References of "Melo de Sousa, Noelita"
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See detailUnknown placental glycoprotein K-76 kDa [Fragment] from Bison bonasus placenta - Access number P85330
Kiewisz, J.; Melo de Sousa, Noelita ULg; Beckers, Jean-François ULg et al

E-print/Working paper (2008)

N-terminal microsequence obtained after purification and characterization of placental proteins in Bison bonasus. Proteins were submitted to SwissProt databank.

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See detailUnknown placental glycoprotein J2-45 kDa [Fragment] from Bison bonasus placenta - Access number P85329
Kiewisz, J.; Melo de Sousa, Noelita ULg; Beckers, Jean-François ULg et al

E-print/Working paper (2008)

N-terminal microsequence obtained after purification and characterization of placental proteins in Bison bonasus. Proteins were submitted to SwissProt databank.

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See detailUnknown placental glycoprotein J1-45 kDa [Fragment] from Bison bonasus placenta - P85328
Kiewisz, J.; Melo de Sousa, Noelita ULg; Beckers, Jean-François ULg et al

E-print/Working paper (2008)

N-terminal microsequence obtained after purification and characterization of placental proteins in Bison bonasus. Proteins were submitted to SwissProt databank.

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See detailPregnancy-Associated Glycoprotein I-50 kDa [Fragment] from Bison bonasus placenta - Access number P85327
Kiewisz, J.; Melo de Sousa, Noelita ULg; Beckers, Jean-François ULg et al

E-print/Working paper (2008)

N-terminal microsequence obtained after purification and characterization of placental proteins in Bison bonasus. Proteins were submitted to SwissProt databank.

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See detailPregnancy-Associated Glycoprotein H-60 kDa [Fragment] from Bison bonasus placenta - Access number P85326
Kiewisz, J.; Melo de Sousa, Noelita ULg; Beckers, Jean-François ULg et al

E-print/Working paper (2008)

N-terminal microsequence obtained after purification and characterization of placental proteins in Bison bonasus. Proteins were submitted to SwissProt databank.

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See detailPregnancy-Associated Glycoprotein G-71 kDa [Fragment] from Bison bonasus placenta - Access number P85325
Kiewisz, J.; Melo de Sousa, Noelita ULg; Beckers, Jean-François ULg et al

E-print/Working paper (2008)

N-terminal microsequence obtained after purification and characterization of placental proteins in Bison bonasus. Proteins were submitted to SwissProt databank.

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See detailPregnancy-Associated Glycoprotein F-50 kDa [Fragment] from Bison bonasus placenta - Access number P85324
Kiewisz, J.; Melo de Sousa, Noelita ULg; Beckers, Jean-François ULg et al

E-print/Working paper (2008)

N-terminal microsequence obtained after purification and characterization of placental proteins in Bison bonasus. Proteins were submitted to SwissProt databank.

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See detailPregnancy-Associated Glycoprotein E-55 kDa [Fragment] from Bison bonasus placenta - Access number P85323
Kiewisz, J.; Melo de Sousa, Noelita ULg; Beckers, Jean-François ULg et al

E-print/Working paper (2008)

N-terminal microsequence obtained after purification and characterization of placental proteins in Bison bonasus. Proteins were submitted to SwissProt databank.

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See detailPregnancy-Associated Glycoprotein C-50 kDa [Fragment] from Bison bonasus placenta - Access number P85322
Kiewisz, J.; Melo de Sousa, Noelita ULg; Beckers, Jean-François ULg et al

E-print/Working paper (2008)

N-terminal microsequence obtained after purification and characterization of placental proteins in Bison bonasus. Proteins were submitted to SwissProt databank.

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See detailPregnancy-Associated Glycoprotein C-50 kDa [Fragment] from Bison bonasus placenta - Access number P85321
Kiewisz, J.; Melo de Sousa, Noelita ULg; Beckers, Jean-François ULg et al

E-print/Working paper (2008)

N-terminal microsequence obtained after purification and characterization of placental proteins in Bison bonasus. Proteins were submitted to SwissProt databank.

