Human granulosa-luteal and cumulus cells express transforming growth factors-beta type 1 and type 2 mRNA

1992 ◽  
Vol 74 (2) ◽  
pp. 458-460 ◽  
Author(s):  
G. W. Mulheron
Keyword(s):  
Growth Factors ◽  
Cumulus Cells ◽  
Transforming Growth Factors

Human granulosa-luteal and cumulus cells express transforming growth factors-beta type 1 and type 2 mRNA.

1992 ◽  
Vol 74 (2) ◽  
pp. 458-460
Author(s):  
G W Mulheron ◽  
N L Bossert ◽  
J A Lapp ◽  
D K Walmer ◽  
D W Schomberg
Keyword(s):  
Growth Factors ◽  
Cumulus Cells ◽  
Transforming Growth Factors

scholarly journals Comparative binding of bovine, human and rat insulin-like growth factors to membrane receptors and to antibodies against human insulin-like growth factor-1

1986 ◽  
Vol 233 (1) ◽  
pp. 215-221 ◽  
Author(s):  
L C Read ◽  
F J Ballard ◽  
G L Francis ◽  
R C Baxter ◽  
C J Bagley ◽  
...  
Keyword(s):  
Growth Factors ◽  
Polyclonal Antiserum ◽  
Competitive Binding ◽  
Membrane Receptors ◽  
Binding Studies ◽  
Comparative Binding ◽  
Placental Membranes ◽  
Insulin Like Growth Factors

The immunological properties of human, bovine and rat insulin-like growth factors (IGF) and insulin were compared in competitive binding studies with Tr10 and NPA polyclonal antisera raised in rabbits against human IGF-1. Bovine IGF-1 was 11-19% as effective as human IGF-1 in competing for binding with 125I-labelled human IGF-1, whereas IGF-2 reacted poorly and insulin did not compete. Similar competitive binding curves were obtained with the mouse monoclonal anti-(human IGF-1) antibody 3D1, except that bovine IGF-1 showed a severalfold greater affinity for the monoclonal antibody than for either polyclonal antiserum. Membranes isolated from human placenta, sheep placenta and foetal-human liver were used as sources of cellular receptors. In human placental membranes, most of the binding of IGF-1 tracers could be attributed to a type-1 receptor, because insulin inhibited up to 65% of tracer binding. The other two tissues apparently contain only type-2 receptors, as evidenced by the very low potency of bovine or human IGF-1 in competing for binding with IGF-2 tracers and the absence of any competition by insulin. In competition for binding with labelled bovine or human IGF-1 to human placental membranes, bovine IGF-1 had a similar potency to human IGF-1, whereas bovine IGF-1 was more potent in binding studies with tissues rich in type-2 receptors. Rat IGF-2 was considerably less effective than human IGF-2 in competition for receptors on any of the membrane preparations.

scholarly journals Specific binding of insulin-like growth factors 1 and 2 to the type 1 and type 2 receptors respectively

1988 ◽  
Vol 249 (3) ◽  
pp. 721-726 ◽  
Author(s):  
F J Ballard ◽  
M Ross ◽  
F M Upton ◽  
G L Francis
Keyword(s):  
Growth Factors ◽  
Specific Binding ◽  
Protein A ◽  
Cell Types ◽  
Bovine Insulin ◽  
Lung Fibroblasts ◽  
Ligand Interactions ◽  
Insulin Like Growth Factors

1. Competitive binding and receptor cross-linking experiments have been used to examine the receptor-ligand interactions between three bovine insulin-like growth factors (IGF) and monolayer cultures of myoblasts and fibroblasts. 2. Labelled IGF-2 bound predominantly to the type 2 receptor with negligible label cross-linked to the type 1 receptor, notwithstanding the ability of IGF-2 to compete effectively for the binding of IGF-1 to the type 1 receptor. Approx. 100-fold higher concentrations of IGF-1 or the N-terminal truncated (des-Gly-Pro-Glu) IGF-1 (-3N:IGF-1) were required to produce competition equivalent to IGF-2. 3. All IGF peptides, but especially IGF-1, enhanced the binding of labelled IGF-2 to the type 2 receptor of lung fibroblasts. This unusual effect was probably a consequence of the displacement of labelled IGF-2 otherwise bound to a medium protein, a conclusion supported by the demonstration of a 38 kDa membrane protein cross-linked to labelled IGF-2. 4. Both IGF-1 and -3N:IGF-1 bound only to the type 1 IGF receptor in L6 myoblasts, rat vascular smooth-muscle cells and human lung fibroblasts. The peptides competed for labelled IGF-1 binding with potencies in the order -3N:IGF-1 greater than IGF-1 greater than IGF-2 much greater than insulin. Since the IGF peptides were equipotent in skin fibroblasts, it was proposed that the apparently higher affinity of -3N:IGF-1 for receptors in the other cell types was instead a consequence of a low affinity of this peptide for the competing 38 kDa binding protein.

