Isolation and partial characterization of three pregnancy-associated glycoproteins from the ewe placenta

• Published in: Molecular reproduction and development Vol. 64; no. 2; pp. 199 - 206
• Main Authors: El Amiri, Bouchra, Remy, Benoit, Sousa, Noelita Melo, Joris, Bernard, Ottiers, Nicole Gerardin, Perenyi, Zsolt, Mboko, Henri Banga, Beckers, Jean-Francois
• Format: Journal Article Web Resource
• Language: English
• Published: New York Wiley Subscription Services, Inc., A Wiley Company 01-02-2003; Wiley-Liss; Wiley Liss, Inc
• Subjects: Animals; binucleate cell; Biological and medical sciences; Female; Fundamental and applied biological sciences. Psychology; Glycoproteins - isolation & purification; Glycoproteins - metabolism; Life sciences; Mother. Fetoplacental unit. Mammary gland. Milk; Médecine vétérinaire & santé animale; N-terminal microsequencing; Placenta - metabolism; Pregnancy; Pregnancy Proteins - isolation & purification; Pregnancy Proteins - metabolism; Pregnancy. Parturition. Lactation; Sciences du vivant; Sequence Analysis, Protein; Sheep; trophoblast; Vertebrates: reproduction; Veterinary medicine & animal health; Trophoblaste; Fetal membrane; N-terminal microsequencing; binucleate cell; Pregnancy; Vertebrata; Ewe; Mammalia; Placenta; Isoelectric point; Sheep; Female; Artiodactyla; trophoblast; Molecular mass; Pregnancy specific glycoprotein; Ungulata; Aminoacid sequence
• ISSN: 1040-452X; 1098-2795; 1098-2795
• DOI: 10.1002/mrd.10246

Pregnancy‐associated glycoproteins (PAGs) are synthesized in the outer epithelial layer of the placenta in artiodactyls. In this work, three novel ovine PAGs were isolated from late‐pregnancy fetal cotyledons and characterized biochemically. The isolation procedure included acid and ammonium sulfate precipitations and anion and cation exchange chromatographies. The isolated PAGs have different NH2‐terminal amino acid sequences (RGSXLTILPLRNMRDIVY, ISRVSXLTIHPLRNIMDML, and RGSNLTIHPLRNIRD) and apparent molecular masses (55, 57, and 59 kDa). Each shows several isoforms with different pI values. The three proteins share high sequence identity with each other and with other ovine, bovine, and caprine PAGs. They have not been described previously. The ovPAG‐59 sequence differs from the previously identified ovPAG‐4 sequence (determined by DNA cloning and sequencing) at only one position among the 15 N‐terminal residues. The newly characterized ovPAGs and the procedure used to isolate them will be helpful in producing new antisera for investigating PAG secretion in pregnant ewes. Mol. Reprod. Dev. 64: 199–206, 2003. © 2003 Wiley‐Liss, Inc.