Characterization of NAADP-mediated calcium signaling in human spermatozoa

Sánchez-Tusié, Ana A.; Vasudevan, Sridhar R.; Churchill, Grant C.; Nishigaki, Takuya; Treviño, Claudia L.

doi:10.1016/j.bbrc.2013.12.011

Cited by 14 publications

(23 citation statements)

References 26 publications

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“…Their data suggest that the generation of sustained [Ca 2 + ] i signals (such as the second component of the biphasic progesterone-induced [Ca 2 + ] i signal) and consequent effects on motility may depend, at least partly, upon generation of cADPR by prostasome-derived enzymes. Interestingly, CD38-null mice proved to be fertile, but analysis showed that 20% of normal ADPR cyclase activity remained in prostasomes from these animals, indicating the presence of a non-CD38 ADPR-cyclase, potentially that described by Sanchez-Tusie et al . (2014) .…”

Section: Ca 2 + Stores Mechanisms For mentioning

confidence: 74%

“…Furthermore, the presence of a novel NAADP synthase, which lacks the cyclase activity of CD38, has been described both in sea urchin ( Vasudevan et al . 2008 ) and human sperm ( Sanchez-Tusie et al . 2014 ).…”

Section: Ca 2 + Stores Mechanisms For mentioning

confidence: 99%

“…In sea urchin sperm this enzyme is strongly Ca 2 + -regulated and most active at acid pH whereas the human enzyme shows only weak Ca 2 + -regulation and activity is maximal at pH 7–8 ( Vasudevan et al . 2008 , Sanchez-Tusie et al . 2014 ).…”

Section: Ca 2 + Stores Mechanisms For mentioning

confidence: 99%

“…Recent findings have supported the idea that NAADP is functional in human sperm. Sanchez-Tusie et al . (2014) investigated the effects of cell-permeant (AM-ester) derivatives of NAAPD and cADPR.…”

Section: Ca 2 + Stores Mechanisms For mentioning

confidence: 99%

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Regulation and roles of Ca2+ stores in human sperm

Correia¹,

Michelangeli²,

Publicover³

2015

Reproduction

100

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[Ca2 +]i signalling is a key regulatory mechanism in sperm function. In mammalian sperm the Ca2 +-permeable plasma membrane ion channel CatSper is central to [Ca2 +]i signalling, but there is good evidence that Ca2 + stored in intracellular organelles is also functionally important. Here we briefly review the current understanding of the diversity of Ca2 + stores and the mechanisms for the regulation of their activity. We then consider the evidence for the involvement of these stores in [Ca2 +]i signalling in mammalian (primarily human) sperm, the agonists that may activate these stores and their role in control of sperm function. Finally we consider the evidence that membrane Ca2 + channels and stored Ca2 + may play discrete roles in the regulation of sperm activities and propose a mechanism by which these different components of the sperm Ca2 +-signalling apparatus may interact to generate complex and spatially diverse [Ca2 +]i signals.

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Section: Ca 2 + Stores Mechanisms For mentioning

confidence: 74%

Section: Ca 2 + Stores Mechanisms For mentioning

confidence: 99%

Section: Ca 2 + Stores Mechanisms For mentioning

confidence: 99%

Section: Ca 2 + Stores Mechanisms For mentioning

confidence: 99%

See 2 more Smart Citations

Regulation and roles of Ca2+ stores in human sperm

Correia¹,

Michelangeli²,

Publicover³

2015

Reproduction

100

View full text Add to dashboard Cite

show abstract

“…TPC2 transcripts are present in reproductive tissues and TPC1 proteins were documented in sperm from mouse, rat, and human by Western blot (Arndt et al 2014). Interestingly, in human sperm NAADP induced Ca 2+ mobilization (Sánchez-Tusie et al 2014) and the AR (Arndt et al 2014) in the absence of extracellular Ca 2+ , a condition also observed by De Blas et al (2002) but implicating the IP3R instead of TPC. Since Arndt also observed colocalization of IP3R and TPC1 in lipid rafts, they proposed that acrosomal exocytosis may well fit the "NAADP trigger hypothesis" (Calcraft et al 2009), in which initial NAADP Ca 2+ release triggers further Ca 2+ release through IP3 or Ryanodine receptors located in adjacent Ca 2+ stores amplifying the signal (Correia et al 2015).…”

