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Gene Review

AS-A  -  arylsulfatase A

Sus scrofa

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High impact information on AS-A

  • All of these results designated a new function of AS-A in gamete interaction [1].
  • In this report, we identified P68 as arylsulfatase A (AS-A) based on the presence of P68 tryptic peptide sequences in the pig testis AS-A cDNA sequence [1].
  • The presence of AS-A on the sperm plasma membrane was conclusively demonstrated by indirect immunofluorescence, immunogold electron microscopy, and AS-A's desulfation activity on live mouse sperm [2].
  • Furthermore, Alexa-430 conjugated AS-A bound to mouse ZP of unfertilized eggs but not to fertilized ones, and this level of binding increased and approached saturation with increasing Alexa-430 AS-A concentrations [2].
  • Using anti-AS-A antibody, we have shown by immunoblotting that AS-A was present in a Triton X-100 extract of mouse sperm [2].

Biological context of AS-A


Anatomical context of AS-A


Associations of AS-A with chemical compounds

  • By fractionating intralysosomal soluble proteins by velocity sedimentation on sucrose gradients or gel permeation chromatography we identified a thyroid arylsulfatase A holoenzyme which corresponds to a 120,000 Mr species [5].
  • An example of the latter is the removal of the sulfate group from cerebroside sulfate by arylsulfatase A. The mechanism of lipid sequestration from membranes and presentation of the lipid-protein complex to catabolic enzymes is a crucial aspect of the function of this protein [6].
  • When compared to adrenal enzyme activities in animals on high dietary levels of ascorbate, the adrenals of animals on 2.4 mg of ascorbate per day expressed 50% increase in the activities of acid phosphatase, arylsulfatase A, and arylsulfatase B (p less than 0.02) [7].

Other interactions of AS-A

  • Lysosomal enzymes, cathepsin D, beta-D-galactosidase, beta-D-glucosidase, alpha-D-mannosidase, alpha-L-fucosidase, hexosaminidase, and arylsulfatase A and B, were assayed in crude fractions from various pig tissues, heart, brain, liver, kidney, thyroid, adrenals, ovary, and spleen [5].

Analytical, diagnostic and therapeutic context of AS-A


  1. Arylsulfatase a is present on the pig sperm surface and is involved in sperm-zona pellucida binding. Carmona, E., Weerachatyanukul, W., Soboloff, T., Fluharty, A.L., White, D., Promdee, L., Ekker, M., Berger, T., Buhr, M., Tanphaichitr, N. Dev. Biol. (2002) [Pubmed]
  2. Role of sperm surface arylsulfatase A in mouse sperm-zona pellucida binding. Tantibhedhyangkul, J., Weerachatyanukul, W., Carmona, E., Xu, H., Anupriwan, A., Michaud, D., Tanphaichitr, N. Biol. Reprod. (2002) [Pubmed]
  3. Purification of boar acrosomal arylsulfatase A and possible role in the penetration of cumulus cells. Dudkiewicz, A.B. Biol. Reprod. (1984) [Pubmed]
  4. Boar seminal vesicles secrete arylsulfatases into seminal plasma: evidence that desulfation of seminolipid occurs only after ejaculation. Gadella, B.M., Colenbrander, B., Van Golde, L.M., Lopes-Cardozo, M. Biol. Reprod. (1993) [Pubmed]
  5. Evidence for the presence of a very high concentration of arylsulfatase A in the pig thyroid: identification of arylsulfatase A subunits as the two major glycoproteins in purified thyroid lysosomes. Selmi, S., Maire, I., Rousset, B. Arch. Biochem. Biophys. (1989) [Pubmed]
  6. Disulfide connectivity in cerebroside sulfate activator is not necessary for biological activity or alpha-helical content but is necessary for trypsin resistance and strong ligand binding. Faull, K.F., Higginson, J., Waring, A.J., Johnson, J., To, T., Whitelegge, J.P., Stevens, R.L., Fluharty, C.B., Fluharty, A.L. Arch. Biochem. Biophys. (2000) [Pubmed]
  7. Effect of ascorbate on lysosomal enzyme activities in guinea pig cartilage and adrenals. Leveille, C.R., Schwartz, E.R. International journal for vitamin and nutrition research. Internationale Zeitschrift für Vitamin- und Ernährungsforschung. Journal international de vitaminologie et de nutrition. (1982) [Pubmed]
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