Linked Life Data

12599210

Source:http://linkedlifedata.com/resource/pubmed/id/12599210

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2003-2-24
pubmed:abstractText
Although muscle satellite cells were identified almost 40 years ago, little is known about the induction of their proliferation and differentiation in response to physiological/pathological stimuli or to growth factors/cytokines. In order to investigate the role of the insulin-like growth factor (IGF)/IGF binding protein (IGFBP) system in adult human myoblast differentiation we have developed a primary human skeletal muscle cell model. We show that under low serum media (LSM) differentiating conditions, the cells secrete IGF binding proteins-2, -3, -4 and -5. Intact IGFBP-5 was detected at days 1 and 2 but by day 7 in LSM it was removed by proteolysis. IGFBP-4 levels were also decreased at day 7 in the presence of IGF-I, potentially by proteolysis. In contrast, we observed that IGFBP-3 initially decreased on transfer of cells into LSM but then increased with myotube formation. Treatment with 20 ng/ml tumour necrosis factor-alpha (TNFalpha), which inhibits myoblast differentiation, blocked IGFBP-3 production and secretion whereas 30 ng/ml IGF-I, which stimulates myoblast differentiation, increased IGFBP-3 secretion. The TNFalpha-induced decrease in IGFBP-3 production and inhibition of differentiation could not be rescued by addition of IGF-I. LongR(3)IGF-I, which does not bind to the IGFBPs, had a similar effect on differentiation and IGFBP-3 secretion as IGF-I, both with and without TNFalpha, confirming that increased IGFBP-3 is not purely due to increased stability conferred by binding to IGF-I. Furthermore reduction of IGFBP-3 secretion using antisense oligonucleotides led to an inhibition of differentiation. Taken together these data indicate that IGFBP-3 supports myoblast differentiation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9541
pubmed:author
pubmed:copyrightInfo
Copyright 2003 Wiley-Liss, Inc.
pubmed:issnType
Print
pubmed:volume
195
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
70-9
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:12599210-Adult, pubmed-meshheading:12599210-Aged, pubmed-meshheading:12599210-Aged, 80 and over, pubmed-meshheading:12599210-Cell Differentiation, pubmed-meshheading:12599210-Cells, Cultured, pubmed-meshheading:12599210-Culture Media, Conditioned, pubmed-meshheading:12599210-Female, pubmed-meshheading:12599210-Humans, pubmed-meshheading:12599210-Insulin-Like Growth Factor Binding Protein 3, pubmed-meshheading:12599210-Insulin-Like Growth Factor Binding Protein 4, pubmed-meshheading:12599210-Insulin-Like Growth Factor Binding Protein 5, pubmed-meshheading:12599210-Insulin-Like Growth Factor I, pubmed-meshheading:12599210-Male, pubmed-meshheading:12599210-Middle Aged, pubmed-meshheading:12599210-Myoblasts, Skeletal, pubmed-meshheading:12599210-Oligonucleotides, Antisense, pubmed-meshheading:12599210-Tumor Necrosis Factor-alpha
pubmed:year
2003
pubmed:articleTitle
Role of insulin-like growth factor binding protein-3 (IGFBP-3) in the differentiation of primary human adult skeletal myoblasts.
pubmed:affiliation
Division of Surgery, University of Bristol, Bristol Royal Infirmary, Bristol, England. foulstone@bristol.ac.uk
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't