The role of molecular chaperones in spermatogenesis and the post-testicular maturation of mammalian spermatozoa

Dun, Matthew D.; Aitken, R. John; Nixon, Brett

doi:10.1093/humupd/dms009

Cited by 111 publications

(104 citation statements)

References 254 publications

(340 reference statements)

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“…Other five of these 18 SP-proteins (EGF-like repeat and discoidin I-like domain-containing protein 3, Putative phospholipase B-like 2 isoform 1, Prominin-2, Ezrin and Syntaxinbinding protein 2) have been related with sperm capacitation [63][64][65][66][67]. Heat shock cognate 71 kDa is a protein related to environmental or physiological stresses [68] synthesized by sperm cells [69] that has been recently related to boar sperm cryotolerance [70]. Finally, Ectonucleotide pyrophosphatase/phosphodiesterase family member is an ATPhydrolyzing enzyme described in epididymis suggesting that this protein could be involved in the modulation of the epididymal environment [71].…”

Section: Discussionmentioning

confidence: 99%

Characterization of the porcine seminal plasma proteome comparing ejaculate portions

Pérez-Patiño

Barranco

Parrilla

et al. 2016

Journal of Proteomics

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Full identification of SP-proteins remains challenging, particularly in some livestock species such as porcine. This experimental study aims to provide an extensive proteomic analysis of boar SP and to generate a public accessible database of boar SP-proteome. A SP-pool from 33 entire ejaculates from 11 boars (3 ejaculates per boar) was analyzed to characterize the boar SP-proteome. Moreover, 20 ejaculates collected in fractions (P1: first 10 mL of sperm rich ejaculate fraction (SRF), P2: rest of SRF and P3: post-SRF) from 5 boars (4 ejaculates per boar) were analyzed to evaluate differentially expressed SP-proteins among portions. SP-samples were subjected to a combination of SEC, 1-D SDS PAGE and NanoLC-ESI-MS/MS followed by functional bioinformatics analysis.The identified proteins were quantified from normalized LFQ intensity data. A total of 33,557 spectra corresponding to 8,189 peptides and 536 SP-proteins were identified with ≥ 95% Confidence (Unused Score > 1.3) and a false discovery rate (FDR) ≤ 1%. Of the 536 SP-proteins, 409 were identified in Sus Scrofa taxonomy and 374 of them were Biological Significance: This proteomic study provides the major characterization of the boar SP-proteome with more than 250 proteins first reported. The boar SP-proteome is described so that a spectral library can be built for relative 'label free' protein quantitation with SWATH approach. This proteomic profiling allows the creation of a publicly accessible database of the boar SP-proteome, as a first step for further understanding the role of SP-proteins in reproductive outcomes as well as for identification of biomarkers for sperm quality and fertility.

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Section: Discussionmentioning

confidence: 99%

Characterization of the porcine seminal plasma proteome comparing ejaculate portions

Pérez-Patiño

Barranco

Parrilla

et al. 2016

Journal of Proteomics

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“…By targeting cyclin T2, miR-15a had a negative effect on the early steps of spermatogenesis (Teng et al 2011). Specifically, HSPs are critically important during spermatogenesis and the posttesticular maturation of mammalian spermatozoa that aberrant expression is associated with spermatogenesis arrested and defects in sperm function (Dun et al 2012). The stage-specific expression pattern displayed by HSPs during spermatogenesis indicates that HSPs are involved in germ cell development (Feng et al 2001, Huo et al 2004, Asquith et al 2005, Terada et al 2005, Held et al 2006, Adly et al 2008, Walsh et al 2008, Lachance et al 2010, Ji et al 2012.…”

Section: Discussionmentioning

confidence: 99%

Expressions of miR-15a and its target gene HSPA1B in the spermatozoa of patients with varicocele

