Isolation, characterization and the role of rabbit testicular arysulphatase A in fertilization

Farooqui, Akhlaq A.; Srivastava, Pranay

doi:10.1042/bj1810331

Cited by 47 publications

(23 citation statements)

References 44 publications

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“…However, it has been shown that the arylsulfatases are involved in the degradation of cerebroside sulfate esters, likely membrane components of most target cells. In this regard it is of interest that arylsulfatase from rabbit testes has been reported to disperse the cumulus of rabbit ova, thereby facilitating fertilization (27). The enzyme's role in the attenuation of anaphylaxis is well recognized (19), and a congenital absence of arylsulfatase is the cause for several human genetic disorders (28).…”

Section: -'mentioning

confidence: 99%

Arylsulfatase in natural killer cells: its possible role in cytotoxicity.

Zucker‐Franklin¹,

Grusky²,

Yang³

1983

Proc. Natl. Acad. Sci. U.S.A.

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Ultrastructural cytochemistry of natural killer cells enriched by Percoll gradient centrifugation showed them to possess arylsulfatase (aryl-sulfate sulfohydrolase, EC 3.1.6.1). The enzyme was located in vesicles, granules, and the parallel tubular arrays, organelles characteristic for cytotoxic lymphocytes. Biochemically, peak enzyme activity correlated with the Percoll fractions containing cells with cytotoxicity for melanoma target cells. Treatment of natural killer cells with Na2SO4, a competitive inhibitor of arylsulfatase, suppressed cytotoxicity by almost 50%. Electron microscopy of effector-target cell conjugates, which had been permitted to incubate for only 30 min, disclosed numerous arylsulfatase-positive sites at the points of contact between the effector/target cell membranes. Thus, the enzyme was translocated to the surface before lysis of the target cell was morphologically evident. It is postulated that the parallel tubular arrays play a role in this translocation and that arylsulfatase may function in the degradation of cerebroside sulfate ester components of the target cell membrane to initiate the lytic event.A small subpopulation of peripheral blood lymphocytes is able to kill tumor cells in vivo and in vitro without any prior exposure to the neoplasm. The cells endowed with such ability have been called natural killer (NK) cells and their properties are fairly well defined (1, 2). They are recognized as nonadherent, nonphagocytic, large granular lymphocytes that have receptors for the Fc portion of IgG, a weak affinity for sheep erythrocytes, and an ultrastructural marker, the parallel tubular array (PTA) (3, 4). Monoclonal antisera specific for some of their surface antigens also have been developed (5). It is not known how NK cells select their targets and by what mechanism they inflict their lethal effect. However, physical contact between the effector and target cell appears to be necessary for tumor cell lysis to occur. The remarkable interdigitation between the surface membranes of the conjugated cells also has been illustrated repeatedly (4,6,7). However, because it has not been possible to resolve any membrane damage, even on electron microscopy, it is generally assumed that the biochemical alterations that lead to swelling and subsequent lysis of the target cells are beyond morphologic resolution. This has led to biochemical studies intended to show that proteinases associated with NK cells or secreted by them may be responsible for target cell lysis. Indeed, inhibitors of serine proteinases partially inhibit the NK cell effect (4, 6, 8). In our own hands, inhibitors of trypsin-like enzymes and serine esterases have substantially impaired NK cell function (4). A role for free oxygen radicals generated on cell contact has been suggested by others (9, 10). In addition, the translocation of acid hydrolases has been proposed as a possible mechanism involved in cytotoxicity (6, 7). A group of enzymes not heretofore considered to play a role in target cell lysis are the arylsulfa...

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Section: -'mentioning

confidence: 99%

Arylsulfatase in natural killer cells: its possible role in cytotoxicity.

Zucker‐Franklin¹,

Grusky²,

Yang³

1983

Proc. Natl. Acad. Sci. U.S.A.

