Profiling signaling proteins in human spermatozoa: biomarker identification for sperm quality evaluation

Silva, Joana Vieira; Freitas, Maria João; Correia, Bárbara; Korrodi‐Gregório, Luís; Patrício, António; Pelech, Steven; Fardilha, Margarida

doi:10.1016/j.fertnstert.2015.06.039

Cited by 37 publications

(31 citation statements)

References 92 publications

(84 reference statements)

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“…On grouping of bulls based on PEBP4 expression, the total motile spermatozoa, type-A sperm, and fructose uptake were higher in PEBP4 expressing bulls indicating its significance in sperm functional activity. As the fructose uptake was higher in protein present group, the PEBP4 also might regulate spermatozoa metabolic activity and motility through protein phosphorylations signaling cascades (Silva et al, 2015). Hence, PEBP4 in spermatozoa might regulate the motility by switching the pathways connected to sperm energy consumption.…”

Section: Discussionmentioning

confidence: 76%

“…This is the first study reporting the localization of PEBP4 in the principal piece of ejaculated spermatozoa and a positive association of PEBP4 expression with sperm motility. As the fructose uptake was higher in protein present group, the PEBP4 also might regulate spermatozoa metabolic activity and motility through protein phosphorylations signaling cascades (Silva et al, 2015). The PEBP4 is also a member of RAF kinase inhibitory protein (RKIP1) family inactivating Raf-1/MEK/ERK by exhibiting scaffolding of proteins regulating apoptosis (Yeung et al, 1999;Hickox et al, 2002).…”

Section: Discussionmentioning

confidence: 80%

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Comparative sperm protein profiling in bulls differing in fertility and identification of phosphatidylethanolamine‐binding protein 4, a potential fertility marker

et al. 2017

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This study aimed to identify sperm proteomic signatures regulating sperm functions and fertility by: (i) comparing the sperm electrophoretic protein profiles and identifying the differentially abundant proteins among breeding bulls differing in fertility status and (ii) elucidating the possible role of one of the identified novel proteins, PEBP4 on sperm function and fertility. The grouping of bulls as fertile (n = 6) and low fertile (n = 6) was performed based on bull fertility index and infertile (n = 6) based on semen rejection rate (>33%). The sperm motility, fructolysis index, acrosomal reaction, intracellular calcium levels, and seminal plasma fructose and calcium levels were studied among fertility groups. The differentially expressed sperm proteins observed in single- and two-dimensional gel electrophoresis (2DE) were identified using Nano-LC-MS/MS. In the fertile bulls, the expression levels of calmodulin (CALM1), spermadhesinZ13 (SPADH2), and phosphatidylethanolamine-binding protein 4 (PEBP4) were significantly (p < 0.05) higher than in other fertility groups. In bovine, expression of PEBP4 a novel seminal protein was not observed in spermatozoa of infertile bulls. When the bulls were grouped based on the presence (n = 8) or absence (n = 10) of PEBP4 protein in spermatozoa, a positive significant (p < 0.05) association of this protein with the percentage of motile, type-A spermatozoa, and sperm fructose uptake was observed. Further, PEBP4 was localized in elongated spermatids, Leydig cells, excurrent duct system, and principal piece of spermatozoa. These findings suggest a crucial role for the PEBP4 protein in spermiogenesis, epididymal sperm maturation, and sperm motility. This first study in bovine indicates the positive association of PEBP4 in regulating sperm maturation, functions, and fertility and could be a potential marker for predicting semen quality and fertility.

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Section: Discussionmentioning

confidence: 76%

Section: Discussionmentioning

confidence: 80%

Comparative sperm protein profiling in bulls differing in fertility and identification of phosphatidylethanolamine‐binding protein 4, a potential fertility marker

et al. 2017

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“…The PPAR γ agonist rosiglitazone induced clear improvements in mitochondrial function, and reduced caspase 3 activity, these effects also linked to increased phosphorylation of Akt. Previous reports indicate the importance of Akt phosphorylation in sperm function [15, 16, 52, 53], and recently a link between PPARγ agonists and Akt phosphorylation in human [22] and pig spermatozoa [23] has been reported. Moreover strategies to maintain Akt phosphorylated in spermatozoa have proven to be successful in human sperm cryopreservation [52, 54]…”

Section: Discussionmentioning

confidence: 99%

Rosiglitazone in the thawing medium improves mitochondrial function in stallion spermatozoa through Akt phosphorylation and reduction of caspase 3

