Hyaluronan in follicular fluids and fertilization of oocytes

2000 ◽  
Vol 74 (6) ◽  
pp. 1148-1152 ◽  
Author(s):  
Hidekazu Saito ◽  
Tomoko Kaneko ◽  
Toshifumi Takahashi ◽  
Satoshi Kawachiya ◽  
Takakazu Saito ◽  
...  
Keyword(s):  
Zygote ◽  
2008 ◽  
Vol 16 (3) ◽  
pp. 239-247 ◽  
Author(s):  
T. Metoki ◽  
H. Iwata ◽  
M. Itoh ◽  
M. Kasai ◽  
A. Takajyo ◽  
...  

SummaryWe examined the effect of supplementing the culture medium with follicular fluid (FF) on the growth of porcine preantral follicles and oocytes. Firstly, preantral follicles were retrieved from ovaries and then FF was collected from all antral follicles that were 2–7 mm in diameter (AFF), which included large follicles of 4–7 mm in diameter (LFF) and small follicles of 2–3 mm in diameter (SFF). When preantral follicles with a diameter of 250 μm were cultured in medium containing AFF, the growth of follicles and oocytes was greater than when follicles were cultured in medium containing fetal calf serum (FCS). When this growth-promoting effect in AFF was compared for LFF and SFF, the LFF were shown to be significantly more effective than SFF. This LFF effect was lost, however, when the concentration of LFF in the medium was decreased from 5% to 0.5% or when LFF were heat treated (60 °C for 30 min) or trypsin was added. In contrast, a decrease in SFF concentration from 5% to 0.5% and heat treatment of the SFF enhanced preantral follicle growth. Furthermore, proteins obtained from LFF that had molecular weights greater than 10 kDa (LFF > 10 kDa) had similar, but relatively reduced, growth-promoting properties. The remaining three LFF protein fractions (<10 kDa or <100 kDa or >100 kDa), however, did not have these growth-promoting properties. In conclusion, the supplementation of medium with LFF, rather than serum, enhanced preantral follicle and oocyte growth. Factors that enhanced follicle development in LFF and factors that suppressed follicle development in SFF were proteins and these LFF factors ranged in size from 10 kDa to over 100 kDa.


1990 ◽  
Vol 7 (1) ◽  
pp. 22-27
Author(s):  
David W. Richards ◽  
Patrick Quinn ◽  
Bronte A. Stone ◽  
Richard P. Marrs

1993 ◽  
Vol 8 (5) ◽  
pp. 674-677 ◽  
Author(s):  
S. Kamada ◽  
T. Kubota ◽  
M. Taguchi ◽  
T. Aso

2003 ◽  
Vol 3 (1) ◽  
pp. 27-31 ◽  
Author(s):  
F. Kawasaki ◽  
Y. Kawano ◽  
Z. Kosay Hasan ◽  
H. Narahara ◽  
I. Miyakawa

1993 ◽  
Vol 128 (1) ◽  
pp. 88-94 ◽  
Author(s):  
Nobuyoshi Kokawa ◽  
Mareo Yamoto ◽  
Kenichi Furukawa ◽  
Ryosuke Nakano

We performed partial purification of low molecular weight luteinizing hormone binding inhibitor from porcine follicular fluids and examined its biological activities. Following ultrafiltration, gel filtration and anion exchange of the pooled porcine follicular fluids, low molecular weight fractions (500–10,000 MW) inhibited [125I]hLH binding to porcine granulosa cells in a dose-dependent manner. The binding inhibition kinetics study revealed that the luteinizing hormone binding inhibitor may indicate a non-competitive inhibition with [125I]hLH binding. In vitro bioassay using adult mouse testicular interstitial cells revealed that the partially purified luteinizing hormone binding inhibitor reduced ovine LH-stimulated testosterone and cAMP production in a dose-dependent manner, whereas the luteinizing hormone binding inhibitor did not affect basal production of testosterone and cAMP. The inhibitory activity was heat stable and did not disappear with activated charcoal adsorption. The results of the present study suggest that the luteinizing hormone binding inhibitor may play an important role as an ovarian non-steroidal regulator modulating the receptor binding of LH and LH-mediated steroidogenesis.


1999 ◽  
Vol 14 (Suppl_3) ◽  
pp. 173-174
Author(s):  
N. Thomas ◽  
R. Goodacre ◽  
É.M. Timmins ◽  
P. Mitchell ◽  
M. Jamieson ◽  
...  

1991 ◽  
Vol 3 (6) ◽  
pp. 659 ◽  
Author(s):  
T O'Shea ◽  
CM Andrews ◽  
BM Bindon ◽  
MA Hillard ◽  
K Miyamoto ◽  
...  

Ewes were immunized with either a synthetic peptide (peptide 1-32) that has an amino acid sequence identity with the first 32 amino acids at the amino terminal of the alpha-subunit of porcine inhibin, or with bovine or porcine monoclonal antibody purified inhibin (bMPI and pMPI respectively), obtained by immunochromatography from follicular fluids. The peptide 1-32 was conjugated to albumin before use. Peptide 1-32 and bMPI increased ovulation rate and number of follicles (greater than or equal to 5 mm diameter). Although bMPI increased plasma FSH concentration the peptide did not. pMPI had no effect on ovarian activity but markedly elevated both plasma FSH and LH concentrations. The plasma LH concentration was lowered in ewes immunized with peptide 1-32. It appears, therefore, that ovulation rate can be increased following increased plasma FSH concentrations at luteolysis or in the absence of such an increase. Conversely, greatly increased plasma gonadotrophin concentrations at luteolysis (pMPI) were not followed by an increase in ovulation rate. Antibodies in the plasma of ewes immunized with peptide 1-32 and bMPI bound to iodinated synthetic human inhibin alpha-chain 6-30 peptide. The results suggest that ovulation rate is at least partly determined by intraovarian factors.


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