Assessment of pregnancy-associated glycoprotein (PAG) concentrations in swamp buffalo samples from fetal and maternal origins by using interspecies antisera.
; ; et al
in Animal Science Journal (2012), 83(10), 683-689
Pregnancy-associated glycoproteins (PAG) constitute a large family of glycoproteins found in the outer placental epithelial cell layer of the placenta in Eutherian species. In ruminants, they are noted to ... [more ▼]
Pregnancy-associated glycoproteins (PAG) constitute a large family of glycoproteins found in the outer placental epithelial cell layer of the placenta in Eutherian species. In ruminants, they are noted to be structurally closely related among the different species. This study was designed to determine PAG concentrations in maternal and fetal plasma, allantoic and amniotic fluids in buffalo species. Antisera (AS) generated in rabbits against distinct PAG molecules were used in three RIA-PAG systems: RIA-1 (raised against bovine PAG67kDa; AS#497), RIA-2 (raised against caprine PAG55+62kDa; AS#706) or RIA-3 (raised against buffalo PAG; AS#859). Samples were collected at slaughterhouse (n = 67). PAG concentrations determined by RIA-2 gave significantly higher results in both allantoic and amniotic fluids (12.7 ± 2.1 ng/ml and 24.0 ± 7.3 ng/ml, respectively). Regarding maternal and fetal plasma, PAG concentrations obtained by RIA-2 (21.8 ± 2.4 ng/ml and 20.2 ± 2.5 ng/ml, respectively) and RIA-3 (25.0 ± 2.2 ng/mL and 21.9 ± 3.2 ng/ml, respectively) were higher than those obtained by RIA-1 (15.5 ± 1.4 ng/ml and 16.1 ± 1.8 ng/ml, respectively). The correlation among the three systems was very high. The study clearly reveals the ability of PAG-RIA systems to determine PAG concentration in swamp buffalo samples. [less ▲]Detailed reference viewed: 67 (7 ULg)
A novel messenger ribonucleic acid homologous to human MAGE-D is strongly expressed in rat Sertoli cells and weakly in Leydig cells and is regulated by follitropin, lutropin, and prolactin.
Hennuy, Benoît ; ; Cornet, Anne et al
in Endocrinology (2000), 141(10), 3821-31
We have cloned a novel complementary DNA whose expression was decreased in rat Sertoli cell cultures after treatment with FSH. This complementary DNA encodes a protein of 570 amino acids and shares 92 ... [more ▼]
We have cloned a novel complementary DNA whose expression was decreased in rat Sertoli cell cultures after treatment with FSH. This complementary DNA encodes a protein of 570 amino acids and shares 92% homology with the human MAGE-D protein. In contrast to other MAGE genes (A, B, or C), we have shown that MAGE-D expression was ubiquitous in healthy rat tissues. In the seminiferous tubules, the MAGE-D was expressed in Sertoli cells but not in germ cells as demonstrated by RT-PCR and in situ hybridization, whereas for the other MAGE genes, expression has been shown to be restricted to germ cells. Interestingly, MAGE-D was also detected for the first time in the female gonad by Northern blotting. In MLTC-1 cells (mouse Leydig tumor cell line-1), LH and PRL stimulated MAGE-D expression. Using hypophysectomized rats, it was confirmed that FSH decreased MAGE-D expression, whereas LH and PRL increased MAGE-D messenger RNA level in the whole testis most probably through a direct action on Leydig cells. As MAGE-D is present in both the seminiferous compartment and interstitium and hormonally regulated in each, it is possible that it has specific functions in each compartment during the development and the maintenance of the testis. [less ▲]Detailed reference viewed: 37 (6 ULg)