -- Cell adhesion -- Skeletal muscle regeneration -- Excitation-contraction coupling -- Intracellular calcium
Biomedical materials -- Periodicals
Biocompatible Materials -- Periodicals
Biomatériaux -- Périodiques
610.28 - Journal URLs:
- http://www.sciencedirect.com/science/journal/01429612 ↗
http://www.clinicalkey.com/dura/browse/journalIssue/01429612 ↗
http://www.clinicalkey.com.au/dura/browse/journalIssue/01429612 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.biomaterials.2015.07.041 ↗
- Languages:
- English
- ISSNs:
- 0142-9612
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 2087.715000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 8186.xml