The sperm chemoattractant “allurin” is expressed and secreted from the Xenopus oviduct in a hormone-regulated manner

Xiang, Xueyu; Burnett, Lindsey A.; Rawls, Alan; Bieber, Allan L.; Chandler, Douglas E.

doi:10.1016/j.ydbio.2004.08.011

Cited by 34 publications

(36 citation statements)

References 58 publications

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“…However, it is not without precedent. Allurin, which is a non-CRISP CAP, is produced by the oviductal secretory epithelium within Xenopus where it permeates the egg jelly and subsequently establishes a diffusion gradient and acts as a sperm chemoattractant (Olson et al, 2001;Xiang et al, 2004;Burnett et al, 2008). The mechanism through which allurin has a chemoattractant activity is currently unknown.…”

Section: Discussionmentioning

confidence: 99%

Cysteine‐rich secretory proteins are not exclusively expressed in the male reproductive tract

Reddy¹,

Gibbs²,

Merriner³

et al. 2008

Developmental Dynamics

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The Cysteine-RIch Secretory Proteins (CRISPs) are abundantly produced in the male reproductive tract of mammals and within the venom of reptiles and have been shown to regulate ion channel activity. CRISPs, along with the Antigen-5 proteins and the Pathogenesis related-1 (Pr-1) proteins, form the CAP superfamily of proteins. Analyses of EST expression databases are increasingly suggesting that mammalian CRISPs are expressed more widely than in the reproductive tract. We, therefore, conducted a reverse transcription PCR expression profile and immunohistochemical analyses of 16 mouse tissues to define the sites of production of each of the four murine CRISPs. These data showed that each of the CRISPs have distinct and sometimes overlapping expression profiles, typically associated with the male and female reproductive tract, the secretory epithelia of exocrine glands, and immune tissues including the spleen and thymus. These investigations raise the potential for a role for CRISPs in general mammalian physiology. Developmental Dynamics 237:3313-3323, 2008.

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Section: Discussionmentioning

confidence: 99%

Cysteine‐rich secretory proteins are not exclusively expressed in the male reproductive tract

Reddy¹,

Gibbs²,

Merriner³

et al. 2008

Developmental Dynamics

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“…At spawning, these peptides diffuse into the seawater and can activate motility in swimming sperm (Suzuki et al, 1981;Hansbrough and Garbers, 1981) and also act as a chemoattractant (Ward et al, 1985). In Xenopus, allurin, an unglycosylated, heat-stable 21-kDa protein, localizes in the outer layers of the egg-jelly as a sperm chemoattractant (Olson et al, 2001;Xiang et al, 2004). Although the molecular features and the localization of allurin in Xenopus egg-jelly seem to be similar to those of the newt SMIS (Mizuno et al, 1999;Figs.…”

Section: A B C Dmentioning

confidence: 99%

Identification of the sperm motility-initiating substance in the newt, Cynops pyrrhogaster, and its possible relationship with the acrosome reaction during internal fertilization

Watanabe¹,

Kubo²,

Takeshima³

et al. 2010

Int. J. Dev. Biol.

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Motility initiation is a key event during internal fertilization of female-stored sperm, although the underlying mechanisms remain unclear. In internally fertilizing urodeles, quiescent sperm initiate motility on the surface of the egg-jelly, a thick extracellular matrix that accumulates around the egg in oviduct. By immunizing mice with egg-jelly extracts, we successfully generated an α34 monoclonal antibody (mAb) which neutralized sperm motility-initiating activity in the eggjelly of the newt, Cynops pyrrhogaster, in a dose-dependent manner. The α34 mAb recognized an unglycosylated 34 kDa protein in the outermost of the six layers that comprise egg-jelly. Under nonreducing conditions, immunoblotting with α34 mAb produced many bands in addition to the 34 kDa protein, suggesting that the 34 kDa protein associates not only with the jelly matrix itself, but also with additional substances present in the matrix. Our current results are compatible with the supposed features of sperm motility-initiating substance (SMIS), indicating that the 34 kDa protein itself, or a complex consisting of the 34 kDa protein and some other molecules, is the SMIS in C. pyrrhogaster. Immunofluorescence staining further indicated that SMIS was distributed in a dot-like pattern in the outermost jelly layer and was fully covered with acrosome reactioninducing substance (ARIS). Immunocytochemical and scanning electron microscopic examinations of the outermost jelly layer strongly suggests that the 34 kDa protein localized in granules (2 μm) and that ARIS was distributed covering the granules and in the sheet-like structure above the granules. These data suggest that the initiation of sperm motility is mediated by the acrosome reaction.

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“…In amphibians, allurin, a member of the CRISP family proteins, is expressed in the oviduct (Al-Anzi and Chandler, 1998;Olson et al, 2001;Xiang et al, 2004). This protein is accumulated as a jelly component and diffuses into the medium to attract spermatozoa (Xiang et al, 2004).…”

Section: Cysteine Rich Secretory Proteins (Crisps)mentioning

confidence: 99%

In silico identification of the genes for sperm-egg interaction in the internal fertilization of the newt Cynops pyrrhogaster

Watanabe¹,

Takayama‐Watanabe²

2014

Int. J. Dev. Biol.

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A specific sperm-egg interaction in the oviductal matrix is crucial for internal fertilization of the red-bellied newt, Cynops pyrrhogaster. An understanding of the molecular basis of this interaction is expected to elucidate the evolutionary history of internal fertilization in amphibians. Recently, deep sequencing technology has provided global gene information even in nonmodel animals, allowing us to understand specific features of the molecular mechanisms underlying fertilization in C. pyrrhogaster. In the present study, we screened de novo assembled RNAseq from ovary, testis, and oviduct samples in C. pyrrhogaster and identified the base sequences encoding zona pellucida (ZP) proteins, voltage-dependent Ca 2+ channels, and cysteine-rich secretory proteins (CRISPs), which respectively are sperm receptors for egg envelopes, major mediators of sperm intracellular signaling, and expected extracellular modulators for sperm function in the female reproductive tract. In the ovary, ZP homologues of all six subgroups were found, including a ZP1 homologue that was newly found in amphibians, a ZP4 homologue, and six ZPC homologues. The unique combination of ZP proteins suggests a new mechanism for sperm binding to egg envelopes in the internal fertilization of C. pyrrhogaster. In the testis, CaV1.1, 1.2, and 3.2, which are L-and T-type voltage-dependent Ca 2+ channels, were found as potential mediators for the internal fertilization-specific sperm-egg interaction. We also found CRISP 2 in the oviduct, which is speculated to participate in the sperm-egg interaction. These results indicate that the de novo assembled RNAseq is a powerful tool allowing analysis of the specific sperm-egg interactions in C. pyrrhogaster.

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The sperm chemoattractant “allurin” is expressed and secreted from the Xenopus oviduct in a hormone-regulated manner

Cited by 34 publications

References 58 publications

Cysteine‐rich secretory proteins are not exclusively expressed in the male reproductive tract

Cysteine‐rich secretory proteins are not exclusively expressed in the male reproductive tract

Identification of the sperm motility-initiating substance in the newt, Cynops pyrrhogaster, and its possible relationship with the acrosome reaction during internal fertilization

In silico identification of the genes for sperm-egg interaction in the internal fertilization of the newt Cynops pyrrhogaster

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