Skip to main content

Soluble miniagrin enhances contractile function of engineered skeletal muscle.

Publication ,  Journal Article
Bian, W; Bursac, N
Published in: FASEB journal : official publication of the Federation of American Societies for Experimental Biology
February 2012

Neural agrin plays a pleiotropic role in skeletal muscle innervation and maturation, but its specific effects on the contractile function of aneural engineered muscle remain unknown. In this study, neonatal rat skeletal myoblasts cultured within 3-dimensional engineered muscle tissue constructs were treated with 10 nM soluble recombinant miniagrin and assessed using histological, biochemical, and functional assays. Depending on the treatment duration and onset time relative to the stage of myogenic differentiation, miniagrin was found to induce up to 1.7-fold increase in twitch and tetanus force amplitude. This effect was associated with the 2.3-fold up-regulation of dystrophin gene expression at 6 d after agrin removal and enhanced ACh receptor (AChR) cluster formation, but no change in cell number, expression of muscle myosin, or important aspects of intracellular Ca(2+) handling. In muscle constructs with endogenous ACh levels suppressed by the application of α-NETA, miniagrin increased AChR clustering and twitch force amplitude but failed to improve intracellular Ca(2+) handling and increase tetanus-to-twitch ratio. Overall, our studies suggest that besides its synaptogenic function that could promote integration of engineered muscle constructs in vivo, neural agrin can directly promote the contractile function of aneural engineered muscle via mechanisms distinct from those involving endogenous ACh.

Duke Scholars

Published In

FASEB journal : official publication of the Federation of American Societies for Experimental Biology

DOI

EISSN

1530-6860

ISSN

0892-6638

Publication Date

February 2012

Volume

26

Issue

2

Start / End Page

955 / 965

Related Subject Headings

  • Up-Regulation
  • Tissue Engineering
  • Solubility
  • Recombinant Proteins
  • Receptors, Cholinergic
  • Rats
  • Myosins
  • Myoblasts, Skeletal
  • Muscle, Skeletal
  • Isometric Contraction
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Bian, W., & Bursac, N. (2012). Soluble miniagrin enhances contractile function of engineered skeletal muscle. FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology, 26(2), 955–965. https://doi.org/10.1096/fj.11-187575
Bian, Weining, and Nenad Bursac. “Soluble miniagrin enhances contractile function of engineered skeletal muscle.FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology 26, no. 2 (February 2012): 955–65. https://doi.org/10.1096/fj.11-187575.
Bian W, Bursac N. Soluble miniagrin enhances contractile function of engineered skeletal muscle. FASEB journal : official publication of the Federation of American Societies for Experimental Biology. 2012 Feb;26(2):955–65.
Bian, Weining, and Nenad Bursac. “Soluble miniagrin enhances contractile function of engineered skeletal muscle.FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology, vol. 26, no. 2, Feb. 2012, pp. 955–65. Epmc, doi:10.1096/fj.11-187575.
Bian W, Bursac N. Soluble miniagrin enhances contractile function of engineered skeletal muscle. FASEB journal : official publication of the Federation of American Societies for Experimental Biology. 2012 Feb;26(2):955–965.

Published In

FASEB journal : official publication of the Federation of American Societies for Experimental Biology

DOI

EISSN

1530-6860

ISSN

0892-6638

Publication Date

February 2012

Volume

26

Issue

2

Start / End Page

955 / 965

Related Subject Headings

  • Up-Regulation
  • Tissue Engineering
  • Solubility
  • Recombinant Proteins
  • Receptors, Cholinergic
  • Rats
  • Myosins
  • Myoblasts, Skeletal
  • Muscle, Skeletal
  • Isometric Contraction