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

Xu, Huiling; Liu, Fang; Srakaew, Nopparat; Koppisetty, Chaitanya A. K.; Nyholm, Per-Georg; Carmona, Eurı́dice; Tanphaichitr, Nongnuj

doi:10.1530/rep-11-0338

Cited by 17 publications

(30 citation statements)

References 62 publications

(117 reference statements)

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“…Arylsulfatase A (ARSA), sperm surface protein, is obtained by epididymal transit and remains on the cell surface during capacitation . ARSA seems to bind to mouse ZP receptor 2 (mZP2) and mouse ZP receptor 3 (mZP3) . In addition, we found a tetraspanin family protein (CD9) that has only recently been described in mouse sperm.…”

Section: Discussionmentioning

confidence: 74%

Bovine sperm plasma membrane proteomics through biotinylation and subcellular enrichment

et al. 2015

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A significant proportion of mammalian fertilization is mediated through the proteomic composition of the sperm surface. These protein constituents can present as biomarkers to control and regulate breeding of agricultural animals. Previous studies have addressed the bovine sperm cell apical plasma membrane (PM) proteome with nitrogen cavitation enrichment. Alternative workflows would enable to expand the compositional data more globally around the entire sperm's surface. We used a cell surface biotin-labeling in combination with differential centrifugation to enrich sperm surface proteins. Using nano-LC MS/MS, 338 proteins were confidently identified in the PM-enriched proteome. Functional categories of sperm-egg interaction, protein turnover, metabolism as well as molecular transport, spermatogenesis, and signal transduction were represented by proteins with high quantitative signal in our study. A highly significant degree of enrichment was found for transmembrane and PM-targeted proteins. Among them, we also report proteins previously not described on bovine sperm (CPQ, CD58, CKLF, CPVL, GLB1L3, and LPCAT2B) of which CPQ and CPVL cell surface localization was further validated. A descriptive overview of the bovine sperm PM integral and peripheral proteins is provided to complement future studies on animal reproduction and its relation to sperm cell surface. All MS data have been deposited in the ProteomeXchange with identifier PXD001096 (http://proteomecentral.proteomexchange.org/dataset/PXD001096).

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Section: Discussionmentioning

confidence: 74%

Bovine sperm plasma membrane proteomics through biotinylation and subcellular enrichment

et al. 2015

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“…Electrostatic analyses of the structural characteristics of ARSA have revealed the presence of an additional domain adjacent to the active site that could account for the ability of the enzyme to bind to the ZP when the active site being concurrently occupied with alternate substrates (Schenk et al, 2009). Furthermore, recent studies have indicated that mutation of the active site does not inhibit the ability of ARSA to bind to mouse ZP2 and ZP3 (Xu et al, 2012). The more modest reduction in sperm -ZP binding observed after incubation of human spermatozoa with anti-SPAM1 antibodies (Fig.…”

Section: Discussionmentioning

confidence: 99%

Investigation of the mechanisms by which the molecular chaperone HSPA2 regulates the expression of sperm surface receptors involved in human sperm-oocyte recognition

Redgrove

Anderson²,

McLaughlin³

et al. 2012

Molecular Human Reproduction

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A unique characteristic of mammalian spermatozoa is that, upon ejaculation, they are unable to recognize and bind to an ovulated oocyte. These functional attributes are only realized following the cells' ascent of the female reproductive tract whereupon they undergo a myriad of biochemical and biophysical changes collectively referred to as 'capacitation'. We have previously shown that this functional transformation is, in part, engineered by the modification of the sperm surface architecture leading to the assembly and/or presentation of multimeric sperm -oocyte receptor complexes. In this study, we have extended our findings through the characterization of one such complex containing arylsulfatase A (ARSA), sperm adhesion molecule 1 (SPAM1) and the molecular chaperone, heat shock 70kDa protein 2 (HSPA2). Through the application of flow cytometry we revealed that this complex undergoes a capacitation-associated translocation to facilitate the repositioning of ARSA to the apical region of the human sperm head, a location compatible with a role in the mediation of sperm -zona pellucida (ZP) interactions. Conversely, SPAM1 appears to reorient away from the sperm surface, possibly reflecting its primary role in cumulus matrix dispersal preceding sperm -ZP recognition. The dramatic relocation of the complex was completely abolished by incubation of capacitating spermatozoa in exogenous cholesterol or broad spectrum protein kinase A (PKA) and tyrosine kinase inhibitors suggesting that it may be driven by alterations in membrane fluidity characteristics and concurrently by the activation of a capacitation-associated signal transduction pathway. Collectively these data afford novel insights into the sub-cellular localization and potential functions of multimeric protein complexes in human spermatozoa.

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“…In an alternate experiment, immunofluorescence of CLU was performed on sperm that were bound to the zona(e) pellucida(e) (ZP) layer coated onto the surface of a glass slide. ZP used in this experiment were prepared from mouse ovaries as previously described (Xu et al 2012) and heat solubilized in 0.2 M sodium phosphate buffer, pH 6.8 at two ZP/µL. The solubilized ZP solution was plated into the middle of the well of a Thermo Scientific 8-well Diagnostic glass slide (Thermo Fisher Scientific) and allowed to air-dry.…”

Section: Immunofluorescence Localization Of Clu and Sed1 On Spermmentioning

confidence: 99%

Clusterin in the mouse epididymis: possible roles in sperm maturation and capacitation

Saewu¹,

Kadunganattil²,

Raghupathy³

et al. 2017

Reproduction

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Clusterin (CLU) is known as an extracellular chaperone for proteins under stress, thus preventing them from aggregation and precipitation. We showed herein that CLU, expressed by principal cells of the mouse caput epididymis, was present in high amounts in the lumen. In the cauda epididymis, CLU bound tightly to the sperm head surface and its amount on total sperm was similar to that in the bathing luminal fluid. In both immotile and motile caudal epididymal sperm, CLU was localized over the entire sperm head except at the convex ridge, although in the motile sperm population, the CLU immunofluorescence pattern was distinctively mottled with a lower intensity. However, when motile sperm became capacitated, CLU was relocalized to the head hook region, with immunofluorescence intensity being higher than that on the non-capacitated counterparts. Under a slightly acidic pH of the epididymal lumen, CLU may chaperone some luminal proteins and deliver them onto the sperm surface. Immunoprecipitation of epididymal fluid proteins indicated that CLU interacted with SED1, an important egg-binding protein present in a high amount in the epididymal lumen. In a number of non-capacitated sperm, fractions of SED1 and CLU co-localized, but after capacitation, SED1 and CLU dissociated from one another. While CLU moved to the sperm head hook, SED1 translocated to the head convex ridge, the egg-binding site. Overall, CLU localization patterns can serve as biomarkers of immotile sperm, and non-capacitated and capacitated sperm in mice. The chaperone role of CLU may also be important for sperm maturation and capacitation.

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

Cited by 17 publications

References 62 publications

Bovine sperm plasma membrane proteomics through biotinylation and subcellular enrichment

Bovine sperm plasma membrane proteomics through biotinylation and subcellular enrichment

Investigation of the mechanisms by which the molecular chaperone HSPA2 regulates the expression of sperm surface receptors involved in human sperm-oocyte recognition

Clusterin in the mouse epididymis: possible roles in sperm maturation and capacitation

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