The role of the acrosomal matrix in fertilization

Buffone, Mariano G.; Foster, James A.; Gerton, George L.

doi:10.1387/ijdb.072532mb

Cited by 112 publications

(116 citation statements)

References 122 publications

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“…Since the intra-acrosomal pH is between 5.3 and 6.2 (Nakanishi et al 2001), ASA in the AC should exist in the oligomeric form of a size in between a dimer and an octamer. The oligomeric forms of ASA, like those of sp56, another acrosomal protein with ZP binding ability, would likely exist as scaffolds beneficial for the interaction between acrosome reacting sperm and the ZP (Buffone et al 2008a(Buffone et al , 2008b. Previous studies of Wassarman and colleagues.…”

Section: Discussionmentioning

confidence: 99%

“…Once mZP2 is cleaved at Ala166 to form mZP2 f , as occurring after fertilization (Burkart et al 2012), the ZP matrix becomes refractory to sperm binding (Florman & Ducibella 2006). Accumulated evidence also reveals the participation of acrosomal matrix proteins in ZP binding, a basis for how acrosome reacting sperm remain bound to the ZP (Kim & Gerton 2003, Buffone et al 2008a, 2008b. Proacrosin is an example of these acrosomal proteins, and it has affinity for both mZP2 and mZP3 (Howes et al 2001).…”

Section: Introductionmentioning

confidence: 99%

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Sperm arylsulfatase A binds to mZP2 and mZP3 glycoproteins in a nonenzymatic manner

Xu¹,

Liu²,

Srakaew³

et al. 2012

Reproduction

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We have shown previously that sperm surface arylsulfatase A (ASA) of mouse, pig, and human is involved in sperm-egg zona pellucida (ZP) binding. By treating capacitated mouse sperm with A23187 to induce the acrosome reaction, we demonstrated by immunoblotting that ASA also existed in the acrosomal content and on the inner acrosomal membrane. Since mZP2 and mZP3 are known as sperm receptors, whereas mZP1 as a cross-linker of mZP2/mZP3, we determined whether purified ASA bound to mZP2 and mZP3 selectively. The three mZP glycoproteins were purified from solubilized ovarian ZP by size exclusion column chromatography. Immuno-dot blot analyses revealed that purified sperm ASA bound to mZP2 at the highest level followed by mZP3, whereas the binding of ASA to mZP1 was minimal. The results confirmed the physiological significance of sperm ASA in the ZP binding process. The binding of ASA to mZP2 and mZP3 was, however, not dependent on the active site pocket amino acids, Cys69, Lys123, and Lys302, which are pertinent to the capturing of an arylsulfate substrate, since ASA mutant with Ala substitution at these three residues still bound to mZP2 and mZP3. The availability of the active site pocket of ASA bound to the ZP suggested that ASA would still retain enzymatic activity, which might be important for subsequent sperm penetration through the ZP.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Sperm arylsulfatase A binds to mZP2 and mZP3 glycoproteins in a nonenzymatic manner

Xu¹,

Liu²,

Srakaew³

et al. 2012

Reproduction

View full text Add to dashboard Cite

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“…Perhaps reflecting a reorganization of its content (Yoshinaga & Toshimori 2003, Olsen et al 2004, Buffone et al 2008, although not visible in the rat or in man, this has been observed in the guinea pig, chinchilla, loris, rhesus monkey, rabbit, hyrax and white-tailed rat (Mystromys albicaudatus). As noted, the eutherian acrosome is not merely a bag of enzymes in that the fenestrated carapace usually first tethers the sperm head to the zona.…”

Section: Sperm Maturationmentioning

confidence: 96%

Singular features of fertilization and their impact on the male reproductive system in eutherian mammals