Ortiz-Rodríguez

Silva

Masot

et al. 2019

Preprint

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20 Background 21 The population of stallion spermatozoa surviving thawing, experience, among other changes, 22 compromised mitochondrial functionality and accelerated senescence. It is known that the 23 stallion spermatozoa show very active oxidative phosphorylation that may accelerate sperm 24 senescence through increased production of reactive oxygen species. Rosiglitazone has proven 25 to enhance the glycolytic capability of stallion spermatozoa maintained in refrigeration. Objectives27 Thus, we hypothesized that thawed sperm may also benefit from rosiglitazone supplementation. Material and Methods29 Thawed sperm doses were washed and re-suspended in Tyrodes media, split sampled and 30 supplemented with 0 or 75 M rosiglitazone. After 1 and two hours of incubation, 31 mitochondrial functionality, Akt phosphorylation and caspase 3 activity were evaluated. Further 32 samples were incubated in presence of the Akt1/2 inhibitor, compound C (AMPK inhibitor) and 33 GW9662 (antagonist of the PPAR receptor). Results35 Rosiglitazone maintained Akt phosphorylated and reduced caspase 3 activation (p<0.01) that 36 was prevented by incubation in presence of the three inhibitors. Rosiglitazone also enhanced 37 mitochondrial functionality (p<0.01). Conclusion39 We provide, for the first time, evidences that the functionality of frozen stallion spermatozoa 40 can be potentially improved after thawing through the activation pro survival pathways, opening 41 new clues to improve current sperm biotechnologies. 42 43 44 45 INTRODUCTION 46 47The stallion spermatozoa can be stored in the liquid state for short periods, or frozen for long-48 term storage. Frozen thawed sperm has numerous advantages, however its wider use is still 49 constrained by a number of weaknesses [1]. Among them, the high stallion-to-stallion 50 variability and the insufficient standardization of the freezing and thawing procedures. While 51 cryopreservation induces mortality to on average 50% of the initial sperm population, the 52 surviving spermatozoa are not completely functional; on the contrary they experience 53 accelerated senescence that requires more intense and costly mare management for insemination 54 to compensate this reduced lifespan. Most of the studies on sperm cryopreservation have aimed 55 to increase the number of spermatozoa surviving the procedure, but studies aiming to improve 56 the quality of the surviving population are scarce. Although the changes induced by 57 cryopreservation have been extensively investigated, mostly focusing on cryopreservation 58 induced necrosis [2][3][4], few studies have addressed the physiology of spermatozoa surviving 59 freezing and thawing. There are not many studies that have tried to develop measures to 60 increase the quality of frozen sperm after thawing, with the exception of procedures to remove 61 dead and damaged spermatozoa from the cryopreserved sample [5][6][7]. The population of 62 spermatozoa surviving freezing and thawing, experience changes recently termed spermptosis 63 [8]. These change...

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“…While H 2 S decreases phosphorylation by MAPK in the testis [39], NO activates MAPK participating in the tight-junction dynamics of Sertoli cells [106]. This MAPK regulation by H 2 S and NO may also be of interest regarding sperm cells, as it is a crucial pathway affecting sperm motility, morphology, and capacitation [57,107]. For the first time in human spermatozoa, Silva et al [107] identified JNK, which represent a subfamily of MAPKs also referred to as stress-activated protein kinases (SAPKs), as they are activated by phosphorylation under stress conditions (e.g., oxidative stress).…”

Section: No and H 2 S Interactionsmentioning

confidence: 99%

“…This MAPK regulation by H 2 S and NO may also be of interest regarding sperm cells, as it is a crucial pathway affecting sperm motility, morphology, and capacitation [57,107]. For the first time in human spermatozoa, Silva et al [107] identified JNK, which represent a subfamily of MAPKs also referred to as stress-activated protein kinases (SAPKs), as they are activated by phosphorylation under stress conditions (e.g., oxidative stress). The same authors observed a negative correlation of JNK phosphorylated levels with total and progressive motility.…”

Section: No and H 2 S Interactionsmentioning

confidence: 99%

The Roles of NO and H2S in Sperm Biology: Recent Advances and New Perspectives

Kadlec

Ros-Santaella

Pintus

2020

IJMS

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After being historically considered as noxious agents, nitric oxide (NO) and hydrogen sulfide (H2S) are now listed as gasotransmitters, gaseous molecules that play a key role in a variety of cellular functions. Both NO and H2S are endogenously produced, enzymatically or non-enzymatically, and interact with each other in a range of cells and tissues. In spite of the great advances achieved in recent decades in other biological systems, knowledge about H2S function and interactions with NO in sperm biology is in its infancy. Here, we aim to provide an update on the importance of these molecules in the physiology of the male gamete. Special emphasis is given to the most recent advances in the metabolism, mechanisms of action, and effects (both physiological and pathophysiological) of these gasotransmitters. This manuscript also illustrates the physiological implications of NO and H2S observed in other cell types, which might be important for sperm function. The relevance of these gasotransmitters to several signaling pathways within sperm cells highlights their potential use for the improvement and successful application of assisted reproductive technologies.

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Profiling signaling proteins in human spermatozoa: biomarker identification for sperm quality evaluation

Abstract: This study contributed toward establishing a biomarker "fingerprint" to assess sperm quality on the basis of molecular parameters.

Cited by 37 publications

References 92 publications

Comparative sperm protein profiling in bulls differing in fertility and identification of phosphatidylethanolamine‐binding protein 4, a potential fertility marker

Comparative sperm protein profiling in bulls differing in fertility and identification of phosphatidylethanolamine‐binding protein 4, a potential fertility marker

Rosiglitazone in the thawing medium improves mitochondrial function in stallion spermatozoa through Akt phosphorylation and reduction of caspase 3

The Roles of NO and H2S in Sperm Biology: Recent Advances and New Perspectives

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