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See detailPregnancy-Associated Glycoprotein B-55 kDa [Fragment] from Bison bonasus placenta - Access number P85320
Kiewisz, J.; Melo de Sousa, Noelita ULg; Beckers, Jean-François ULg et al

E-print/Working paper (2008)

N-terminal microsequence obtained after purification and characterization of placental proteins in Bison bonasus. Proteins were submitted to SwissProt databank.

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See detailPregnancy-Associated Glycoprotein A-67 kDa [Fragment] from Bison bonasus placenta - Access number P85319
Kiewisz, J.; Melo de Sousa, Noelita ULg; Beckers, Jean-François ULg et al

E-print/Working paper (2008)

N-terminal microsequence obtained after purification and characterization of placental proteins in Bison bonasus. Proteins were submitted to SwissProt databank.

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See detailPregnancy diagnosis in ruminant species.
Melo de Sousa, Noelita ULg; Szenci, O.; Taverne, M. A. M. et al

in Reproduction in Domestic Animals (2008), 43(Suppl 5), 104

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See detailEffect of different treatment protocols on ovulation and pregnancy rate in dairy cattle.
Repasy, A.; Melo de Sousa, Noelita ULg; Beckers, Jean-François ULg et al

in Magyar Allatorvosok Lapja = Hungarian Veterinary Journal (2008), (Suppl II), 314

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See detailDetermination of PAG in the milk and blood in cow’s in comparison to other examination methods for pregnancy diagnosis.
Gajewski, Z.; Melo de Sousa, Noelita ULg; Konopka, A. A. et al

in Magyar Allatorvosok Lapja = Hungarian Veterinary Journal (2008), (Suppl II), 190

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See detailNative and recombinant bovine placental lactogens.
Alvarez Oxiley, Andrea Vivian ULg; Melo de Sousa, Noelita ULg; Beckers, Jean-François ULg

in Reproductive Biology (2008), 8(2), 85-106

The bovine placenta produces a wide variety of proteins that are structurally and functionally similar to the pituitary proteins from the GH/PRL gene family. Bovine placental lactogen (bPL) is a 200-amino ... [more ▼]

The bovine placenta produces a wide variety of proteins that are structurally and functionally similar to the pituitary proteins from the GH/PRL gene family. Bovine placental lactogen (bPL) is a 200-amino acid long glycoprotein hormone that exhibits both lactogenic and somatogenic properties. The apparent molecular masses of purified native (n) bPL molecules (31-33 kDa) exceed 23 041 Da, which is the theoretical molecular mass of the protein core. At least six isoelectric variants (pI: 4.85-6.3) of bPL were described in cotyledonary extracts and three different bPL isoforms (pI: 4.85-5.25) were found in fetal sera. The bPL molecules that are detected in higher concentrations in peripheral circulation exhibit a more acidic pI than those present in placental homogenates. This may reflect an important glycosylation process occurring just prior to the bPL secretion. The bPL mRNA is transcribed in trophectoderm binucleate cells starting from Day 30 of pregnancy until the end of gestation. In mothers, bPL is involved in the regulation of ovarian function, mammogenesis, lactogenesis, and pregnancy stage-dependent adaptation of nutrient supplies to the fetus. Due to the higher fetal, compared to maternal concentrations of circulating hormone, it has been suggested that bPL primarily targets fetal tissues. [less ▲]

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See detailConcentration of bovine pregnancy associated glycoprotein in plasma and milk: its application for pregnancy diagnosis in cows
Gajewski, Z.; Melo de Sousa, Noelita ULg; Beckers, Jean-François ULg et al

in Journal of Physiology and Pharmacology : an Official Journal of the Polish Physiological Society (2008), 59(Suppl 9), 55-64

