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1.
Front Physiol ; 13: 1012212, 2022.
Artigo em Inglês | MEDLINE | ID: mdl-36176771

RESUMO

Embryo mortality rate, which can reach up to 40% in avian species, is a major issue for breeding. It is therefore important to identify new embryo development biomarkers for genetic selection to improve reproductive performances. We have recently shown that chemerin is expressed in the oviductal hen magnum, accumulates in egg white, is correlated with embryo survival and could thus be used as a molecular marker of embryo development. Eggs from seven hen breeds (n = 70) were collected during five successive days at the end of the laying period. After weighing eggs, yolk and albumen, an egg white sample from each egg was collected and a blood sample was taken from each hen. Chemerin concentrations in albumen and blood samples were measured by a specific home made ELISA assay. Hen's plasma and egg's albumen chemerin levels were found to be correlated with reproductive parameters such as fecundity, fertility, embryo mortality, hatchability and laying rates. The inter-hen chemerin level variability in albumen was higher than intra-hen except for one breed (R+). We observed significantly different levels of chemerin in egg white between breeds. However, chemerin concentrations in egg white were not significantly associated to variations of hen plasma chemerin levels. Interestingly, we observed negative correlations between albumen chemerin concentrations and egg weight (r = -0.43, p = 0.001), between albumen weight (r = -0.40, p = 0.002), and between yolk weight (r = -0.28, p = 0.03). We also showed negative correlations between egg white chemerin concentrations and fecundity (r = -0.32, p = 0.011) and fertility (r = -0.27, p = 0.04) whereas no significant correlation was observed with the laying rate. Taken together, these results suggest that egg white chemerin concentration might be a good biomarker for genetic selection for egg weight and fertility in hens, provided these data are confirmed on a larger scale.

2.
Poult Sci ; 101(11): 102142, 2022 Nov.
Artigo em Inglês | MEDLINE | ID: mdl-36167019

RESUMO

Two divergently selected broiler lines were created by selection for low (pHu-) or high (pHu+) Pectoralis major ultimate pH (pHu) in order to better understand the molecular mechanisms underlying meat quality traits in broilers and are also unique genetic resources reflecting low and high glycogen levels in chicken muscle. The present study aimed to reveal the correlated phenotypical changes of egg quality traits in broiler breeders from the 2 divergent lines at the 14th generation. Birds were reared on littered floor system until 18 wk of age and in individual cages up to 42 wk. Individual egg production was recorded daily from age at first egg to 42 wk. External (egg weight: EW and shape index: SI), internal (albumen height: AH, Haugh unit: HU, yolk index: YI, and yolk color: YC), and shell (shell percentage: ESP, thickness: EST and strength: ESS) characteristics of eggs in pHu- and pHu+ lines were measured in all eggs for 4 consecutive days at 26, 27, 28, 30, 31, 32, 41, and 42 wk of age. The pHu- line had significantly higher egg percentage than pHu+ (55.9 and 49.1%, respectively). The EW in pHu- line (57.2 g) was significantly lower than in pHu+ (59.0 g) and increased with age in both lines. The mean ESP, EST and ESS were lower in the pHu+ eggs compared to the pHu- line. ESP and EST decreased mainly from 26 to 27 wk of age and they had a stable trend with advancing age in the remaining weeks. AH and YI were lower in pHu- line eggs than in pHu+. YC was more intense and HU higher in pHu+ eggs than pHu- in pre-peak and peak laying period. In conclusion, these results showed that a divergent selection for muscle energy metabolism has led to correlated responses on internal and external egg quality traits and suggest that the production of good-quality eggs may be impaired in broiler breeders with low energy reserves.


Assuntos
Galinhas , Músculos Peitorais , Animais , Galinhas/genética , Óvulo , Carne/análise , Concentração de Íons de Hidrogênio , Ovos
3.
Reproduction ; 150(1): 53-63, 2015 Jul.
Artigo em Inglês | MEDLINE | ID: mdl-25918435

RESUMO

In mammals, nicotinamide phosphoribosyltransferase (NAMPT) is an adipokine produced by adipose tissue that is found in intracellular and extracellular compartments. The intracellular form of NAMPT is a nicotinamide phosphoribosyltransferase, whereas the extracellular form is considered an adipokine. In humans, NAMPT regulates energy metabolism and reproductive functions, such as ovarian steroidogenesis. To date, no study has investigated the role of NAMPT in hen ovaries. We investigated whether NAMPT is present in hen ovarian follicles and its role in granulosa cells. Using RT-PCR, western blotting and immunocytochemistry, we detected mRNA transcripts and proteins related to NAMPT in theca and granulosa cells from pre-ovulatory follicles. Using RT-PCR, we demonstrated that mRNA NAMPT levels were higher in granulosa cells than they were in theca cells and that during follicle development, theca cell levels decreased, whereas levels remained unchanged in granulosa cells. NAMPT protein quantities were significantly higher in theca cells than they were in granulosa cells, but they were unchanged during follicular development. Plasma NAMPT levels, as determined by ELISA and immunoblotting, were significantly lower in adult hens than they were in juveniles. In vitro, treatment with human recombinant NAMPT (100 ng/ml, 48 h) halved basal and IGF1-induced progesterone secretion, and this was associated with a reduction in STAR and HSD3B protein levels and MAPK3/1 phosphorylation levels in granulosa cells. These effects were abolished by the addition of FK866, a specific inhibitor of NAMPT enzymatic activity. Moreover, NAMPT had no effect on granulosa cell proliferation. In conclusion, NAMPT is present in hen ovarian cells and inhibits progesterone production in granulosa cells.


Assuntos
Células da Granulosa/metabolismo , Nicotinamida Fosforribosiltransferase/metabolismo , Progesterona/metabolismo , Acrilamidas/farmacologia , Animais , Galinhas , Feminino , Células da Granulosa/efeitos dos fármacos , Fator de Crescimento Insulin-Like I/farmacologia , Complexos Multienzimáticos/metabolismo , Nicotinamida Fosforribosiltransferase/farmacologia , Fosfoproteínas/metabolismo , Fosforilação , Piperidinas/farmacologia , Progesterona Redutase/metabolismo , Transdução de Sinais/efeitos dos fármacos , Esteroide Isomerases/metabolismo , Células Tecais/efeitos dos fármacos , Células Tecais/metabolismo
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