Insulin-like growth factor-I (IGF-I) system during follicle development in the bovine ovary: Relationship among IGF-I, type 1 IGF receptor (IGFR-1) and pregnancy-associated plasma protein-A (PAPP-A)

2007 ◽  
Vol 264 (1-2) ◽  
pp. 197-203 ◽  
Author(s):  
N. Sudo ◽  
T. Shimizu ◽  
C. Kawashima ◽  
E. Kaneko ◽  
M. Tetsuka ◽  
...  
Keyword(s):  
Growth Factor ◽  
Plasma Protein ◽  
Protein A ◽  
Follicle Development ◽  
Insulin Like Growth Factor ◽  
Factor I ◽  
Igf I ◽  
Bovine Ovary ◽  
Igf Receptor

Receptor binding of insulin-like growth factor-I to mammary microsomes from non-pregnant, pregnant and lactating sheep

1993 ◽  
Vol 136 (2) ◽  
pp. 297-304 ◽  
Author(s):  
S. J. Winder ◽  
S. D. Wheatley ◽  
I. A. Forsyth
Keyword(s):  
Growth Factor ◽  
Membrane Protein ◽  
Binding Affinity ◽  
Binding Sites ◽  
Insulin Like Growth Factor ◽  
Factor I ◽  
Pregnant Sheep ◽  
Igf I ◽  
Igf Receptor

ABSTRACT Sucrose density centrifugation was used to prepare a partially purified membrane fraction from the mammary glands of non-pregnant, pregnant and lactating sheep. The binding of125 I-labelled insulin-like growth factor-I (IGF-I) was dependent on membrane protein concentration, pH, time and temperature. The binding showed the characteristics of a type-1 IGF receptor, being displaced by IGF-I (median effective dose (ED50) 0·55 nmol/l), less effectively by IGF-II (ED50 8·8 nmol/l) and least effectively by insulin. Glucagon, ovine prolactin and ovine placental lactogen could not displace binding. A molecular weight of 135 000 was determined by affinity cross-linking using disuccinimidyl suberate; this was consistent with the reported size of the type-1 receptor α-subunit. Scatchard analysis was used to determine binding affinity and numbers of IGF-I-binding sites. A single class of high-affinity binding sites was found in all physiological states. In non-pregnant sheep and sheep at days 40, 75 and 110–120 of pregnancy and at term, the binding affinity was similar (apparent dissociation constant (Kd) 2·73 ±0·31 nmol/l, n = 22). In lactating sheep (weeks 1, 4 and 10), the binding affinity was significantly (P = 0·02) higher (Kd 0·77± 0·06 nmol/l n = 9). Binding capacity was similar in non-pregnant and pregnant sheep (1005 ± 113 fmol/mg, n = 19), but fell by parturition and remained low in lactation (570±52 fmol/mg membrane protein, n = 12). The results suggest that the mammary growth of pregnancy is not regulated at the level of the type-1 IGF receptor. Journal of Endocrinology (1993) 136, 297–304

scholarly journals The C Region of Human Insulin-like Growth Factor (IGF) I Is Required for High Affinity Binding to the Type 1 IGF Receptor

1989 ◽  
Vol 264 (19) ◽  
pp. 11004-11008 ◽  
Author(s):  
M L Bayne ◽  
J Applebaum ◽  
D Underwood ◽  
G G Chicchi ◽  
B G Green ◽  
...  
Keyword(s):  
Growth Factor ◽  
Human Insulin ◽  
Affinity Binding ◽  
Insulin Like Growth Factor ◽  
High Affinity Binding ◽  
High Affinity ◽  
Igf I ◽  
Igf Receptor

scholarly journals Insulin-like growth factor (IGF) receptor, IGF-I, interleukin-1 beta (IL-1 beta), and IL-6 mRNA expression in osteoarthritic and normal human cartilage.

