Phospholipase Cδ4 is required for Ca2+ mobilization essential for acrosome reaction in sperm

Fukami, Kiyoko; Yoshida, Manabu; Inoue, Takafumi; Kurokawa, Manabu; Fissore, Rafael A.; Yoshida, Nobuaki; Mikoshiba, Katsuhiko; Takenawa, Tadaomi

doi:10.1083/jcb.200210057

Cited by 143 publications

(120 citation statements)

References 48 publications

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“…The spatiotemporal pattern of [Ca 2C ] i changes observed in this study is apparently different from the one reported in mouse (Fukami et al 2003), though as yet the [Ca 2C ] i in the entire flagellum of mouse sperm has not been reported. Fukami et al (2003) showed that progesterone initiates an increase in the (Lishko et al 2011, Strunker et al 2011. Interestingly, mouse CatSper does not seem to be activated by progesterone (Lishko et al 2011).…”

Section: Discussioncontrasting

confidence: 52%

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A caged progesterone analog alters intracellular Ca2+ and flagellar bending in human sperm

Servin‐Vences¹,

Tatsu²,

Ando³

et al. 2012

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Progesterone is a physiological agonist for mammalian sperm, modulating its flagellar movement and facilitating the acrosome reaction. To study the initial action of progesterone, we developed a caged analog with a photosensitive group: nitrophenylethanediol, at position 20. Using this compound combined with stroboscopic illumination, we performed Ca 2C imaging of human spermatozoa and analyzed ] i immediately in the flagellum (mid-piece and principal piece), thereafter in the head with a short time lag. This observation is different from the progesterone-induced Ca 2C mobilization in mouse spermatozoa, where the Ca 2C rise initiates at the base of the sperm head. Our finding is mostly consistent with the recent discovery that progesterone activates CatSper channels in human spermatozoa, but not in mouse spermatozoa.

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Section: Discussioncontrasting

confidence: 52%

“…Although CatSper is not activated by progesterone in mouse sperm, progesterone somehow elicits the Ca 2C transient in these cells even from CatSper1-null mice (Ren et al 2001, Fukami et al 2003. This fact suggests that progesterone might activate another Ca 2C influx pathway besides CatSper in mammalian sperm.…”

Section: Discussionmentioning

confidence: 90%

A caged progesterone analog alters intracellular Ca2+ and flagellar bending in human sperm

Servin‐Vences¹,

Tatsu²,

Ando³

et al. 2012

Reproduction

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“…Calcium is a key molecule in the regulation of AR and hyperactivation by steroid hormones (Luconi et al 1999, Baldi et al 2000, 2009, Noguchi et al 2008, Fujinoki 2009). After progesterone binds to the sperm head, it stimulates calcium influx and activation of PLC (Fukami et al 2003, Lö sel & Wehling 2003, Harper et al 2004, Luconi et al 2004, Noguchi et al 2008, Baldi et al 2009, Fujinoki 2009). Moreover, spermatozoa are not hyperactivated in the mTALP medium without calcium (Fujinoki 2008, Noguchi et al 2008.…”

Section: Discussionmentioning

confidence: 99%

“…Moreover, it has been suggested that progesterone binds to the acrosome region, and PGR is localized to the same region in human (Gadkar et al 2002) and hamster spermatozoa (Noguchi et al 2008). Phospholipase C (PLC; Fukami et al 2003) and/or protein kinase A (Harrison et al 2000) are involved in progesteroneinduced AR. Progesterone also changes motility parameters (Yang et al 1994) and enhances hyperactivation in human (Sueldo et al 1993) and hamster spermatozoa (Noguchi et al 2008).…”

Section: Introductionmentioning

confidence: 99%

Suppression of progesterone-enhanced hyperactivation in hamster spermatozoa by estrogen

Fujinoki¹

2010

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In this study, I examined whether sperm hyperactivation in hamster is regulated by steroid hormones such as estrogen (estradiol, E 2 ) and progesterone. Although sperm hyperactivation was enhanced by progesterone, 17b-estradiol (17bE 2 ) itself did not affect sperm hyperactivation. However, 17bE 2 suppressed progesterone-enhanced hyperactivation in a concentration-dependent manner through non-genomic pathways when spermatozoa were exposed to 17bE 2 at the same time or before exposure to progesterone. When spermatozoa were exposed to 17bE 2 after exposure to progesterone, 17bE 2 did not suppress progesterone-enhanced hyperactivation. Moreover, 17a-estradiol, an inactive isomer of E 2 , did not suppress progesterone-enhanced hyperactivation. Observations using a FITC-conjugated 17bE 2 showed that it binds to the acrosome region of the sperm head. Binding of 17bE 2 to spermatozoa was not inhibited by progesterone, although 17bE 2 did not suppress progesterone-enhanced hyperactivation when spermatozoa were exposed to 17bE 2 after exposure to progesterone. On the other hand, binding of progesterone to spermatozoa was also not inhibited by 17bE 2 even if progesterone-enhanced hyperactivation was suppressed by 17bE 2 . Although tyrosine phosphorylations of sperm proteins were enhanced by progesterone, enhancement of tyrosine phosphorylations by progesterone was suppressed by 17bE 2 . Moreover, tyrosine phosphorylations were inhibited by 17bE 2 when only 17bE 2 was added to the medium. From these results, it is likely that 17bE 2 competitively suppresses progesterone-enhanced hyperactivation through the inhibition of tyrosine phosphorylations via non-genomic pathways.

