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Protein disulfide isomerase-P5, down-regulated in the final stage of boar epididymal sperm maturation, catalyzes disulfide formation to inhibit protein function in oxidative refolding of reduced denatured lysozyme

Akama, Kuniko ; Horikoshi, Tomoe ; Sugiyama, Atsushi ; Nakahata, Satoko ; Akitsu, Aoi ; Niwa, Nobuyoshi ; Intoh, Atsushi ; Kakui, Yasutaka ; Sugaya, Michiko ; Takei, Kazuo ; Imaizumi, Noriaki ; Sato, Takaya ; Matsumoto, Rena ; Iwahashi, Hitoshi ; Kashiwabara, Shin-ichi ; Baba, Tadashi ; Nakamura, Megumi ; Toda, Tosifusa

Biochimica et biophysica acta, 2010-06, Vol.1804 (6), p.1272-1284 [Periódico revisado por pares]

Netherlands: Elsevier B.V

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Título:
Protein disulfide isomerase-P5, down-regulated in the final stage of boar epididymal sperm maturation, catalyzes disulfide formation to inhibit protein function in oxidative refolding of reduced denatured lysozyme
Autor: Akama, Kuniko ; Horikoshi, Tomoe ; Sugiyama, Atsushi ; Nakahata, Satoko ; Akitsu, Aoi ; Niwa, Nobuyoshi ; Intoh, Atsushi ; Kakui, Yasutaka ; Sugaya, Michiko ; Takei, Kazuo ; Imaizumi, Noriaki ; Sato, Takaya ; Matsumoto, Rena ; Iwahashi, Hitoshi ; Kashiwabara, Shin-ichi ; Baba, Tadashi ; Nakamura, Megumi ; Toda, Tosifusa
Assuntos: Animals ; Anti-chaperone activity ; Base Sequence ; Cloning, Molecular ; Disulfides - chemistry ; Disulfides - metabolism ; Down-Regulation - physiology ; Enzyme Precursors - biosynthesis ; Enzyme Precursors - chemistry ; Enzyme Precursors - genetics ; Epididymis - enzymology ; Fertilization - physiology ; Gene Expression Regulation, Enzymologic - physiology ; Humans ; Male ; Molecular Chaperones - antagonists & inhibitors ; Molecular Chaperones - chemistry ; Molecular Chaperones - genetics ; Molecular Chaperones - metabolism ; Molecular Sequence Data ; Muramidase - chemistry ; Muramidase - metabolism ; Oxidation-Reduction ; Protein Denaturation ; Protein disulfide isomerase A3 ; Protein disulfide isomerase-P5 ; Protein Disulfide-Isomerases - biosynthesis ; Protein Disulfide-Isomerases - chemistry ; Protein Disulfide-Isomerases - genetics ; Protein Folding ; Proteomics ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Species Specificity ; Sperm maturation ; Spermatogenesis - physiology ; Spermatozoa - enzymology ; Swine ; Two-dimensional gel electrophoresis
É parte de: Biochimica et biophysica acta, 2010-06, Vol.1804 (6), p.1272-1284
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SourceType-Scholarly Journals-1
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Descrição: 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.
Editor: Netherlands: Elsevier B.V
Idioma: Inglês

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Protein disulfide isomerase-P5, down-regulated in the final stage of boar epididymal sperm maturation, catalyzes disulfide formation to inhibit protein function in oxidative refolding of reduced denatured lysozyme

Netherlands: Elsevier B.V

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