1996 ◽  
Vol 44 (2) ◽  
pp. 133-141 ◽  
Author(s):  
J Middleton ◽  
A Manthey ◽  
J Tyler
Keyword(s):  
Extracellular Matrix ◽  
Growth Factor ◽  
Interleukin 1 ◽  
Insulin Like Growth Factor ◽  
Interleukin 1 Beta ◽  
Normal Cartilage ◽  
Igf I ◽  
Cartilage Cells ◽  
Igf Receptor

Insulin-like growth factor-I (IGF-I) stimulates the production of extracellular matrix by cartilage cells and this action is mediated through the Type 1 IGF receptor. Expression of the genes for the IGF receptor and for IGF-I was examined in normal and osteoarthritic (OA) human articular cartilage by in situ hybridization. RNA transcripts for Type 1 receptor were detected in all 73 tissue samples and in 80-100% of chondrocytes per section. Signal for the receptor was present in normal and OA cells, and the highest message levels were in the tissues exhibiting advanced pathology. Strong message signals in the cells of the more advanced lesions were also noted for IGF-I, whereas little or no IGF-I mRNA was detected in normal samples. Interleukin-1 beta (IL-1 beta) induces degradation of extracellular matrix by cartilage cells, and expression of this gene was examined with digoxygenin-labeled oligonucleotide probes. mRNA transcripts were detected in only one in five of the cartilage samples taken from OA joints. Unlike IGF-I, expression did not correlate with the degree of OA pathology and positive cells were demonstrated also in samples from young normal cartilage. IL-6 mRNA was present both in surface and deep cells of fibrillated OA cartilage, but no signal was evident in histologically normal cartilage from OA tissue or in normal young joints.

Characteristics of binding of insulin-like growth factor (IGF)-I and IGF-II analogues to the type 1 IGF receptor determined by BIAcore analysis

2002 ◽  
Vol 269 (3) ◽  
pp. 961-968 ◽  
Author(s):  
Briony E. Forbes ◽  
Perry J. Hartfield ◽  
Kerrie A. McNeil ◽  
Kathy H. Surinya ◽  
Steven J. Milner ◽  
...  
Keyword(s):  
Growth Factor ◽  
Insulin Like Growth Factor ◽  
Igf I ◽  
Igf Receptor

Insulin-like growth factor (IGF)-I A- and B-domain analogues with altered type 1 IGF and insulin receptor binding specificities

1996 ◽  
Vol 17 (3) ◽  
pp. 237-246 ◽  
Author(s):  
G K Shooter ◽  
B Magee ◽  
M A Soos ◽  
G L Francis ◽  
K Siddle ◽  
...  
Keyword(s):  
Growth Factor ◽  
Insulin Receptor ◽  
Receptor Binding ◽  
Insulin Like Growth Factor ◽  
Receptor Isoforms ◽  
Insulin Receptor Isoforms ◽  
Igf I ◽  
Igf Receptor ◽  
Specificity Of Binding

ABSTRACT Insulin-like growth factor-I (IGF-I) analogues were produced with the aim of identifying IGF-I residues that contribute to the specificity of binding to the type 1 IGF receptor as opposed to the insulin receptor. Receptor binding properties of a series of A- and B-domain analogues were compared using rat L6 myoblasts, soluble human IGF type 1 receptors and soluble human insulin receptor isoforms HIR-A (−Ex11) and HIR-B (+Ex11). IGF-I analogues, [Leu8] IGF-I and [Phe59] IGF-I, were shown to exhibit respectively, a 28- and 17-fold decrease in affinity for the HIR-A with only a 6- and 5-fold decrease in affinity for the human IGF type 1 receptor. In contrast, the analogue [His4] IGF-I was equipotent to IGF-I in binding to the soluble type 1 IGF receptor while showing 7-fold and 4-fold increases in HIR-A and HIR-B binding respectively. Furthermore, [Leu62] IGF-I was 8-fold less potent than IGF-I in soluble IGF type 1 receptor binding but only showed a 2-fold decrease in HIR-A and HIR-B binding. Our study supports the conclusion that the co-evolution of the IGF-I and insulin receptor/ligand systems has resulted in subtle structural differences in the A- and B-regions of each ligand important for defining receptor binding specificity.

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