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, K.; Imaizumi, Noriaki; Sato, Tokijiro; Matsumoto, Ryosuke; Iwahashi, Hitoshi; Kashiwabara, Shin‐ichi; Baba, Tadashi; Nakamura, Megumi; Toda, Tosifusa

doi:10.1016/j.bbapap.2010.02.004

Cited by 19 publications

(23 citation statements)

References 56 publications

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“…The decline in PDIA3 expression during epididymal progression in healthy boars contrasts with the findings of (Akama et al, 2010), who found that, in boars, PDIA3 remained unchanged during epididymal maturation. This may reflect a level of species/strain or age-related diversity in chaperone expression control in epididymal tissues.…”

Section: (A) (B)contrasting

confidence: 55%

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GnRH immunization alters the expression and distribution of protein disulfide isomerases in the epididymis

et al. 2016

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SUMMARYHypogonadism is defined as the inadequate gonadal production of testosterone. Low serum testosterone leads to infertility by impairing spermatogenesis and reducing sperm count, however, the impact of hypogonadism in epididymal sperm maturation is poorly understood. From the testis, spermatozoa are transported into the epididymis where they find a specific microenvironment composed of a complex mixture of proteins that facilitate sperm storage and maturation. Inside the epididymal ductule, spermatozoa undergo several changes, resulting in their becoming capable of fertilizing eggs. Protein disulfide isomerases (PDIs) are known to participate in the folding and assembly of secreted proteins in the endoplasmic reticulum. However, little is known about the control and function of PDIs in the testis and epididymis, particularly during male development. The aim of this work was to compare the expression and distribution of PDI and PDIA3 (ERp57) in the testis and epididymis of healthy and GnRH-immunized boars. We detected higher amounts of PDIA3 and PDI in sperm preparations and fluid from the proximal regions of the epididymis of healthy boars. However, we observed an increase in PDIA3 expression in the testis and cauda epididymis in the immunocastrated group. GnRH-immunized boars showed a marked increase in PDI content in cauda spermatozoa and fluid, indicating a possible endocrine dysregulation of PDI. The results of our study suggest that PDIs are associated with epididymal sperm maturation and may be attractive candidates for monitoring male fertility.

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Section: (A) (B)contrasting

confidence: 55%

“…Protein-disulfide isomerase-associated 3 was previously described in boar epididymal spermatozoa (Akama et al, 2010) and is also associated with fertility potential in men. It was demonstrated recently that the amount of PDIA3 is reduced in the spermatozoa of male individuals with obesity-associated asthenozoospermia (Liu et al, 2015).…”

Section: Introductionmentioning

confidence: 99%

GnRH immunization alters the expression and distribution of protein disulfide isomerases in the epididymis

et al. 2016

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“…Here the population of vesicles might be mixed and derived from different organs, such as prostate, epididymis, or accessory glands. For instance, PDIA3, a marker of the vesicles isolated after 20,0009g centrifugation is a protein constitutively expressed in the epididymal structures (Akama et al 2010). However, no specific tissue marker characterized the two prostasome populations.…”

Section: Discussionmentioning

confidence: 99%

Identification and Partial Characterization of Two Populations of Prostasomes by a Combination of Dynamic Light Scattering and Proteomic Analysis

Chiasserini

Mazzoni²,

Bordi

et al. 2015

J Membrane Biol

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Prostasomes are vesicles secreted by prostate epithelial cells and are found in abundance in the semen. Here we characterized two different prostasome populations isolated from human seminal fluid. Prostasomes were isolated using differential centrifugation, while dynamic light scattering (DLS) was used to characterize their size and size distribution. Their protein content was analyzed using two-dimensional electrophoresis and mass spectrometry. DLS showed two distinct prostasome subpopulations in centrifuged seminal plasma, with an average hydrodynamic radius of 80 and 300 nm. The larger population was isolated after centrifugation at 20,000 × g (P20), while the smaller one was recovered at 100,000 × g (P100). The two fractions had a similar lipid composition, showing an elevated content of sphingomyelin and cholesterol. The P100 vesicles showed a significant over-expression of proteins involved in the endosomal sorting complexes required for transport (ESCRT) machinery such as Alix, TSG101, and syntenin-1. Some proteins possibly involved in prostate cancer were present only in one specific population (TMPRSS2 in P100 and VCP in P20). The different size and protein profile in the two subpopulations of prostasomes might support differential roles of the semen vesicles toward the target cells, and/or different secretion pathways from the organ of origin.

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“…While the enzymes involved in sperm sulfhydryl oxidation are not well characterized, a sulfhydryl oxidase activity is present in epididymal luminal fl uid which prevented fl agellar angulation in hamster caput epididymal spermatozoa induced to acquire motility [ 98 , 101 ]. Protein disulfi de isomerase which catalyzes disulfi de bond formation is also present in the epididymal fl uid and may participate in sperm disulfi de bond formation [ 102 ]. Finally, sperm sulfhydryl oxidation has been shown to facilitate protein tyrosine phosphorylation.…”

Section: Disulfide Bond Formationmentioning

confidence: 98%

Role of Posttranslational Protein Modifications in Epididymal Sperm Maturation and Extracellular Quality Control

Cornwall

2014

Advances in Experimental Medicine and Biology

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The epididymal lumen is a complex microenvironment in which spermatozoa acquire motility and fertility. Spermatozoa are synthetically inactive and therefore the maturation process requires their interaction with proteins that are synthesized and secreted in a highly regionalized manner by the epididymal epithelium. In addition to the integration of epididymal secretory proteins, posttranslational modifications of existing sperm proteins are important for sperm maturation and acquisition of fertilizing potential. Phosphorylation, glycosylation, and processing are several of the posttranslational modifications that sperm proteins undergo during epididymal transit resulting in changes in protein function and localization ultimately leading to mature spermatozoa. In addition to these well-characterized modifications, protein aggregation and cross-linking also occur within the epididymal lumen and may represent unique mechanisms for controlling protein function including that for maturation as well as for extracellular quality control.

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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

Cited by 19 publications

References 56 publications

GnRH immunization alters the expression and distribution of protein disulfide isomerases in the epididymis

GnRH immunization alters the expression and distribution of protein disulfide isomerases in the epididymis

Identification and Partial Characterization of Two Populations of Prostasomes by a Combination of Dynamic Light Scattering and Proteomic Analysis

Role of Posttranslational Protein Modifications in Epididymal Sperm Maturation and Extracellular Quality Control

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