TAILIEUCHUNG - Báo cáo Y học: The porcine trophoblastic interferon-c, secreted by a polarized epithelium, has specific structural and biochemical properties

At the time of implantation in the maternal uterus, the trophectoderm of the pig blastocyst is the source of a massive secretion of interferon-gamma (IFN-c), together with lesser amounts of IFN-d, a unique species of type I IFN. This trophoblastic IFN-c (TrIFN-c) is an unprecedented example of IFN-c being produced spontaneously by an epithelium. We therefore studied some of its structural and biochemical properties, by comparison with pig IFN-c from other sources, either natural LeIFN-c (from adult leucocytes), or recombinant. . | Eur. J. Biochem. 269 2772-2781 2002 FEBS 2002 doi The porcine trophoblastic interferon-c secreted by a polarized epithelium has specific structural and biochemical properties Avrelija Cencic1 2 Celine Henry3 Francois Lefevre1 Jean-Claude Huet3 Srecko Koren4 and Claude La Bonnardiere1 1Unite de Virologie et d Jmmunologie Moleculaires INRA Jouy en Josas France 2Faculty of Agriculture University of Maribor Slovenia 3 Unite de Biochimie des Proteines INRA Jouy-en-Josas France 4Institute of Microbiology and Immunology Medical Faculty University of Ljubljana Slovenia At the time of implantation in the maternal uterus the trophectoderm of the pig blastocyst is the source of a massive secretion of interferon-gamma IFN-y together with lesser amounts of IFN-8 a unique species of type I IFN. This trophoblastic IFN-y TrIFN-y is an unprecedented e. mi-ple of IFN-y being produced spontaneously by an epithelium. We therefore studied some of its structural and biochemical properties by comparison with pig IFN-y from other sources either natural LeIFN-y from adult leucocytes or recombinant. Biologically active TrIFN-y is a dimeric molecule of which monomers are mainly composed of a truncated polypeptide chain with two glycotypes unlike LeIFN-y which is formed of at least two polypeptide chains and four glycotypes. TrIFN-y collected in the uterus lumen was enzymatically deglycosylated and analysed by mass spectrometry MALDI-TOF . The data revealed that the more abundant polypeptide has a mass of kDa corresponding to a C-terminal cleavage of 17 residues from the expected 143-residue long mature sequence. A minor polypeptide with a mass of kDa corresponds to a C-terminal truncation of 36 amino acids. MALDI-TOF analysis of tryptic peptides from the glycosylated molecule s identifies a single branched carbohydrate motif with six acetylgalactosamines and no sialic acid. The only glycan microheterogeneity seems to reside in the number of .

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