Trp2 regulates entry of Ca2+ into mouse sperm triggered by egg ZP3

Jungnickel, Melissa K.; Marrero, Héctor; Birnbaumer, Lutz; Lemos, José R.; Florman, Harvey M.

doi:10.1038/35074570

Cited by 293 publications

(229 citation statements)

References 29 publications

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“…Our studies support the possibility that mTRPC2 clone 14 protein expression is restricted to certain cell types including hematopoietic cells and brain. The plasma membrane localization of mTRPC2 in hematopoietic cells is consistent with current and previous functional results (24,36), which require membrane localization of mTRPC2 for calcium influx. Liman et al (38) also localized rat TRPC2 to the microvillar plasma membrane of VNO receptor neurons.…”

Section: Discussionsupporting

confidence: 77%

“…Their tissue distribution and function has been controversial (24, 34, 36 -38). High expression of mTRPC2 in testis, sperm, and VNO has been reported (24,36,38), but the presence of expressed sequence tags derived from TRPC2 mRNA in kidney (GenBank TM accession number AA473022) and spleen (GenBank TM accession number AA145678) suggests that mTRPC2 may be present in many other tissues but at low levels. Here, using RT-PCR specific for each of the known mTRPC2 isoforms, we identified expression of mTRPC2 ␣ and mTRPC2 clone 14 but not mTRPC2 ␤ or clone 17 in murine hematopoietic cells.…”

Section: Discussionmentioning

confidence: 99%

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Erythropoietin Modulates Calcium Influx through TRPC2

Chu¹,

Cheung

Barber

et al. 2002

Journal of Biological Chemistry

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Section: Discussionsupporting

confidence: 77%

Section: Discussionmentioning

confidence: 99%

Erythropoietin Modulates Calcium Influx through TRPC2

Chu¹,

Cheung

Barber

et al. 2002

Journal of Biological Chemistry

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Section: Signalling Events During Zp-mediated Acrosomal Exocytosismentioning

confidence: 99%

“…36 Mammalian transient receptor potential proteins, which are homologues of the Drosophila melanogaster photoreceptor cell transient receptor potential protein, are involved in the ZP3-mediated capacitative calcium entry in mice. 36 Transient receptor potential homologues have also been located in human sperm. 37,38 In addition, members of soluble Nethyl maleimide-sensitive factor attachment protein receptor proteins present in the acrosome region of mammalian sperm may also facilitate calcium entry, thereby leading to the AR.…”

Section: Signalling Events During Zp-mediated Acrosomal Exocytosismentioning

confidence: 99%

Acrosome reaction: relevance of zona pellucida glycoproteins

Gupta

Bhandari²

2010

Asian J Androl

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During mammalian fertilisation, the zona pellucida (ZP) matrix surrounding the oocyte is responsible for the binding of the spermatozoa to the oocyte and induction of the acrosome reaction (AR) in the ZP-bound spermatozoon. The AR is crucial for the penetration of the ZP matrix by spermatozoa. The ZP matrix in mice is composed of three glycoproteins designated ZP1, ZP2 and ZP3, whereas in humans, it is composed of four (ZP1, ZP2, ZP3 and ZP4). ZP3 acts as the putative primary sperm receptor and is responsible for AR induction in mice, whereas in humans (in addition to ZP3), ZP1 and ZP4 also induce the AR. The ability of ZP3 to induce the AR resides in its C-terminal fragment. O-linked glycans are critical for the murine ZP3-mediated AR. However, N-linked glycans of human ZP1, ZP3 and ZP4 have important roles in the induction of the AR. Studies with pharmacological inhibitors showed that the ZP3-induced AR involves the activation of the G i -coupled receptor pathway, whereas ZP1-and ZP4-mediated ARs are independent of this pathway. The ZP3-induced AR involves the activation of T-type voltage-operated calcium channels (VOCCs), whereas ZP1-and ZP4-induced ARs involve both T-and L-type VOCCs. To conclude, in mice, ZP3 is primarily responsible for the binding of capacitated spermatozoa to the ZP matrix and induction of the AR, whereas in humans (in addition to ZP3), ZP1 and ZP4 also participate in these stages of fertilisation. Keywords: acrosome reaction; fertilisation; oocyte; signalling pathways; spermatozoa; zona pellucida glycoproteins INTRODUCTION Mammalian fertilisation is a highly synchronized process that involves a complex series of interactions between the spermatozoon and the egg, culminating in their unison. The initial steps in fertilisation involves the binding of the spermatozoon to the zona pellucida (ZP) matrix surrounding the egg, followed by induction of the acrosome reaction (AR) in the zona-bound spermatozoon, a pre-requisite for penetration of the ZP matrix by the spermatozoon. The spermatozoon acrosome is a Golgi-derived organelle that forms a cap over the anterior two-thirds of its nucleus. The AR involves the fusion of the sperm membrane with the outer acrosomal membrane, resulting in release of the acrosomal contents and exposure of the inner acrosomal membrane on the anterior head of the spermatozoon. Various physiological agents, such as progesterone, serum albumin, follicular fluid, hormones (including biogenic amines), hydrolytic enzymes (particularly proteases), hyaluronic acid and ZP glycoproteins, have been implicated in the induction of the AR. [1][2][3] In the present paper, we review the role of the ZP matrix and its constituents in AR induction. Various downstream signalling pathways involved in the ZP glycoprotein-induced AR will also be discussed. On the basis of the current literature and studies from our group, the salient differences in the ZP glycoprotein-mediated induction of the AR in mouse versus human will be highlighted.

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“…TRP channels are also known to play a role in regulating sperm motility, but spe-41/trp-3 mutant sperm do not have any detectable defects in motility or migratory behavior (39,40). In mammalian sperm, calcium influx is associated with the regulation of membrane fusion events (41). Therefore, the defect in calcium influx may result in a defect in sperm-oocyte fusion.…”

Section: Fertilizationmentioning

confidence: 99%

Fertilization and the oocyte-to-embryo transition in C. elegans

Marcello¹,

Singson²

2010

BMB Reports

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Fertilization is a complex process comprised of numerous steps. During fertilization, two highly specialized and differentiated cells (sperm and egg) fuse and subsequently trigger the development of an embryo from a quiescent, arrested oocyte. Molecular interactions between the sperm and egg are necessary for regulating the developmental potential of an oocyte, and precise coordination and regulation of gene expression and protein function are critical for proper embryonic development. The nematode Caenorhabditis elegans has emerged as a valuable model system for identifying genes involved in fertilization and the oocyte-to-embryo transition as well as for understanding the molecular mechanisms that govern these processes. In this review, we will address current knowledge of the molecular underpinnings of gamete interactions during fertilization and the oocyte-to-embryo transition in C. elegans. We will also compare our knowledge of these processes in C. elegans to what is known about similar processes in mammalian, specifically mouse, model systems. [BMB reports 2010; 43(6): 389-399]

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Trp2 regulates entry of Ca2+ into mouse sperm triggered by egg ZP3

Cited by 293 publications

References 29 publications

Erythropoietin Modulates Calcium Influx through TRPC2

Erythropoietin Modulates Calcium Influx through TRPC2

Acrosome reaction: relevance of zona pellucida glycoproteins

Fertilization and the oocyte-to-embryo transition in C. elegans

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