Intriguing location of myeloperoxidase in the prostate: A preliminary immunohistochemical study

Roumeguere, T.; Delrée, P.; Antwerpen, Pierre Van; Rorive, Sandrine; Vanhamme, Luc; Ryhove, L. de la Kethulle de; Serteyn, Didier; Wespes, Eric; Vanhaerverbeek, M.; Boudjeltia, Karim Zouaoui

doi:10.1002/pros.21452

Cited by 23 publications

(20 citation statements)

References 21 publications

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“…Samples were divided around the median sperm count of 56.5 9 10 6 /mL of seminal plasma (below/equal median group n = 17; above median group n = 16). A recent study has shown the presence of myeloperoxidase in the glandular epithelial cells of the prostate (Roumeguere et al, 2012); however, the importance of this is unclear. The seminal plasma myeloperoxidase protein concentration was significantly different between the two groups (two-sample independent t-test with unequal variances).…”

Section: Discussionmentioning

confidence: 98%

“…This would preclude the prostate and seminal vesicles, where the presence of neutrophils is well established, as neutrophils from these glands should only come into contact with spermatozoa at the point of ejaculation (Aitken & Baker, 2013). A recent study has shown the presence of myeloperoxidase in the glandular epithelial cells of the prostate (Roumeguere et al, 2012); however, the importance of this is unclear. How and where inflammatory processes are able to impact on sperm health should be a focus for future studies.…”

Section: Discussionmentioning

confidence: 99%

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Elevated seminal plasma myeloperoxidase is associated with a decreased sperm concentration in young men

et al. 2017

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Myeloperoxidase is a major neutrophil protein which generates oxidants that are highly reactive, and if present in seminal fluid, could be potentially damaging to spermatozoa. We recruited young males aged 18-35 years, unscreened for fertility status, for a pilot study measuring seminal plasma myeloperoxidase. On three occasions, over a 3-month period, we measured parameters of semen quality and correlated these with seminal myeloperoxidase protein and activity. After baseline measurement, participants were supplemented daily with 250 mg of vitamin C, a potent scavenger of reactive oxygen species with antiinflammatory activities. Seminal plasma from eight of the 12 participants had measurable concentrations of myeloperoxidase protein, across a broad range (15-250 ng/mL). Median myeloperoxidase protein concentrations were ~45-fold higher in semen samples with low vs. high sperm concentrations. Seminal plasma myeloperoxidase protein concentration was inversely correlated with the percentage of rapidly motile spermatozoa assessed by computer-assisted sperm analysis, and the total number of spermatozoa per ejaculate, but positively correlated with sperm maturity, measured by DNA staining ability. We measured an inverse correlation between semen vitamin C concentration and seminal plasma myeloperoxidase protein concentration, although vitamin C supplementation had no effect on semen quality. Our pilot data suggest that high concentrations of myeloperoxidase were present in the seminal plasma of many of our young participants, and that this may be associated with decreases in semen quality. A larger study is required to confirm these findings.

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Section: Discussionmentioning

confidence: 98%

Section: Discussionmentioning

confidence: 99%

Elevated seminal plasma myeloperoxidase is associated with a decreased sperm concentration in young men

et al. 2017

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“…To date, few data are available about the origin and characterization of NSC in the equine. In dogs, squamous epithelial cells are observed in prostatic squamous metaplasia [27,28] and, recently, MPO has been observed in epithelial cells of human prostatic biopsies [29]. Further investigation in the equine should consider specific staining of genital tract biopsy samples to assess NSC anatomic origin.…”

