Regulation of insulin-like growth factor (IGF)-binding protein synthesis by insulin and IGF-I in cultured bovine fibroblasts

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Abstract

Specific insulin-like growth factor-binding proteins (IGFBPs) are synthesized and secreted by bovine fibroblasts in vitro. By Western ligand blotting, three molecular forms of IGFBP were identified in conditioned medium from control cultures with mol wt (M(r)) of 34,000, 28,000, and 24,000. Concentrations of these three IGFBP forms increased with time in serum-free conditioned medium without benefit of hormonal supplementation. Insulin and IGF-I were potent stimuli for IGFBP production by bovine fibroblasts, whereas bovine GH, epidermal growth factor, or steroid treatment had little or no effect. Insulin and IGF-I enhanced the production of 24,000, 28,000, and 34,000 M(r) IGFBPs in a dose-dependent fashion. Moreover, addition of low nanomolar concentrations of insulin or IGF-I to bovine fibroblast cultures specifically induced the secretion of a 42,000/38,000 M(r) species of IGFBP, which corresponded in size to the IGF-binding subunit of the principal 150,000 M(r) IGFBP complex in serum. After stimulation with insulin or IGF-I, bovine fibroblasts (3 x 105 cells) secreted approximately 30 ng/24 h 42,000/38,000 M(r) IGFBP. Subunits of 42,000/38,000 M(r) in bovine fibroblast-conditioned medium did not form macromolecular complexes in either the absence or presence of bovine GH.

Original languageEnglish (US)
Pages (from-to)3139-3145
Number of pages7
JournalEndocrinology
Volume126
Issue number6
StatePublished - 1990

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Insulin-Like Growth Factor Binding Proteins
Insulin-Like Growth Factor I
Fibroblasts
Insulin
Conditioned Culture Medium
Macromolecular Substances
Serum-Free Culture Media
Somatomedins
Epidermal Growth Factor
Western Blotting
Steroids
Ligands

ASJC Scopus subject areas

  • Endocrinology
  • Endocrinology, Diabetes and Metabolism

Cite this

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title = "Regulation of insulin-like growth factor (IGF)-binding protein synthesis by insulin and IGF-I in cultured bovine fibroblasts",
abstract = "Specific insulin-like growth factor-binding proteins (IGFBPs) are synthesized and secreted by bovine fibroblasts in vitro. By Western ligand blotting, three molecular forms of IGFBP were identified in conditioned medium from control cultures with mol wt (M(r)) of 34,000, 28,000, and 24,000. Concentrations of these three IGFBP forms increased with time in serum-free conditioned medium without benefit of hormonal supplementation. Insulin and IGF-I were potent stimuli for IGFBP production by bovine fibroblasts, whereas bovine GH, epidermal growth factor, or steroid treatment had little or no effect. Insulin and IGF-I enhanced the production of 24,000, 28,000, and 34,000 M(r) IGFBPs in a dose-dependent fashion. Moreover, addition of low nanomolar concentrations of insulin or IGF-I to bovine fibroblast cultures specifically induced the secretion of a 42,000/38,000 M(r) species of IGFBP, which corresponded in size to the IGF-binding subunit of the principal 150,000 M(r) IGFBP complex in serum. After stimulation with insulin or IGF-I, bovine fibroblasts (3 x 105 cells) secreted approximately 30 ng/24 h 42,000/38,000 M(r) IGFBP. Subunits of 42,000/38,000 M(r) in bovine fibroblast-conditioned medium did not form macromolecular complexes in either the absence or presence of bovine GH.",
author = "Conover, {Cheryl A}",
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T1 - Regulation of insulin-like growth factor (IGF)-binding protein synthesis by insulin and IGF-I in cultured bovine fibroblasts

AU - Conover, Cheryl A

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N2 - Specific insulin-like growth factor-binding proteins (IGFBPs) are synthesized and secreted by bovine fibroblasts in vitro. By Western ligand blotting, three molecular forms of IGFBP were identified in conditioned medium from control cultures with mol wt (M(r)) of 34,000, 28,000, and 24,000. Concentrations of these three IGFBP forms increased with time in serum-free conditioned medium without benefit of hormonal supplementation. Insulin and IGF-I were potent stimuli for IGFBP production by bovine fibroblasts, whereas bovine GH, epidermal growth factor, or steroid treatment had little or no effect. Insulin and IGF-I enhanced the production of 24,000, 28,000, and 34,000 M(r) IGFBPs in a dose-dependent fashion. Moreover, addition of low nanomolar concentrations of insulin or IGF-I to bovine fibroblast cultures specifically induced the secretion of a 42,000/38,000 M(r) species of IGFBP, which corresponded in size to the IGF-binding subunit of the principal 150,000 M(r) IGFBP complex in serum. After stimulation with insulin or IGF-I, bovine fibroblasts (3 x 105 cells) secreted approximately 30 ng/24 h 42,000/38,000 M(r) IGFBP. Subunits of 42,000/38,000 M(r) in bovine fibroblast-conditioned medium did not form macromolecular complexes in either the absence or presence of bovine GH.

AB - Specific insulin-like growth factor-binding proteins (IGFBPs) are synthesized and secreted by bovine fibroblasts in vitro. By Western ligand blotting, three molecular forms of IGFBP were identified in conditioned medium from control cultures with mol wt (M(r)) of 34,000, 28,000, and 24,000. Concentrations of these three IGFBP forms increased with time in serum-free conditioned medium without benefit of hormonal supplementation. Insulin and IGF-I were potent stimuli for IGFBP production by bovine fibroblasts, whereas bovine GH, epidermal growth factor, or steroid treatment had little or no effect. Insulin and IGF-I enhanced the production of 24,000, 28,000, and 34,000 M(r) IGFBPs in a dose-dependent fashion. Moreover, addition of low nanomolar concentrations of insulin or IGF-I to bovine fibroblast cultures specifically induced the secretion of a 42,000/38,000 M(r) species of IGFBP, which corresponded in size to the IGF-binding subunit of the principal 150,000 M(r) IGFBP complex in serum. After stimulation with insulin or IGF-I, bovine fibroblasts (3 x 105 cells) secreted approximately 30 ng/24 h 42,000/38,000 M(r) IGFBP. Subunits of 42,000/38,000 M(r) in bovine fibroblast-conditioned medium did not form macromolecular complexes in either the absence or presence of bovine GH.

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