Pregnancy diagnosis is an important part in reproduction management of ruminants. The aim of the study was to use a new method for evaluating the bPAG and cPAG in milk and blood bPAG and compare this ... [more ▼]

Pregnancy diagnosis is an important part in reproduction management of ruminants. The aim of the study was to use a new method for evaluating the bPAG and cPAG in milk and blood bPAG and compare this results with the other method for pregnancy diagnosis in the cows. The study was carried out in 220 Holstein Frisian cows. Heparinised blood samples were taken from the jugular vein and stored at -20 degrees C until PAG assay by RIA. For bPAG and cPAG, RIA test, milk samples were homogenized. Pure bPAG was used as a standard tracer described by Zoli et al. (1992). The cows were diagnosed as pregnant by means of USG (Aloka SSD 210) and by rectal palpation. bPAG and cPAG concentration in milk increased after 28 day of pregnancy and showed the rapid increase near the parturition. The same results of bPAG concentration we obtained in the blood samples. The decline of bPAG concentration was faster in the milk than in the blood. The data showed that the RIA method is precise enough to measure PAG concentrations in the maternal blood and milk of cows. The data indicate that milk samples can be used for pregnancy diagnosis in cows. The sensitivity and specificity of RIA measurement of PAG are very high. [less ▲]

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See detailIdentification of multiple pregnancy-associated glycoproteins (PAGs) purified from the European bison (Eb; Bison bonasus L.) placentas.
Kiewisz, J.; Melo de Sousa, Noelita ULg; Beckers, Jean-François ULg et al

in Animal Reproduction Science (2008), 112

This paper describes the first identified chorionic PAGs in the European bison (Eb), named EbPAGs, predominantly expressed during early and mid-pregnancy (45-120 day post-coitum; dpc). Many EbPAGs were ... [more ▼]

This paper describes the first identified chorionic PAGs in the European bison (Eb), named EbPAGs, predominantly expressed during early and mid-pregnancy (45-120 day post-coitum; dpc). Many EbPAGs were extracted from various cotyledonary tissues, precipitated, chromatographed (DEAE and VVA: Vicia villosa agglutinin), electrophoresed (1D- and 2D-PAGE), analysed by heterologous (cross-species) Western blotting and then micro-sequenced by Edman degradation. Finally, twelve selected VVA-purified isoforms (Ip 3.7-7.4) were entirely characterised. Nine identified NH(2)-terminal micro-sequences were found to be PAGs. On 45dpc, three identified forms were named: EbPAG(67AkDa) (RGSNLTHPLRNIGDLFYVGN), EbPAG(55BkDa) (RGSNLTHPL) and EbPAG(50CkDa) (SQISLRGSNLTI). On 60dpc, the next three forms were named: EbPAG(71DkDa) (RGSNLTIHPLRNIIDLFYVG), EbPAG(55EkDa) (RGSNLTHPLRNI) and EbPAG(50FkDa) (SQISLRGS). On 120dpc, three other forms were named: EbPAG(71GkDa) (RGSNLTHPLRNIRDLFYVG), EbPAG(60HkDa) (RGSNLTTHPLRNIKDLVVYM) and EbPAG(50IkDa) (SGSNLTTV). These EbPAG ((A-I)) sequences are unique, as they are not identical to any other PAGs purified previously in related species of the Bovidae family. However, the EbPAGs (A-I forms) have some sequence resemblance to internal sequences of various full-length polypeptide PAG precursors (in silico translated from cloned cDNAs) identified in domestic cattle. Three other novel native isoforms (J1, J2 and K): EbUPG(45kDa) J1 (SKDNYKNYIPLIVPFAT), EbUPG(45kDa) J2 (SKDNQKNYIPLIVPFAT) and EbUPG(76kDa) K (SPEFTV), were temporarily named 'unknown placental glycoproteins' (UPGs), due to their efficient VVA-purification (specific for glycoproteins only) and a lack of considerable consensus to previously sequenced placental glycoproteins in the Bovidae family. This is the first study identifying NH(2)-terminals of multiple/diverse EbPAGs and some EbUPGs purified from the synepitheliochorial cotyledonary placenta of the endangered Bison bonasus (Red list) [less ▲]