Section: Discussionmentioning

confidence: 99%

Effect of non–sperm cells removal with single-layer colloidal centrifugation on myeloperoxidase concentration in post-thaw equine semen

et al. 2013

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Myeloperoxidase (MPO) is a pro-oxidant enzyme contained in and released by neutrophils during degranulation or after lysis. Post-thaw semen contains MPO and its concentration is associated with decreased sperm motility. Recently, MPO concentration in post-thaw semen was shown to be associated with the presence of non-sperm cells (NSC). The objective of this study was to evaluate the effect of a single-layer colloidal centrifugation before cryopreservation on NSC and MPO concentrations in equine semen. The experimental design consisted of freezing semen with or without previous centrifugation through two concentrations of single-layer colloid media. Non-sperm cells and MPO concentrations were assessed in pellet and upper layer at each step of the procedure and MPO was detected in cells by immunocytochemistry. Single-layer colloid centrifugation decreased NSC and MPO concentrations in post-thaw semen. The MPO concentration was correlated with concentration of NSC in the upper layer of the supernatant. In post-thaw semen, with or without previous single-layer colloid centrifugation, MPO concentration was correlated with concentration of NSC. Overall, neutrophils were rarely observed and NSC were mainly epithelial cells or cellular debris, as demonstrated by MPO immunocytochemistry. At all steps of the semen processing and cryopreservation, MPO immunostaining was clearly identified only on NSC. In conclusion, our study shows that NSC present in fresh semen release MPO during freezing.

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“…Previously, MPO immunostaining has been observed in horses NSC ) and in human prostatic cells (Roumeguere et al 2012). Recent studies (Ponthier et al 2013) confirmed that NSC undergoing cellular damage associated to freezing (Graham-Pole et al 1977;Wang et al 1997b) release MPO, somehow acting like sponges.…”

Section: Discussionmentioning

confidence: 87%

Concentration, Activity and Biochemical Characterization of Myeloperoxidase in Fresh and Post‐Thaw Equine Semen and their Implication on Freezability

Ponthier

Franck

Parrilla-Hernandez

et al. 2014

Reprod Domestic Animals

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Myeloperoxidase (MPO) is a pro-oxidant enzyme associated with decreased motility in thawed equine semen. This study aimed to describe MPO concentration, activity and subunits in raw and thawed semen and to correlate these data with motilities in raw and thawed semen. Semen samples from five stallions were collected four times. Motilities were assessed in raw and thawed semen. MPO assays were performed in raw seminal plasma, raw sperm-rich pellet and thawed semen. Total and active MPO concentrations were, respectively, assayed by enzyme-linked immunosorbent assay and specific immunological extraction followed by enzymatic detection. MPO subunits present in semen were characterized by Western blot. Purified active MPO was added in saline solution and freezing extender to control its activity during freezing procedure. Differences between medians were determined using Kruskal-Wallis test, and correlations were determined using Spearman's test for nonparametric data. Active MPO concentration was low in seminal plasma and thawed semen, but high in pellet (p = 0.0058), as the opposite relation was observed for total MPO concentration (p < 0.0001). In seminal plasma and post-thaw semen, inactive 86-kDa MPO precursor was mainly observed. Purified MPO activity was decreased in the extender (p = 0.0286). MPO activity in pellet was highly correlated with thawed progressive motility (r = -0.5576, p = 0.0086). Inactive MPO precursor and unknown low molecular weight inactive MPO precursor subunits explain low MPO activity in semen. Major MPO activity was observed in pellet, and post-thaw loss of activity is partially explained by MPO inactivation in extender. Thawed semen motility was negatively correlated with MPO activity in pellet, becoming a potential freezability predictor.

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Intriguing location of myeloperoxidase in the prostate: A preliminary immunohistochemical study

Abstract: We identified, for the first time, the presence of MPO at the surface of prostatic epithelial cells. In view of the pro-oxidant properties of this enzyme, further research is needed to define whether MPO contributes to the development of prostatic lesions.

Cited by 23 publications

References 21 publications

Elevated seminal plasma myeloperoxidase is associated with a decreased sperm concentration in young men

Elevated seminal plasma myeloperoxidase is associated with a decreased sperm concentration in young men

Effect of non–sperm cells removal with single-layer colloidal centrifugation on myeloperoxidase concentration in post-thaw equine semen

Concentration, Activity and Biochemical Characterization of Myeloperoxidase in Fresh and Post‐Thaw Equine Semen and their Implication on Freezability

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