Role of Insulin-Like Growth Factor Binding Protein (IGFBP)-3 in TGF-β- and GDF-8 (Myostatin)-Induced Suppression of Proliferation in Porcine Embryonic Myogenic Cell Cultures

E. Kamanga-Sollo, M. S. Pampusch, M. E. White, William R. Dayton

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22 Scopus citations

Abstract

Both transforming growth factor (TGF-β) and growth and development factor (GDF)-8 (myostatin) affect muscle differentiation by suppressing proliferation and differentiation of myogenic cells. In contrast, insulin-like growth factors (IGFs) stimulate both proliferation and differentiation of myogenic cells. In vivo, IGFs are found in association with a family of high-affinity insulin-like growth factor binding proteins (IGFBP 1-6) that affect their biological activity. Treatment of porcine embryonic myogenic cell (PEMC) cultures with either TGF-β1 of GDF-8 suppressed proliferation and increased production of IGFBP-3 protein and mRNA (P < 0.005). An anti-IGFBP-3 antibody that neutralizes the biological activity of IGFBP-3 reduced the ability of either TGF-β1 of GDF-8 to suppress PEMC proliferation (P < 0.005). However, this antibody did not affect proliferation rate in the presence of both TGF-β1 and GDF-8. These data show that IGFBP-3 plays a role in mediating the activity of either TGF-β1 of GDF-8 alone but not when both TGF-β 1 and GDF-8 are present. In contrast to findings in T47D breast cancer cells, treatment of PEMC cultures with IGFBP-3 did not result in increased levels of phosphosmad-2. Since TGF-β and GDF-8 are believed to play a significant role in regulating proliferation and differentiation of myogenic cells, our current data showing that IGFBP-3 plays a role in mediating the activity of these growth factors in muscle cell cultures strongly suggest that IGFBP-3 also may be involved in regulating these processes in myogenic cells.

Original languageEnglish (US)
Pages (from-to)225-231
Number of pages7
JournalJournal of cellular physiology
Volume197
Issue number2
DOIs
StatePublished - Nov 1 2003

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