Partial biochemical maturation of aneurally cultured human skeletal muscle

S. T. Iannaccone, B. Nagy, F. J. Samaha

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

We studied cultures of human skeletal muscle in vitro and established standards for biochemical markers of cellular differentiation. DNA synthesis ceased at the time of fusion, implying the absence of fibroblasts. Myosin heavy-chain synthesis, creatine and pyruvate kinase activities, and isoenzymes of creatine kinase were measured serially over 36 days. Filamin and fibronectin proteins were identified in these cultures. Compared to chick muscle in culture, human skeletal muscle cells remained relatively immature. These data provide a basis for the study of diseased human muscle cells in culture.

Original languageEnglish (US)
Pages (from-to)846-851
Number of pages6
JournalNeurology
Volume32
Issue number8
StatePublished - 1982

Fingerprint

Skeletal Muscle
Creatine Kinase
Muscle Cells
Filamins
Pyruvate Kinase
Fibronectins
Isoenzymes
Cell Culture Techniques
Fibroblasts
Biomarkers
Muscles
DNA
Proteins
In Vitro Techniques
myosin-heavy-chain kinase

ASJC Scopus subject areas

  • Neuroscience(all)

Cite this

Partial biochemical maturation of aneurally cultured human skeletal muscle. / Iannaccone, S. T.; Nagy, B.; Samaha, F. J.

In: Neurology, Vol. 32, No. 8, 1982, p. 846-851.

Research output: Contribution to journalArticle

Iannaccone, S. T. ; Nagy, B. ; Samaha, F. J. / Partial biochemical maturation of aneurally cultured human skeletal muscle. In: Neurology. 1982 ; Vol. 32, No. 8. pp. 846-851.
@article{2a286cfca8fc487ea6f3002234326d6f,
title = "Partial biochemical maturation of aneurally cultured human skeletal muscle",
abstract = "We studied cultures of human skeletal muscle in vitro and established standards for biochemical markers of cellular differentiation. DNA synthesis ceased at the time of fusion, implying the absence of fibroblasts. Myosin heavy-chain synthesis, creatine and pyruvate kinase activities, and isoenzymes of creatine kinase were measured serially over 36 days. Filamin and fibronectin proteins were identified in these cultures. Compared to chick muscle in culture, human skeletal muscle cells remained relatively immature. These data provide a basis for the study of diseased human muscle cells in culture.",
author = "Iannaccone, {S. T.} and B. Nagy and Samaha, {F. J.}",
year = "1982",
language = "English (US)",
volume = "32",
pages = "846--851",
journal = "Neurology",
issn = "0028-3878",
publisher = "Lippincott Williams and Wilkins",
number = "8",

}

TY - JOUR

T1 - Partial biochemical maturation of aneurally cultured human skeletal muscle

AU - Iannaccone, S. T.

AU - Nagy, B.

AU - Samaha, F. J.

PY - 1982

Y1 - 1982

N2 - We studied cultures of human skeletal muscle in vitro and established standards for biochemical markers of cellular differentiation. DNA synthesis ceased at the time of fusion, implying the absence of fibroblasts. Myosin heavy-chain synthesis, creatine and pyruvate kinase activities, and isoenzymes of creatine kinase were measured serially over 36 days. Filamin and fibronectin proteins were identified in these cultures. Compared to chick muscle in culture, human skeletal muscle cells remained relatively immature. These data provide a basis for the study of diseased human muscle cells in culture.

AB - We studied cultures of human skeletal muscle in vitro and established standards for biochemical markers of cellular differentiation. DNA synthesis ceased at the time of fusion, implying the absence of fibroblasts. Myosin heavy-chain synthesis, creatine and pyruvate kinase activities, and isoenzymes of creatine kinase were measured serially over 36 days. Filamin and fibronectin proteins were identified in these cultures. Compared to chick muscle in culture, human skeletal muscle cells remained relatively immature. These data provide a basis for the study of diseased human muscle cells in culture.

UR - http://www.scopus.com/inward/record.url?scp=0020024382&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0020024382&partnerID=8YFLogxK

M3 - Article

VL - 32

SP - 846

EP - 851

JO - Neurology

JF - Neurology

SN - 0028-3878

IS - 8

ER -