Mou

et al. 2014

Reproduction

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Hyperthermia and oxidative stresses are the two central elements contributing to varicocele-related sperm damage. Growing evidence indicates that microRNAs (miRNAs) are involved in the regulation of the heat and oxidative stress responses. In this study, we analyzed the expressions of several stress-related miRNAs in the sperm and found that the expression of miR-15a was significantly decreased in patients with varicocele compared with the control. Furthermore, miR-15a repressed the expression of HSPA1B, which is a typical stressinduced chaperone protein, through directly binding its 3 0 -UTR. The expressions of miR-15a and HSPA1B exhibited an inverse correlation in sperm. Our results provide a valuable insight into the varicocele-related sperm impairment and male infertility, and may help to develop potential therapeutic targets and novel biomarkers for male infertility.

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“…As a culmination of epididymal maturation, spermatozoa acquire the potential to move progressively and interact with the ZP. Chaperone proteins including clusterin (Hermo et al 1991), HSPA5 (Lachance et al 2010), and HSPD1 (Asquith et al 2005) are thought to regulate epididymal maturation through their indirect roles in promoting the remodeling of sperm surface architecture (Dun et al 2012a). Although the mechanisms by which proteins are incorporated into spermatozoa during epididymal maturation are yet to be completely resolved, it is postulated that this process occurs through sperm membrane fusion with small, epididymal exosomal vesicles termed epididymosomes (Frenette & Sullivan 2001, Sullivan et al 2007) and/or amorphous, electron-dense structures termed dense bodies (Asquith et al 2005).…”

Section: R32 E G Bromfield and B Nixonmentioning

confidence: 99%

“…The generation of a mature spermatozoon requires multiple maturation steps; the first of these occurs in the testis and is assisted by the regulatory action of a diverse family of chaperones, including chaperonincontaining T-complex/TCP1-ring complex (CCT/TRiC), HSP60 (or HSPD1; Meinhardt et al 1995), clusterin (Onoda & Djakiew 1990), HSPA2 (Huszar et al 2000), and the testis-specific chaperones calmegin (CLGN; Ikawa et al 1997, Ohsako et al 1994, and calsperin (CALR3; Ikawa et al 2011), which are developmentally regulated and expressed in spermatogenic cells (see also Dun et al (2012a)). …”

Section: Introductionmentioning

confidence: 99%

The function of chaperone proteins in the assemblage of protein complexes involved in gamete adhesion and fusion processes

Bromfield

Nixon

2013

Reproduction

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The remarkable complexity of the molecular events governing adhesion and fusion of the male and female gametes is becoming apparent. Novel research suggests that these highly specific cellular interactions are facilitated by multiprotein complexes that are delivered to and/or assembled on the surface of the gametes by molecular chaperones in preparation for sperm-egg interaction. While the activation of these molecular chaperones and the mechanisms by which they shuttle proteins to the surface of the cell remain the subject of ongoing investigation, a compelling suggestion is that these processes are augmented by dynamic membrane microdomains or lipid rafts that migrate to the apical region of the sperm head after capacitation. Preliminary studies of the oocyte plasma membrane have also revealed the presence of lipid rafts comprising several molecular chaperones, raising the possibility that similar mechanisms may be involved in the activation of maternal fusion machinery and the regulation of oocyte plasma membrane integrity. Despite these findings, the analysis of oocyte surface multiprotein complexes is currently lacking. Further analyses of the intermediary proteins that facilitate the expression of key players in sperm-egg fusion are likely to deliver important insights into this unique event, which culminates in the cytoplasmic continuity of the male and female gametes.Reproduction (2013) 145 R31-R42

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The role of molecular chaperones in spermatogenesis and the post-testicular maturation of mammalian spermatozoa

Cited by 111 publications

References 254 publications

Characterization of the porcine seminal plasma proteome comparing ejaculate portions

Characterization of the porcine seminal plasma proteome comparing ejaculate portions

Expressions of miR-15a and its target gene HSPA1B in the spermatozoa of patients with varicocele

The function of chaperone proteins in the assemblage of protein complexes involved in gamete adhesion and fusion processes

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