Modulation of insulinlike growth factor I binding to human fibroblast monolayer cultures by insulinlike growth factor carrier proteins released to the incubation media.

Vroede, Monique A. de; Tseng, Linda; Katsoyannis, Panayotis G.; Nissley, S. Peter; Rechler, Matthew M.

doi:10.1172/jci112343

Cited by 134 publications

(48 citation statements)

References 24 publications

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“…As such, these findings suggest that the apparently enhanced potency of regulate not only the transport of IGFs but also their presentation to cognate cell surface receptors (28). Although the precise role(s) of tissue-derived IGFBPs is a matter of ongoing studies, both stimulation (29,30) and inhibition (31,32) of IGF binding and action have been reported. Thus, the synthesis and secretion ofIGFBPs may play a major role in the regulation of IGF hormonal action at the target cell level.…”

Section: Resultsmentioning

confidence: 87%

Granulosa cell-derived insulin-like growth factor (IGF) binding proteins are inhibitory to IGF-I hormonal action. Evidence derived from the use of a truncated IGF-I analogue.

et al. 1992

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Section: Resultsmentioning

confidence: 87%

Granulosa cell-derived insulin-like growth factor (IGF) binding proteins are inhibitory to IGF-I hormonal action. Evidence derived from the use of a truncated IGF-I analogue.

et al. 1992

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“…The synthesis and secretion of IGFBPs are thought to play important roles in the regulation of IGF hormonal action at the target cell level at a time when the extracellular concentration of IGF-I remains constant (33)(34)(35). Depending on the circumstances, IGFBPs can either inhibit (35) or stimulate (34) the action of IGF-I on mammalian cells, but their predominant Figure 7.…”

Section: Discussionmentioning

confidence: 99%

Interactions between insulin-like growth factor-I (IGF-I) and the renin-angiotensin system in follicular growth and ovulation.

Yoshimura¹,

Aoki²,

Sueoka³

et al. 1996

J. Clin. Invest.

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The interactions between insulin-like growth factor-I (IGF-I) and the renin-angiotensin system (RAS) in follicular growth and ovulation were studied with the use of an isolated perfused rabbit ovary preparation. Ovulation failed to occur in either control ovaries or the experimental ovaries perfused with IGF-I in a concentration of 1, 10, or 100 ng/ml in the absence of gonadotropin. Exposure to IGF-I stimulated the secretion rate of angiotensin II-like immunoreactivity (Ang II-IR) in perfused rabbit ovaries in a dose-dependent manner. The percent increase in follicle diameter in ovaries perfused with IGF-I for 12 h was significantly correlated with the secretion rate of Ang II-IR at 12 h after exposure to IGF-I. The addition of IGFBP-3 to the perfusate did not induce ovulation in the absence of gonadotropin, but exposure to IGFBP-3 inhibited hCG-induced ovulation in a dosedependent manner. In addition, IGFBP-3 significantly reduced the ovarian secretion rate of Ang II-IR and prostaglandins stimulated by hCG administration. Intrafollicular plasminogen activator (PA) activity significantly increased within 4 h after exposure to 100 ng/ml of IGF-I, compared with that in control ovaries perfused with medium alone. The concomitant addition of IGFBP-3 to the perfusate significantly reduced the IGF-I-stimulated PA activity in the preovulatory follicles at 4, 6, and 8 h after exposure to IGF-I. However, IGFBP-3 alone affected neither the ovarian secretion rate of Ang II-IR nor intrafollicular PA activity. Exposure to streptokinase, an exogenous PA, in vitro stimulated both follicular growth and the intrafollicular Ang II-IR content. In conclusion, IGF-I enhances both ovarian Ang II production and follicular development by stimulating intrafollicular PA activity. ( J. Clin. Invest. 1996. 98:308-316.)

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“…Their presence in milk may thus be of importance. inhibit the actions of the IGF on their target tissues (39,40), or, conversely, potentiate IGF action (41,42). In addition to being present in the circulation, mRNA for both IGF-I and IGF-I1 have been identified in multiple organ systems throughout the body, suggesting that the growth factors may be synthesized and act locally via paracrine or autocrine mechanisms (43) and be regulated by locally produced IGFBP (39)(40)(41).…”

mentioning

confidence: 99%

Insulin-Like Growth Factors I and II and Their Binding Proteins in Rat Milk

et al. 1991

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ABSTRACT. IGF-I and -11 are peptide growth factors that may be important contributors to the growth-promoting properties associated with milk. IGF in extracellular fluids, including serum and milk, are carried by specific highaffinity binding proteins (IGFBP). In this study, the levels of IGF-I and -11 in rat serum and milk were quantified by specific RIA, and the IGFBP were characterized using Western ligand blotting and autoradiography throughout lactation. The levels of IGF-I in both milk and maternal serum decreased during lactation. Serum IGF-I decreased from 743 2 187 pglL on d 1 to 391 f 106 (mean f SD) on d 21 of lactation, and milk IGF-I levels fell from 30 +:10 to 13 f 8 pg/L. Levels of IGF-I1 in serum and milk were much lower than IGF-I, and were unaffected by lactation. In maternal serum, several IGFBP were identified: IGFBP-3, which migrates as four glycosylated bands with apparent M, from 38 to 42 kD and one to two nonglycosylated bands with apparent M, of 28 to 29 kD, and an IGFBP with an apparent M, of 24 kD. In milk, IGFBP-3, the 24-kD binding protein, and a third IGFBP with an apparent M, of 29 kD were identified. Treatment of milk and serum with Endoglycosidase F reduced the four glycosylated IGFBP-3 bands (38-42 kD) to two bands with apparent M, of 35 and 32 kD. In rat milk, but not adult rat serum, the IGFBP with an apparent M, of 29 kD was immunoprecipitable by an antibody that recognizes IGFBP-2. These results demonstrate that in adult rat serum and milk both IGF-I and IGF-I1 are present, with IGF-I being predominant. IGFBP are present in rat milk; the presence of IGFBP-2 in rat milk, but not in maternal serum, indicates that IGFBP may be synthesized within the mammary gland. (Pediatr Res 29: 50-55, 1991)

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Modulation of insulinlike growth factor I binding to human fibroblast monolayer cultures by insulinlike growth factor carrier proteins released to the incubation media.

Abstract: The relative contributions of type I and type II insulinlike growth factor (IGF) receptors and IGF carrier proteins to the binding of IGF

Cited by 134 publications

References 24 publications

Granulosa cell-derived insulin-like growth factor (IGF) binding proteins are inhibitory to IGF-I hormonal action. Evidence derived from the use of a truncated IGF-I analogue.

Granulosa cell-derived insulin-like growth factor (IGF) binding proteins are inhibitory to IGF-I hormonal action. Evidence derived from the use of a truncated IGF-I analogue.

Interactions between insulin-like growth factor-I (IGF-I) and the renin-angiotensin system in follicular growth and ovulation.

Insulin-Like Growth Factors I and II and Their Binding Proteins in Rat Milk

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