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“…These results show that tight regulation of ion entry by ion channels is critical to sperm function. Although there is little doubt as to the importance of calcium homeostasis in sperm motility and fertilization (7)(8)(9)(10)(11)(12), the function of the plasma membrane Ca 2ϩ /calmodulin-dependent Ca 2ϩ ATPase (PMCA) 1 during this process remained enigmatic.…”

mentioning

confidence: 99%

Plasma Membrane Ca2+ ATPase 4 Is Required for Sperm Motility and Male Fertility

Schuh

Cartwright

Jankevics

et al. 2004

Journal of Biological Chemistry

232

202

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Calcium and Ca 2؉ -dependent signals play a crucial role in sperm motility and mammalian fertilization, but the molecules and mechanisms underlying these Ca 2؉ -dependent pathways are incompletely understood. Here we show that homozygous male mice with a targeted gene deletion of isoform 4 of the plasma membrane calcium/ calmodulin-dependent calcium ATPase (PMCA), which is highly enriched in the sperm tail, are infertile due to severely impaired sperm motility. Furthermore, the PMCA inhibitor 5-(and-6)-carboxyeosin diacetate succinimidyl ester reduced sperm motility in wild-type animals, thus mimicking the effects of PMCA4 deficiency on sperm motility and supporting the hypothesis of a pivotal role of the PMCA4 on the regulation of sperm function and intracellular Ca 2؉ levels.Successful fertilization requires the sperm to travel long distances and undergo capacitation prior to reaching the female egg. After reaching their target, the sperm must interact with the extracellular matrix of the egg, including proteins of the zona pellucida, and release acrosomal material. Calcium is considered to exert a function on most, if not all, of these processes. In this field, most of the work on Ca 2ϩ signaling has focused on Ca 2ϩ entry mechanisms, especially on the role of Ca 2ϩ channels (1-4). For example, gene ablation of the cation channel of sperm (CatSper) leads to impaired sperm motility and male infertility (5), and mice lacking the mitochondrial voltage-dependent anion channel type 3 (VDAC3) are also infertile due to immotile sperm (6). These results show that tight regulation of ion entry by ion channels is critical to sperm function. Although there is little doubt as to the importance of calcium homeostasis in sperm motility and fertilization (7-12), the function of the plasma membrane Ca 2ϩ /calmodulin-dependent Ca 2ϩ ATPase (PMCA) 1 during this process remained enigmatic.PMCA represents a family of enzymes that extrude calcium from the cytosol across the plasma membrane of eukaryotic cells. Since their initial identification in erythrocytes (13), four different isoforms have been identified, and multiple splice forms of these isoforms have been described. The well defined tissue-specific expression pattern of different isoforms and splice variants of the pump in various mammalian tissues (14) and the regulated expression pattern during mouse development (15) strongly suggest a specific physiological function for each isoform and splice variant (reviewed in Strehler and Zacharias (16)). The identification of physical and functional interaction partners of the Ca 2ϩ pump has given insights into the putative functions of PMCAs as regulators of Ca 2ϩ -dependent signal transduction processes (17-21). Interaction of PMCA2 and -4 "b" splice variants was shown to be mediated by the PDZ-(PSD-95/Dlg/ZO-1) domain of the corresponding interaction partner and the C termini of the PMCA isoform (which harbors a typical PDZ domain binding motif (17)). Both modes of interaction with PDZ domain-containing proteins, specific and...

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Phospholipase Cδ4 is required for Ca2+ mobilization essential for acrosome reaction in sperm

Cited by 143 publications

References 48 publications

A caged progesterone analog alters intracellular Ca2+ and flagellar bending in human sperm

A caged progesterone analog alters intracellular Ca2+ and flagellar bending in human sperm

Suppression of progesterone-enhanced hyperactivation in hamster spermatozoa by estrogen

Plasma Membrane Ca2+ ATPase 4 Is Required for Sperm Motility and Male Fertility

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