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http://purl.uniprot.org/citations/20152940http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20152940http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/20152940http://www.w3.org/2000/01/rdf-schema#comment"In mammalian spermiogenesis, sperm mature during epididymal transit to get fertility. The pig sharing many physiological similarities with humans is considered a promising animal model in medicine. We examined the expression profiles of proteins from boar epididymal caput, corpus, and cauda sperm by two-dimensional gel electrophoresis and peptide mass fingerprinting. Our results indicated that protein disulfide isomerase-P5 (PDI-P5) human homolog was down-regulated from the epididymal corpus to cauda sperm, in contrast to the constant expression of protein disulfide isomerase A3 (PDIA3) human homolog. To examine the functions of PDIA3 and PDI-P5, we cloned and sequenced cDNAs of pig PDIA3 and PDI-P5 protein precursors. Each recombinant pig mature PDIA3 and PDI-P5 expressed in Escherichia coli showed thiol-dependent disulfide reductase activities in insulin turbidity assay. Although PDIA3 showed chaperone activity to promote oxidative refolding of reduced denatured lysozyme, PDI-P5 exhibited anti-chaperone activity to inhibit oxidative refolding of lysozyme at an equimolar ratio. SDS-PAGE and Western blotting analysis suggested that disulfide cross-linked and non-productively folded lysozyme was responsible for the anti-chaperone activity of PDI-P5. These results provide a molecular basis and insights into the physiological roles of PDIA3 and PDI-P5 in sperm maturation and fertilization."xsd:string
http://purl.uniprot.org/citations/20152940http://purl.org/dc/terms/identifier"doi:10.1016/j.bbapap.2010.02.004"xsd:string
http://purl.uniprot.org/citations/20152940http://purl.org/dc/terms/identifier"doi:10.1016/j.bbapap.2010.02.004"xsd:string
http://purl.uniprot.org/citations/20152940http://purl.uniprot.org/core/author"Baba T."xsd:string
http://purl.uniprot.org/citations/20152940http://purl.uniprot.org/core/author"Baba T."xsd:string
http://purl.uniprot.org/citations/20152940http://purl.uniprot.org/core/author"Matsumoto R."xsd:string
http://purl.uniprot.org/citations/20152940http://purl.uniprot.org/core/author"Matsumoto R."xsd:string
http://purl.uniprot.org/citations/20152940http://purl.uniprot.org/core/author"Nakamura M."xsd:string
http://purl.uniprot.org/citations/20152940http://purl.uniprot.org/core/author"Nakamura M."xsd:string
http://purl.uniprot.org/citations/20152940http://purl.uniprot.org/core/author"Sato T."xsd:string
http://purl.uniprot.org/citations/20152940http://purl.uniprot.org/core/author"Sato T."xsd:string
http://purl.uniprot.org/citations/20152940http://purl.uniprot.org/core/author"Sugiyama A."xsd:string
http://purl.uniprot.org/citations/20152940http://purl.uniprot.org/core/author"Sugiyama A."xsd:string
http://purl.uniprot.org/citations/20152940http://purl.uniprot.org/core/author"Iwahashi H."xsd:string
http://purl.uniprot.org/citations/20152940http://purl.uniprot.org/core/author"Iwahashi H."xsd:string
http://purl.uniprot.org/citations/20152940http://purl.uniprot.org/core/author"Kashiwabara S."xsd:string
http://purl.uniprot.org/citations/20152940http://purl.uniprot.org/core/author"Kashiwabara S."xsd:string
http://purl.uniprot.org/citations/20152940http://purl.uniprot.org/core/author"Takei K."xsd:string
http://purl.uniprot.org/citations/20152940http://purl.uniprot.org/core/author"Takei K."xsd:string
http://purl.uniprot.org/citations/20152940http://purl.uniprot.org/core/author"Toda T."xsd:string
http://purl.uniprot.org/citations/20152940http://purl.uniprot.org/core/author"Toda T."xsd:string
http://purl.uniprot.org/citations/20152940http://purl.uniprot.org/core/author"Nakahata S."xsd:string
http://purl.uniprot.org/citations/20152940http://purl.uniprot.org/core/author"Nakahata S."xsd:string