Insulin-like growth factors and the multiplication of Tera-2, a human teratoma-derived cell line

1988 ◽  
Vol 90 (3) ◽  
pp. 475-484
Author(s):  
C. Biddle ◽  
C.H. Li ◽  
P.N. Schofield ◽  
V.E. Tate ◽  
B. Hopkins ◽  
...  
Keyword(s):  
Growth Factors ◽  
Cell Line ◽  
Serum Free Medium ◽  
Free Medium ◽  
Maximal Stimulation ◽  
Igf Receptors ◽  
Igf I ◽  
Insulin Like Growth Factors

A human teratoma cell line (Tera-2) was grown in serum-free medium, and the population multiplication was stimulated by the addition of somatomedins/insulin-like growth factors (IGFs). Both IGF-I and IGF-II gave maximal stimulation when added daily at 10 ng ml-1. The IGFs did not substantially change the labelling index of the cells, and the IGFs appeared to exert their effect on population multiplication by increasing cell survival. Membranes isolated from Tera-2 cells displayed both type 1 and type 2 IGF receptors.

scholarly journals Glucocorticoid metabolism in the bovine cumulus–oocyte complex matured in vitro

Reproduction ◽  
2016 ◽  
Vol 151 (1) ◽  
pp. 73-82 ◽  
Author(s):  
Masafumi Tetsuka ◽  
Ryo Takagi ◽  
Nobuhiro Ambo ◽  
Thet Su Myat ◽  
Yuta Zempo ◽  
...  
Keyword(s):  
Subsequent Development ◽  
Cumulus Cells ◽  
Cumulus Oocyte Complex ◽  
Target Organs ◽  
Glucocorticoid Metabolism ◽  
Glucocorticoid Action ◽  
Expression And Activity

Glucocorticoid action in target organs is regulated by relative activities of 11β-HSD type 1 (HSD11B1) that mainly converts cortisone to active cortisol and type 2 (HSD11B2) that inactivates cortisol to cortisone. HSD11Bs have been shown to be expressed in the ovary of various species. However, little is known about the expression and activity of HSD11Bs in the bovine cumulus–oocyte complex (COC). In the present study, we investigated the expression and activities of HSD11Bs in in vitro-matured (IVM) bovine COCs. Bovine COCs were matured in M199 supplemented with or without FSH and FCS. The expression of HSD11B1 and HSD11B2 was measured by using quantitative RT-PCR in denuded oocytes (DO) and cumulus cells (CC). Reductive and oxidative activities of HSD11Bs were determined by radiometric conversion assay using labeled cortisol, cortisone or dexamethasone in intact COCs, DO or CC in the presence or absence of 11-keto-progesterone (11kP), a selective inhibitor of HSD11B2. The presence of HSD11Bs in the oocyte was examined by immunofluorescence microscopy. Oocytes exclusively expressed HSD11B2 and its expression and activity were largely unchanged during IVM. CC, on the other hand, exclusively expressed HSD11B1 and its expression and activity were upregulated as IVM progressed. As a result, the net glucocorticoid metabolism shifted from inactivation to activation towards the end of IVM. These results indicate that the bovine COC is capable of modulating local glucocorticoid concentration and, by doing so, may create an environment that is favorable to ovulating oocyte for maturation, fertilization and subsequent development.

scholarly journals Binding properties and biological potencies of insulin-like growth factors in L6 myoblasts

1986 ◽  
Vol 233 (1) ◽  
pp. 223-230 ◽  
Author(s):  
F J Ballard ◽  
L C Read ◽  
G L Francis ◽  
C J Bagley ◽  
J C Wallace
Keyword(s):  
Protein Synthesis ◽  
Growth Factors ◽  
Radioligand Binding ◽  
Cross Linking ◽  
Protein Accumulation ◽  
Igf Receptor ◽  
H Protein ◽  
Insulin Like Growth Factors

Protein synthesis in rat L6 myoblasts is stimulated and protein breakdown inhibited in a co-ordinate manner by insulin-like growth factors (IGF) or insulin. For both processes, bovine IGF-1 was somewhat more potent than human IGF-1, which was effective at a tenth the concentration of insulin, rat IGF-2 or human IGF-2. A similar order of potency is noted when DNA synthesis or protein accumulation is monitored over a 24 h period, but between 20- and 50-fold higher concentrations of each growth factor are required than those needed to produce effects in the 4 h protein-synthesis or -breakdown measurements. Binding experiments with labelled human or bovine IGF-1 as ligand demonstrated competition at concentrations of IGF-2, especially human IGF-2, lower than that of either IGF-1 preparation. This pattern was much more pronounced when the radioligand was either human IGF-2 or rat IGF-2. Insulin competed 10-15% for the binding of labelled IGF-1, but not at all with labelled IGF-2. Ligand-receptor cross-linking experiments showed that labelled bovine IGF-1 bound approximately equally to the type 1 IGF receptor (Mr 130000 after reduction) and to the type 2 IGF receptor (Mr 270000 after reduction), and that unlabelled IGF-1 competed equally with radioligand binding to both receptors. On the other hand, rat IGF-2 competed more effectively for binding to the type-2 receptor, and insulin competed only for binding to the type-1 receptor. Further cross-linking experiments with rat IGF-2 as radioligand demonstrated binding only to the type-2 receptor and to proteins with Mr values after reduction of 230000 and 200000. This binding was prevented by high rat IGF-2 concentrations, less effectively by bovine IGF-1 and not at all by insulin. The apparently conflicting biological potencies and receptor binding of the different growth factors can be explained if all the biological actions are mediated via the type-1 IGF receptor, rather than through the abundant type-2 receptor.

Periovulatory human oocytes, cumulus cells, and ovarian leukocytes express type 1 but not type 2 11β-hydroxysteroid dehydrogenase RNA

2000 ◽  
Vol 73 (4) ◽  
pp. 825-830 ◽  
Author(s):  
Michael P Smith ◽  
Raj S Mathur ◽  
Stephen D Keay ◽  
Len Hall ◽  
Michael G.R Hull ◽  
...  
Keyword(s):  
Cumulus Cells ◽  
Hydroxysteroid Dehydrogenase ◽  
Human Oocytes
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