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“…The effect of neuraminidase upon the electrofocusing pattern of arylsulfatase B was monitored using Clostridium perfringens neuraminidase (Type VI) (Sigma Chemical Co., St. Louis, Mo.) (Farooqui and Srivastava, 1979).…”

Section: Enzyme Characterizationmentioning

confidence: 99%

Purification and properties of arylsulfatase B from high- and low-activity mouse strains

et al. 1985

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Arylsulfatase B (arylsulfate sulfohydrolase; EC 3.1.6.1) activities in C57BL/6J, SWR/J, and A/J mouse liver approximate a 5:3:1 ratio. Each enzyme was purified to apparent homogeneity, and the properties of the three purified enzymes were compared. The purified enzyme behaved as a monomer with an apparent molecular weight of 50,000. The purified enzyme catalyzed the hydrolysis of p-nitrocatechol sulfate (pNCS), 4-methylumbelliferyl sulfate (4MUS), and chondroitin-4-sulfate (C4S) heptasaccharide. Purified SWR/J arylsulfatase B possessed a higher relative electrophoretic mobility at pH 4.0 than the A/J and C57BL/6J isozymes, and the SWR/J enzyme was more thermostable than either the C57BL/6J or the A/J enzyme. No differences were observed among the three enzymes with respect to their Michaelis constants for 4MUS and pNCS, isoelectric points, responses to inhibitors, pH optima, or electrophoretic mobilities at pH 8.3. The relative in vivo rates of synthesis of C57BL/6J, A/J, and SWR/J arylsulfatase B were comparable.

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“…Arylsulphatase activity was measured by following the release of p-nitrocatechol from p-nitrocatechol sulphate by incubating the enzyme with 10mM substrate in 0.25 M-sodium acetate buffer, pH 5.5, as described by Farooqui & Srivastava (1979). One unit of enzyme is defined as the amount liberating lumol of p-nitrocatechol/min.…”

Section: Assay Ofenzyme Activitymentioning

confidence: 99%

“…The dialysed solution was subjected to a concanavalin A-Sepharose column chromatography as described by Farooqui & Srivastava (1979). The fractions containing arylsulphatase were pooled, concentrated to 50ml on an Amicon cell (UM 10) and dialysed against 10vol.…”

Section: Assay Ofenzyme Activitymentioning

confidence: 99%

“…Arylsulphatase A is an acid glycoprotein and B is a basic glycoprotein. Arylsulphatases have been purified from various tissues, mammalian semen, testes and urine (see Farooqui & Srivastava, 1979). Among the reproductive processes, sulphated polysaccharides participate in ovulation (Gerbauer et al, 1978) and in the regulation and expansion of the cumulus oophorus (Eppig, 1981).…”

mentioning

confidence: 99%

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Isolation and characterization of the pig endometrial arylsulphatase A.

Hamid¹,

Srivastava²

1983

Biochemical Journal

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The pig endometrial arylsulphatase A was purified 3322-fold to a specific activity of 150 mumol/min per mg. The purification involved (NH4)2SO4 fractionation, chromatography on concanavalin A-Sepharose and DEAE-Sepharose, gel filtrations on Sephadex G-200 at pH 7.4 and 5, and a new preparative gel-electrophoresis technique. The homogeneous enzyme is a glycoprotein containing 20% carbohydrate. The purified enzyme has Mr about 120 000 and it contains subunits of Mr 63 000. The pig endometrial arylsulphatase A shows many properties in common with those of arylsulphatases A purified from other sources. The similarities include their low isoelectric points, the anomalous time-activity relationships, multi-pH optima, inhibition by SO3(2-), SO4(2-), phosphate ions, metal ions and nucleoside phosphates, pH- and ionic-strength-dependent polymerization and amino acid composition.

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Isolation, characterization and the role of rabbit testicular arysulphatase A in fertilization

Cited by 47 publications

References 44 publications

Arylsulfatase in natural killer cells: its possible role in cytotoxicity.

Arylsulfatase in natural killer cells: its possible role in cytotoxicity.

Purification and properties of arylsulfatase B from high- and low-activity mouse strains

Isolation and characterization of the pig endometrial arylsulphatase A.

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