On the nomenclature of the IGF binding proteins

Ballard, John R.; Baxter, Robert C.; Binoux, M; Clemmons, David R.; Drop, S. L. S.; Hall, K.; Hintz, R; Rechler, Matthew M.; Rutanen, Eeva‐Marja; Schwander, J

doi:10.1530/acta.0.1210751

Cited by 130 publications

(50 citation statements)

References 11 publications

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“…The IGFs circulate monocovalently bound to large molecular weight IGFBPs [7,43]. Six binding proteins (-1 to -6) have been characterized in humans, rodents and domestic animals [5,49,77]. IGFBPs are physiological regulators of IGF actions, either stimulating or inhibiting IGF action [44].…”

Section: The Insulin-like Growth Factor Systemmentioning

confidence: 99%

Insulin-Like Growth Factor-I as a Possible Hormonal Mediator of Nutritional Regulation of Reproduction in Cattle

Zulu

Nakao

Sawamukai

2002

The Journal of Veterinary Medical Science

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ABSTRACT. The current review aims to establish insulin-like growth factor-1 (IGF-I) as the factor that signals nutritional status to the reproductive axis, and show that assessment of IGF-I in blood early postpartum during the negative energy balance (NEB) period could be used to predict both nutritional and reproductive status in dairy cattle. The review also explores the effect of nutritional status on circulating IGF-I concentrations and the endocrine role of IGF-I on the reproductive axis. IGF-I plays an important role in gonadotropininduced folliculogenesis, ovarian steroidogenesis and corpus luteum (CL) function. It also modulates pituitary and hypothalamus function. IGF-I clearly has an endocrine role on the reproductive axis. Severe under nutrition significantly reduces plasma IGF-I concentrations. During the critical period of NEB in high yielding dairy cattle early postpartum, IGF-I concentrations are low in blood and its levels are positively correlated to energy status and reproductive function during this period. Changes in circulating IGF-I immediately postpartum may help predict both nutritional and reproductive status in dairy cattle. IGF-I is therefore one of the long sought factors that signal nutritional status to the reproductive axis.

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Section: The Insulin-like Growth Factor Systemmentioning

confidence: 99%

Insulin-Like Growth Factor-I as a Possible Hormonal Mediator of Nutritional Regulation of Reproduction in Cattle

Zulu

Nakao

Sawamukai

2002

The Journal of Veterinary Medical Science

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“…The insulin-like growth factors (IGF)-I and -II circulate bound to a series of six high affinity IGF binding proteins (IGFBP-1 to -6) which regulate their bioavailability and bioactivity (Ballard et al 1989(Ballard et al , 1992. IGFBP-3, combined with either IGF-I or IGF-II and an acid labile subunit (ALS), provides a circulating reservoir of IGFs which is retained in the circulation .…”

Section: Introductionmentioning

confidence: 99%

The effects of recombinant human IGF-I administration on concentrations of acid labile subunit, IGF binding protein-3, IGF-I, IGF-II and proteolysis of IGF binding protein-3 in adolescents with insulin-dependent diabetes mellitus

Cheetham

Holly²,

Baxter³

et al. 1998

Journal of Endocrinology

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“…Our laboratory has demonstrated that a specific form of IGFBP derived from human amniotic fluid, designated IGFBP-1 (1), potentiates the mitogenic activity of IGF-I in smooth muscle cells and fibroblasts in culture (2). Not all ofour IGFBP-1 preparations have demonstrated equivalent biologic activity, and other laboratories, using various biologic test systems, have reported that IGFBP-1 inhibits the effects of IGF-I.…”

Section: Introductionmentioning

confidence: 99%

Phosphorylation of insulin-like growth factor (IGF)-binding protein 1 in cell culture and in vivo: effects on affinity for IGF-I.

Jones

D’Ercole

Camacho‐Hübner

et al. 1991

Proc. Natl. Acad. Sci. U.S.A.

274

190

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The insulin-like growth factors (IGF-I and IGF-II) are present in extracellular fluids bound to specific IGF-binding proteins (IGFBPs). We and others have reported varying biologic activity of different preparations of IGFBP-1 that appeared to have identical amino acid sequences and molecular sizes. This observation prompted us to determine whether IGFBP-1 undergoes posttranslational modifications. Immunoprecipitation was used to show that Chinese hamster ovary cells (transfected with a human IGFBP-l cDNA construct) and human hepatoma (HepG2) cells secrete 32P-labeled IGFBP-1 following incubation with [32P orthophosphate. Phospho amino acid analysis of 32P-labeled IGFBP-l revealed only phosphoserine residues. A method was developed that could separate nonphosphorylated IGFBP-l from four or five phosphorylated isoforms. Using this technique we demonstrated that human amniotic fluid and human fetal serum contain a large proportion of nonphosphorylated IGFBP-1, as well as phosphorylated forms. In contrast, HepG2 cells and human decidual cells secrete predominantly the phosphorylated isoforms. These observations suggest that IGFBP-1 is secreted as a phosphoprotein and is subsequently dephosphorylated in vivo. Binding studies showed that the phosphorylated IGFBP-1 secreted by HepG2 cells has a 6-fold higher affinity for IGF-I than it does after dephosphorylation. We conclude that IGFBP-1 is phosphorylated and that this phosphorylation is a physiologically important posttranslational modification.

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On the nomenclature of the IGF binding proteins

Cited by 130 publications

References 11 publications

Insulin-Like Growth Factor-I as a Possible Hormonal Mediator of Nutritional Regulation of Reproduction in Cattle

Insulin-Like Growth Factor-I as a Possible Hormonal Mediator of Nutritional Regulation of Reproduction in Cattle

The effects of recombinant human IGF-I administration on concentrations of acid labile subunit, IGF binding protein-3, IGF-I, IGF-II and proteolysis of IGF binding protein-3 in adolescents with insulin-dependent diabetes mellitus

Phosphorylation of insulin-like growth factor (IGF)-binding protein 1 in cell culture and in vivo: effects on affinity for IGF-I.

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