Isolation and characterization of the pig endometrial arylsulphatase A.

Hamid, Rizwan; Srivastava, Pranay

doi:10.1042/bj2110649

Cited by 14 publications

(4 citation statements)

References 40 publications

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“…In somatic cells, ARSA acts as a lysosomal enzyme that has the ability to desulfate various arylsulfates including the natural substrates of sulfogalactosylglycerolipid and sulfogalactosylcerebroside, in addition to a variety of small artificial substrates such as P-nitrocatechol sulfate and P-nitrophenylsulfate (Mehl and Jatzkewitz, 1968;Rahi and Srivastava, 1983). In addition to well-documented roles in the regulation of myelin sheath deposition in the central nervous system (Eckhardt, 2008), ARSA has also been identified within the acrosome of sperm from a variety of species including boar (Dudkiewicz, 1984;Tanphaichitr et al, 1998), mouse (Tanphaichitr et al, 1990;White et al, 2000;Tantibhedhyangkul et al, 2002;Weerachatyanukul et al, 2003) and human Tantibhedhyangkul et al, 2002).…”

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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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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“…Fish ARSA apparently does not display this aggregation phenomenon . However, recent studies of mammalian ARSA indicate that the enzyme is synthesized as a 63-kDa precursor which is processed and dimerized into the mature "monomer" reported in earlier studies (Rahi and Srivastava, 1983;. It is plausible that the fish enzyme may also consist of two identical or very similar subunits.…”

Section: Discussionmentioning

confidence: 95%

Arylsulfatase and beta-glucuronidase expression in green sunfish, bluegill, and their reciprocal interspecific hybrids

Daniel

Kahle

1989

Biochem Genet

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Fish arylsulfatases (arylsulfate sulfohydrolase; EC 3.1.6.1) were resolved into cationic arylsulfatase A-like (ARSA) and anionic arylsulfatase B-like (ARSB) fractions by DEAE-Sephacel chromatography. Green sunfish (GSF) hepatic ARSA was more acidic and more thermostable than bluegill (BG) ARSA. GSF x BG interspecific hybrids preferentially expressed GSF ARSA, while BG x GSF hybrids appeared to produce a dimeric enzyme consisting of both GSF and BG ARSA polypeptides. GSF hepatic beta-glucuronidase (GUS) also proved to be more thermostable than BG GUS. Thermostabilities of GUS produced by reciprocal interspecific hybrids were very similar to that of GSF GUS. Either GSF GUS is preferentially expressed in both interspecific hybrids or both the GSF and BG GUS polypeptides are synthesized in comparable amounts, and the GSF GUS polypeptide sufficiently stabilizes the heterotetramers produced by the hybrids to produce denaturation profiles closely approximating that of the GSF enzyme.

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“…Interestingly, AS-A has been shown to exist in a multimeric form (i.e., a dimer at physiological pH and an octomer at an acidic pH [16,35,36]). At 63 nM, AS-A was, in fact, a dimer.…”

Section: Discussionmentioning

confidence: 99%

“…The enzyme is known to exist as a dimer at the neutral pH and as an octomer at an acidic pH [16,35,36]. To test whether AS-A at 63 nM manifested as a multimer in our treatment condition, the enzyme was subjected to gel filtration at neutral pH using Sephadex G-100 resin, to which the proteins of molecular masses lower than 100 kDa are restrained.…”

Section: Premature Acrosome Reaction Occurred As a Consequence Of Spementioning

confidence: 99%

Binding of Arylsulfatase A to Mouse Sperm Inhibits Gamete Interaction and Induces the Acrosome Reaction1

Carmona¹,

Weerachatyanukul²,

Xu³

et al. 2002

Biology of Reproduction

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We have shown previously that male germ cell-specific sulfoglycolipid, sulfogalactosylglycerolipid (SGG), is involved in sperm-zona pellucida binding, and that SGG and its desulfating enzyme, arylsulfatase A (AS-A), coexist in the same sperm head area. However, AS-A exists at a markedly low level in sperm as compared to SGG (i.e., 1/400 of SGG molar concentration). In the present study, we investigated whether perturbation of this molar ratio would interfere with sperm-egg interaction. We demonstrated that purified AS-A bound to the mouse sperm surface through its high affinity with SGG. When capacitated, Percoll gradient-centrifuged mouse sperm were treated for 1 h with various concentrations of AS-A, their binding to zona-intact eggs was inhibited in a dose-dependent manner and reached the background level with 63 nM AS-A. This inhibition could be partially explained by an increase in premature acrosome reaction. The acrosome-reacted sperm population of the 63 nM AS-A-treated sperm sample was twice that of the control sample (treated with 63 nM ovalbumin) at 1 h (i.e., 32% vs. 15%) and rose to 53% at 2 h. This induction was presumably due to SGG aggregation attributed to AS-A, existing as a dimer at neutral pH, and could be mimicked by anti-SGG immunoglobulin (Ig) G/IgM + secondary IgG antibody. Drastic inhibition (75%) of in vivo fertilization was also observed in females inseminated with sperm suspension containing 630 nM AS-A as compared to the rate in females inseminated with sperm suspension included with 630 nM ovalbumin. Our results demonstrate a promising potential for AS-A as a nonhormonal, vaginal contraceptive.

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Isolation and characterization of the pig endometrial arylsulphatase A.

Cited by 14 publications

References 40 publications

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

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

Arylsulfatase and beta-glucuronidase expression in green sunfish, bluegill, and their reciprocal interspecific hybrids

Binding of Arylsulfatase A to Mouse Sperm Inhibits Gamete Interaction and Induces the Acrosome Reaction1

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