Allurin, an Amphibian Sperm Chemoattractant Having Implications for Mammalian Sperm Physiology

Burnett, Lindsey A.; Washburn, Catherine; Sugiyama, Hitoshi; Xiang, Xueyu; Olson, John H.; Al-Anzi, Bader; Bieber, Allan L.; Chandler, Douglas E.

doi:10.1016/b978-0-12-394306-4.00007-1

Cited by 8 publications

(8 citation statements)

References 217 publications

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“…Our subsequent structure–function experiments showing that CRISP1 with a deficient disulfide bond content ( Ellerman et al, 2002 ) was unable to stimulate sperm orientation, support the relevance of protein conformation and/or disulfide bond formation for CRISP1 sperm-orienting activity as previously reported for allurin ( Burnett et al, 2011a ,b ). As synthetic peptides that mimic the hinge region of allurin in structure exhibit chemoattractant activity to sperm ( Burnett et al, 2012 ), it is likely that the orienting ability of CRISP1 requires the proper conformation of the hinge region of the molecule.…”

Section: Discussionmentioning

confidence: 99%

“…Whereas the role of CRISP1 expressed in the male tract has been studied extensively, only scattered information is available on the presence of this protein in the mammalian female tract ( Reddy et al, 2008 ; Burnett et al, 2012 ). In this regard, it is known that allurin, a nonmammalian homologue of CRISP proteins, is secreted in the oviduct of the frogs Xenopus leavis and Xenopus tropicalis ( Olson et al, 2001 ; Burnett et al, 2008 ), binds to their egg jelly, and exerts a chemoattractant effect in vitro not only on frog but also on mouse sperm ( Xiang et al, 2005 ; Burnett et al, 2011a ).…”

Section: Introductionmentioning

confidence: 99%

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CRISP1 as a novel CatSper regulator that modulates sperm motility and orientation during fertilization

Ernesto

Muñoz

Battistone

et al. 2015

Journal of Cell Biology

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

CRISP1 as a novel CatSper regulator that modulates sperm motility and orientation during fertilization

Ernesto

Muñoz

Battistone

et al. 2015

Journal of Cell Biology

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“…Sperm-oocyte interaction occurs at many levels beginning with chemotactic signals that modify sperm swimming behavior, followed by binding interactions between the sperm and the extracellular matrix of the oocyte, and concluding with sperm binding to and fusing with the oocyte plasma membrane (Vacquier & Swanson 2011; Burnett et al . 2012; Bromfield & Nixon 2012; Gupta et al .…”

Section: Discussionmentioning

confidence: 99%

Protein tyrosine kinase signaling in the mouse oocyte cortex during sperm–egg interactions and anaphase resumption

McGinnis

Luo

Kinsey

2013

Molecular Reproduction Devel

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Fertilization triggers activation of a series of pre-programmed signal transduction pathways in the oocyte that establish a block to polyspermy, induce meiosis resumption, and initiate zygotic development. The fusion between sperm and oocyte results in rapid changes in oocyte intracellular free calcium levels which in turn activate multiple protein kinase cascades in the ooplasm. The present study has examined the possibility that sperm-oocyte interaction involves localized activation of oocyte protein tyrosine kinases which could provide an alternative signaling mechanism triggered by the fertilizing sperm. Confocal immunofluorescence analysis with antibodies to phosphotyrosine and phosphorylated protein tyrosine kinases allowed detection of minute signaling events localized to the site of sperm-oocyte interaction that were not amenable to biochemical analysis. The results provide evidence for localized accumulation of phosphotyrosine at the site of sperm contact, binding, or fusion, which suggests active protein tyrosine kinase signaling prior to and during sperm incorporation. The PYK2 kinase was found to be concentrated and activated at the site of sperm-oocyte interaction and likely participates in this response. Widespread activation of PYK2 and FAK kinases was subsequently observed within the oocyte cortex indicating that sperm incorporation is followed by more global signaling by these kinases during meiosis resumption. The results demonstrate an alternating signaling pathway triggered in mammalian oocytes by sperm contact, binding, or fusion with the oocyte.

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“…In mice, CRISP1 inhibited membrane depolarization as well as Catsper signaling in epididymal spermatozoa, confirming the ability of the protein to block this sperm Ca 2+ channel [82]. However, only scattered information is available regarding the presence of this protein in the mammalian female tract [83]. Ernesto et al [82] was the first group to provide evidence that CRISP1 is also expressed by oviduct cells and plays a role in fertilization by modulating hyperactivation, via modulation of key Catsper channels in human spermatozoa.…”

Section: Discussionmentioning

confidence: 78%

Does the Pre-Ovulatory Pig Oviduct Rule Sperm Capacitation In Vivo Mediating Transcriptomics of Catsper Channels?

Martínez

Álvarez‐Rodríguez

Wright

et al. 2020

IJMS

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Spermatozoa need to conduct a series of biochemical changes termed capacitation in order to fertilize. In vivo, capacitation is sequentially achieved during sperm transport and interaction with the female genital tract, by mechanisms yet undisclosed in detail. However, when boar spermatozoa are stored in the tubal reservoir pre-ovulation, most appear to be in a non-capacitated state. This study aimed at deciphering the transcriptomics of capacitation-related genes in the pig pre-ovulatory oviduct, following the entry of semen or of sperm-free seminal plasma (SP). Ex-vivo samples of the utero-tubal junction (UTJ) and isthmus were examined with a microarray chip (GeneChip ® Porcine Gene 1.0 ST Array, Thermo Fisher Scientific) followed by bioinformatics for enriched analysis of functional categories (GO terms) and restrictive statistics. The results confirmed that entry of semen or of relative amounts of sperm-free SP modifies gene expression of these segments, pre-ovulation. It further shows that enriched genes are differentially associated with pathways relating to sperm motility, acrosome reaction, single fertilization, and the regulation of signal transduction GO terms. In particular, the pre-ovulation oviduct stimulates the Catsper channels for sperm Ca 2+ influx, with AKAPs, CATSPERs, and CABYR genes being positive regulators while PKIs and CRISP1 genes appear to be inhibitors of the process. We postulate that the stimulation of PKIs and CRISP1 genes in the pre-ovulation sperm reservoir/adjacent isthmus, mediated by SP, act to prevent premature massive capacitation prior to ovulation.

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Allurin, an Amphibian Sperm Chemoattractant Having Implications for Mammalian Sperm Physiology

Cited by 8 publications

References 217 publications

CRISP1 as a novel CatSper regulator that modulates sperm motility and orientation during fertilization

CRISP1 as a novel CatSper regulator that modulates sperm motility and orientation during fertilization

Protein tyrosine kinase signaling in the mouse oocyte cortex during sperm–egg interactions and anaphase resumption

Does the Pre-Ovulatory Pig Oviduct Rule Sperm Capacitation In Vivo Mediating Transcriptomics of Catsper Channels?

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