Publications by authors named "Xingzhou Xu"

B cell activating factor (BAFF) and its receptors were regarded as elements of the immune system, regulating the fate of B cell. In recent years, these molecules were identified in a number of normal and pathological tissues, expanding their potential functions beyond the immune system. In this study, on the basis of molecular clone and prokaryotic expression of equine BAFF, we reported that equine adipose-derived stem cell (ASC) expressed BAFF and its receptors, which exhibited the increased expression during ASC adipogenic differentiation in vitro.

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B-cell survival depends on signals induced by B-cell activating factor (BAFF) that binds to the BAFF receptor (BAFF-R). Herein, a BAFF-R homolog was identified in a horse (Equus caballus). The horse BAFF-R gene, located on chromosome 28, spans 1444 base pairs and encodes a 183-amino acid protein.

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Oryctolagus cuniculus is an important animal model which is widely used for vaccine development, and investigations of human infectious and autoimmune diseases. TNFSF14 is one of the most important TNF superfamily cytokines playing roles in lymphocyte homeostasis by enhancing effector cell activation and survival, or by cellular elimination through apoptosis. For these applications, we cloned full-length cDNA encoding TNFSF14 and its receptor LTBR from O.

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Members of the tumor necrosis factor (TNF) family play key roles in the regulation of inflammation, immune responses and tissue homeostasis. Here we describe the identification of the Japanese sea perch (Lateolabrax japonicus) homologue of mammalian B cell activating factor of the TNF family (BAFF/BLyS) (designated LjBAFF). The cDNA contains an open reading frame (ORF) of 783 nucleotides that are translated into a predicted 260 amino acid protein.

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In this study, an interferon-γ-inducible-lysosomal thiol reductase (GILT) homologue has been cloned and identified from South African clawed frog Xenopus laevis (designated XlGILT). The open reading frame (ORF) of XlGILT consists of 771 bases encoding a protein of 256 amino acids with an estimated molecular mass of 28.76kDa and a theoretical isoelectric point of 5.

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In this study, an IL-8 homologue has been cloned and identified from South African clawed frog Xenopus laevis (designated XlIL-8). The open reading frame (ORF) of XlIL-8 consists of 312 bases encoding a protein of 103 amino acids. The chemokine CXC domain, which contained Glu-Leu-Arg (ELR) motif and four cysteine residues, was well conserved in South African clawed frog IL-8.

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