Bedford

2014

Reproduction

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Therian (marsupial and eutherian) mammals have evolved a suite of novel reproductive features -seen variously in their gametes, the steps of fertilization and the male reproductive tract -whose adaptive significance remains unclear. Present evidence for the betterunderstood eutherian mammals suggests that the 'prime mover' in their evolution has been the character of the egg coat, with other such features being adaptations to the consequences of this. Its elastic thickness allows the zona pellucida to stretch to a variable degree and yet remain around the blastocyst during much or all of its expansion before implantation, but its character represents an unusual challenge for spermatozoa. Novel aspects of the acrosome related to this challenge enable it to maintain a relatively prolonged binding after the onset of the acrosome reaction, and the structure, shape and behaviour of the sperm head point to physical thrust as a major element of zona penetration -with the unique configuration of gamete fusion as a sequela of this strategy. In the male, such adaptations are reflected in sperm head formation in the testis and in sperm maturation in the epididymis involving at least the sperm head's structure, plasmalemma and acrosome. This complexity allied to a slow epididymal sperm transport, a relatively modest sperm production and the brief life span of mature spermatozoa kept above the cauda epididymidis could account for the evolution of the sperm storage function -a development seemingly linked, in turn, to the need for sperm capacitation and scrotal evolution.Reproduction (2014) 147 R43-R52

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“…The now exposed intra-acrosomal layer of proteins consists of an array of proteins that interact with the zona pellucida (for review see [7]). This so-called secondary zona binding was thought to be specific to ZP2 [66][67][68] but recently it has been shown that the intra-acrosomal protein sp56 binds to ZP3 [4,12].…”

Section: Zona Penetration After the Acrosome Reactionmentioning

confidence: 99%

“…The acrosome exocytosis is a multipoint membrane fusion event between the sperm plasma membrane and the outer acrosomal membrane (see Fig. 5.1 [8,9]) and the exposed acrosomal content is required for sperm to penetrate the zona pellucida [10][11][12]. This so-called zona drilling effectively takes place because the sperm at this stage also has acquired hyperactivated motility [13].…”

mentioning

confidence: 99%

Membrane Fusions During Mammalian Fertilization

Gadella

Evans

2011

Advances in Experimental Medicine and Biology

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Successful completion of fertilization in mammals requires three different types of membrane fusion events. Firstly, the sperm cell will need to secrete its acrosome contents (acrosome exocytosis; also known as the acrosome reaction); this allows the sperm to penetrate the extracellular matrix of the oocyte (zona pellucida) and to reach the oocyte plasma membrane, the site of fertilization. Next the sperm cell will bind and fuse with the oocyte plasma membrane (also known as the oolemma), which is a different type of fusion in which two different cells fuse together. Finally, the fertilized oocyte needs to prevent polyspermic fertilization, or fertilization by more than one sperm. To this end, the oocyte secretes the contents of cortical granules by exocytotic fusions of these vesicles with the oocyte plasma membrane over the entire oocyte cell surface (also known as the cortical reaction or cortical granule exocytosis). The secreted cortical contents modify the zona pellucida, converting it to a state that is unreceptive to sperm, constituting a block to polyspermy. In addition, there is a block at the level of the oolemma (also known as the membrane block to polyspermy). IntroductionFertilization of the oocyte involves three membrane fusion events [1] namely, (1) a preparative series of secretion membrane fusions at the apical sperm surface known as acrosome exocytosis [2]. The membrane fusions are induced when the sperm cell binds to specific zona binding proteins at the sperm surface [3][4][5][6][7]. The acrosome exocytosis is a multipoint membrane fusion event between the sperm plasma membrane and the outer acrosomal membrane (see Fig. 5.1 [8,9]) and the exposed acrosomal content is required for sperm to penetrate the zona pellucida [10][11][12]. This so-called zona drilling effectively takes place because the sperm at this stage also has acquired hyperactivated motility [13]. (2) After zona penetration the sperm enters the perivitelline space where it can bind and fuse with the oocyte plasma membrane [14,15]. This is the actual fertilization fusion in which the contents of the sperm are delivered into the oocyte cytoplasm. The plasma membrane of the equatorial segment (see Fig. 5.1) is the site where proteins are located that orchestrate sperm-oocyte binding and fusion [16]. (3) In order to prevent polyspermy the oocyte has to activate defense systems to block redundant sperm-oocyte fusion [17]. To this end the first fertilizing sperm delivers activation factors

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The role of the acrosomal matrix in fertilization

Cited by 112 publications

References 122 publications

Sperm arylsulfatase A binds to mZP2 and mZP3 glycoproteins in a nonenzymatic manner

Sperm arylsulfatase A binds to mZP2 and mZP3 glycoproteins in a nonenzymatic manner

Singular features of fertilization and their impact on the male reproductive system in eutherian mammals

Membrane Fusions During Mammalian Fertilization

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