Section: Tpc Channelsmentioning

confidence: 89%

Role of Ion Channels in the Sperm Acrosome Reaction

Beltrán

Treviño

Mata-Martínez

et al. 2016

Advances in Anatomy, Embryology and Cell Biology

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The acrosome reaction (AR) is a unique exocytotic process where the acrosome, a single membrane-delimited specialized organelle, overlying the nucleus in the sperm head of many species, fuses with the overlying plasma membrane. This reaction, triggered by physiological inducers from the female gamete, its vicinity, or other stimuli, discharges the acrosomal content modifying the plasma membrane, incorporating the inner acrosomal membrane, and exposing it to the extracellular medium. The AR is essential for sperm-egg coat penetration, fusion with the eggs' plasma membrane, and fertilization. As in most exocytotic processes Ca(2+) is crucial for the AR, as well as intracellular pH and membrane potential changes. Thus, among the required processes needed for this reaction, ion permeability changes involving channels are pivotal. In spite of the key role ion channels play in the AR, their identity and regulation is not fully understood. Though molecular and pharmacological evidence indicates that various ionic channels participate during the AR, such as store-operated Ca(2+) channels and voltage-dependent Ca(2+) channels, whole cell patch clamp recordings have failed to detect some of them until now. Since sperm display a very high resistance and a minute cytoplasmic volume, very few channels are needed to achieve large membrane potential and concentration changes. Functional detection of few channels in the morphologically complex and tiny sperm poses technical problems, especially when their conductance is very small, as in the case of SOCs. Single channel recordings and novel fluorescence microscopy strategies will help to define the participation of ionic channels in the intertwined signaling network that orchestrates the AR.

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Acrosomal alkalization triggers Ca²⁺ release and acrosome reaction in mammalian spermatozoa

Chávez

Vega-Beltrán

Omar

et al. 2018

Journal Cellular Physiology

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The sperm acrosome reaction (AR), an essential event for mammalian fertilization, involves Ca permeability changes leading to exocytosis of the acrosomal vesicle. The acrosome, an intracellular Ca store whose luminal pH is acidic, contains hydrolytic enzymes. It is known that acrosomal pH (pH ) increases during capacitation and this correlates with spontaneous AR. Some AR inducers increase intracellular Ca concentration ([Ca ] ) through Ca release from internal stores, mainly the acrosome. Catsper, a sperm specific Ca channel, has been suggested to participate in the AR. Curiously, Mibefradil and NNC55-0396, two CatSper blockers, themselves elevate [Ca ] by unknown mechanisms. Here we show that these compounds, as other weak bases, can elevate pH , trigger Ca release from the acrosome, and induce the AR in both mouse and human sperm. To our surprise, μM concentrations of NNC55-0396 induced AR even in nominally Ca free media. Our findings suggest that alkalization of the acrosome is critical step for Ca release from the acrosome that leads to the acrosome reaction.

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Characterization of NAADP-mediated calcium signaling in human spermatozoa

Cited by 14 publications

References 26 publications

Regulation and roles of Ca2+ stores in human sperm

Regulation and roles of Ca2+ stores in human sperm

Role of Ion Channels in the Sperm Acrosome Reaction

Acrosomal alkalization triggers Ca²⁺ release and acrosome reaction in mammalian spermatozoa

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Characterization of NAADP-mediated calcium signaling in human spermatozoa

Cited by 14 publications

References 26 publications

Regulation and roles of Ca2+ stores in human sperm

Regulation and roles of Ca2+ stores in human sperm

Role of Ion Channels in the Sperm Acrosome Reaction

Acrosomal alkalization triggers Ca2+ release and acrosome reaction in mammalian spermatozoa

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Product

Resources

About

Acrosomal alkalization triggers Ca²⁺ release and acrosome reaction in mammalian spermatozoa