Hamster Zona Pellucida Is Formed by Four Glycoproteins: ZP1, ZP2, ZP3, and ZP4

Izquierdo-Rico, M. J.; Jiménez-Movilla, María; Llop, Esther; Oliva, Alfonso; Ballesta, José Antonio Camacho; Gutiérrez-Gallego, Ricardo; Jiménez‐Cervantes, Celia; Avilés, Manuel

doi:10.1021/pr800568x

Cited by 52 publications

(39 citation statements)

References 58 publications

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“…However, the ZP matrices of rats, hamsters, bonnet monkeys and humans are composed of four glycoproteins: ZP1, ZP2, ZP3 and ZP4. [8][9][10][11][12][13] In humans, ZP1 has a 638-aa polypeptide backbone; ZP2 has 745 aa; ZP3 has 424 aa and ZP4 has 540 aa. The ZP glycoproteins are heavily glycosylated and have N-as well as O-linked glycans, which have crucial roles in the spermatozoon-ZP interaction and AR induction.…”

Section: Composition Of the Zp Matrixmentioning

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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Section: Composition Of the Zp Matrixmentioning

confidence: 99%

Acrosome reaction: relevance of zona pellucida glycoproteins

Gupta

Bhandari²

2010

Asian J Androl

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“…Although the extracellular coats may be removed in some animals without inhibiting fertilization and these initial gamete interactions may be bypassed by micro-injecting the spermatozoon directly into the oocyte, these events cannot and are not bypassed in nature. The zona pellucida composed of several glycoproteins (ZP) that differ in number between species [4,38,42,57,79,106] serves to modulate sperm binding and to protect the embryo during early development. Whether or not mammalian spermatozoa respond to chemotactic stimuli is very much open to debate [110]; however there is data to suggest that an odorant receptor gene expressed in the testis may be involved in sperm chemotaxis in humans [90,105].…”

Section: Sperm-oocyte Interaction In Mammalsmentioning

confidence: 99%

“…Progression through the outer layers of the oocyte depends on successive molecular interactions that change sperm physiology step-by step promoting fertilization competence. Although there is much information in the literature on the genetics and biochemistry of the outer layers, in particular the zona pellucida [4,38,42,57,79,106], we know little about their topographical constitution and if indeed sperm entry is piloted to a specific site. Recently chemical modulation of the zona by oviductal-specific glycoproteins before the oocyte encounters the spermatozoon has been described and this may also be involved in the fine tuning of sperm-oocyte interactions in mammals [14,15].…”

Section: Sperm-oocyte Interaction In Mammalsmentioning

confidence: 99%

Polyspermy prevention: facts and artifacts?

Dale¹,

DeFelice

2010

J Assist Reprod Genet

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The purpose of this review is to open a debate as to whether or not oocytes actively repel supernumerary sperm or in nature final sperm : oocyte ratios are so low that polyspermy preventing mechanisms are not necessary. Before encountering the oocyte, spermatozoa need to be primed, either by environmental factors as in animals exhibiting external fertilization, or by factors from the female reproductive tract, as in mammals. The spermatozoon must then recognize and interact with the outer layers of the oocyte and progression of the fertilizing spermatozoon through these layers is further controlled and modulated by a precise sequence of signals in situ. Removal of these outer coats may not inhibit fertilization, however does interfere with the dynamics of sperm-oocyte interaction. We propose that monospermy in mammals and sea urchins, under natural conditions, is ensured by the controlled and gradual encounter of a minimum number of spermatozoa with the oocyte and that fine tuning is ensured by the structural and molecular organization of the oocyte and its surrounding coats. We suggest that laboratory experiments using oocytes deprived of their investments and exposed to unnaturally high concentrations of spermatozoa are artifactual and argue that the conclusions leading to the hypothesis of a fast electrical block to polyspermy are unfounded. Under laboratory conditions the majority of spermatozoa, although motile and capable of attaching to the oocyte surface, are either physiologically incompetent or attach to areas of the oocyte surface that do not support entry.

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“…This matrix is composed of three or four glycoproteins (i.e. ZP1, ZP2, ZP3, and ZP4) in mammalian species (Lefievre et al 2004, Hoodbhoy et al 2005, Litscher & Wassarman 2007, Ganguly et al 2008, Izquierdo-Rico et al 2009). In the case of non-mammalian vertebrates such as amphibians (i.e.…”

Section: Introductionmentioning

confidence: 99%

Sperm acrosin is responsible for the sperm binding to the egg envelope during fertilization in Japanese quail (Coturnix japonica)

Sasanami

Yoshizaki²,

Dohra³

et al. 2011

Reproduction

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An antibody library against quail sperm plasma membrane components was established and a mAb, which strongly inhibits sperm perforations of the perivitelline membrane (PVM) was obtained from the library. The antigen molecule of the mAb showed an apparent molecular weight of 45 kDa, and was distributed both on the surface and in the acrosomal matrix of the sperm head. Periodate oxidation revealed that the epitope of the antigen includes a sugar moiety. Tandem mass spectrometry analysis of the antigen revealed that the mAb recognizes sperm acrosin. When sodium dodecyl sulfate-solubilized PVM immobilized on a polyvinylidene difluoride membrane was incubated with sperm plasma membrane lysates, the sperm acrosin was detected on the PVM immobilized on the membrane, indicating that the sperm acrosin interacts with the components of PVM. Indeed, the mAb effectively inhibited the binding of acrosome-intact sperm to the PVM. These results indicate that the 45 kDa sperm acrosin is involved in the binding of sperm to the PVM in fertilization of Japanese quail.

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Hamster Zona Pellucida Is Formed by Four Glycoproteins: ZP1, ZP2, ZP3, and ZP4

Cited by 52 publications

References 58 publications

Acrosome reaction: relevance of zona pellucida glycoproteins

Acrosome reaction: relevance of zona pellucida glycoproteins

Polyspermy prevention: facts and artifacts?

Sperm acrosin is responsible for the sperm binding to the egg envelope during fertilization in Japanese quail (Coturnix japonica)

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