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See detailFactors affecting plasma progesterone in the early fetal period in high producing dairy cows.
Bech-Sabat, G.; Lopez-Gatius, F.; Yaniz, J. L. et al

in Theriogenology (2008), 69(4), 426-32

The aim of the present study was to determine whether certain animal- or management related factors could affect plasma progesterone concentrations on Day 42 of gestation in high producing dairy cows ... [more ▼]

The aim of the present study was to determine whether certain animal- or management related factors could affect plasma progesterone concentrations on Day 42 of gestation in high producing dairy cows. Factors affecting early fetal loss were also analyzed. The study population was comprised of 199 pregnant cows classified as having high (> or =9 ng/ml) or low (<9 ng/ml) plasma progesterone concentrations. Through logistic regression procedures it was determined that, based on the odds ratio, cows with two or more corpora lutea were three times more likely to have high progesterone concentrations than cows with a single corpus luteum. Low producing cows during the warm season were 2.86 times more likely to have high progesterone concentrations than the remaining cows. Primiparous cows with high concentrations (>4 ng/ml) of pregnancy associated glycoprotein-1 (PAG-1) were 2.73 times more likely to have high progesterone concentrations than the remaining cows. Of the 199 pregnancies, 25 (12.6%) suffered early fetal loss: 22/136 (16.2%) during the warm season and 3/63 (4.8%) during the cool season, all in cows without additional corpora lutea. Based upon the odds ratio, cows without an additional corpus luteum were 3.67 times more likely to suffer fetal loss during the warm season than during the cool season. Our results indicate that milk production, the presence of two or more corpora lutea and plasma PAG-1 concentrations can affect plasma progesterone concentrations at the onset of the fetal period. The presence of an additional corpus luteum strongly diminished the risk of early fetal loss during the warm period. [less ▲]

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See detailIsolation of new pregnancy-associated glycoproteins from water buffalo (Bubalus bubalis) placenta by Vicia villosa affinity chromatography.
Barbato, O.; Melo de Sousa, Noelita ULg; Klisch, K. et al

in Research in Veterinary Science (2008), 85(3), 457-66

The present study describes the isolation and characterization of new pregnancy-associated glycoprotein molecules (PAG) from midpregnancy and late-pregnancy placentas in the water buffalo (Bubalus bubalis ... [more ▼]

The present study describes the isolation and characterization of new pregnancy-associated glycoprotein molecules (PAG) from midpregnancy and late-pregnancy placentas in the water buffalo (Bubalus bubalis). After extraction, the homogenates are subjected to acid and ammonium sulfate precipitations followed by DEAE chromatography. Subsequently, the water buffalo PAG (wbPAG) from these solutions are enriched by Vicia villosa agarose (VVA) affinity chromatography. As determined by western blotting with anti-PAG sera, the apparent molecular masses of the immunoreactive bands from the VVA peaks range from 59.5 to 75.8kDa and from 57.8 to 73.3kDa in the midpregnancy and late-pregnancy placentas, respectively. Amino-terminal microsequencing of the immunoreactive proteins has allowed the identification of three distinct wbPAG sequences, which have been deposited in the SwissProt database: RGSXLTIHPLRNIRDFFYVG (acc. no. P85048), RGSXLTILPLRNIID (acc. no. P85049), and RGSXLTHLPLRNI (acc. no. P85050). Their comparison to previously identified proteins has shown that two of them are new because they have not been described before. Our results confirm the suitability of VVA chromatography for the enrichment of the multiple PAG molecules expressed in buffalo placenta. [less ▲]

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