131
Views
8
CrossRef citations to date
0
Altmetric
Original Article

Mammalian arylsulfatase A functions as a novel component of the extracellular matrix

, , , , , , , & show all
Pages 388-396 | Received 12 May 2009, Accepted 04 Dec 2009, Published online: 18 Mar 2010

REFERENCES

  • Hanson, S.R., Best, M.D., and Wong, C.H. (2004). Sulfatases: Structure, mechanism, biological activity, inhibition, and synthetic utility. Angew. Chem. Int. Ed. 43:5736–5763.
  • Bond, C.S., Clements, P.R., Ashby, S.J., Collyer, C.A., Harrop, S.J., Hopwood, J.J., and Guss, J.M. (1997). Structure of a lysosomal sulfatase. Structure 5:277–289.
  • Parenti, G., Meroni, G., and Ballabio, A. (1997). The sulfatase gene family. Curr. Opin. Genet. Dev. 7:386–391.
  • Ferrante, P., Messali, S., Meroni, G., and Ballabio, A. (2002). Molecular and biochemical characterisation of a novel sulphatase gene: Arylsulfatase G (ARSG). Eur. J. Hum. Genet. 10:813–818.
  • Sardiello, M., Annunziata, I., Roma, G., and Ballabio, A. (2005). Sulfatases and sulfatase modifying factors: An exclusive and promiscuous relationship. Hum. Mol. Genet. 14:3203–3217.
  • Obaya, A.J. (2006). Molecular cloning and initial characterization of three novel human sulfatases. Gene 372:110–117.
  • Gustavson, K.H., and Hagberg, B. (1971). The incidence and genetics of metachromatic leucodystrophy in northern Sweden. Acta Pediatr. Scand. 60:585–590.
  • Kolodny, E.H. (1995). In The Metabolic and Molecular Bases of Inherited Disease, 6th ed. C.R. Scriver, A.L. Beaudet, W.S. Sly and D. Valle ( eds.)pp. 2693–2740. New York: McGraw-Hill.
  • Consiglio, A., Quatirini, A., Martino, S., Bensadoun, J.C., Dolcetta, D., Trojani, A., Benaglia, G., Marchesini, S., Cestari, V., Oliverio, A., Bordignon, C., and Naldini, L. (2001). In vivo gene therapy of metachromatic leukodystrophy by lentiviral vectors: Correction of neuropathology and protection against learning impairments in affected mice. Nat. Med. 7:310–316.
  • Matzner, U., Herbst, E., Hedayati, K.K., Lullmann-Rauch, R., Wessig, C., Schroder, S., Eistrup, C., Moller, C., Fogh, J., and Gieselmann, V. (2005). Enzyme replacement improves nervous system pathology and function in a mouse model for metachromatic leukodystrophy. Hum. Mol. Genet. 14:1139–1152.
  • Sevin, C., Benraiss, A., Van Dam, D., Bonnin, D., Nagels, G., Verot, L., Laurendeau, I., Vidaud, M., Gieselmann, V., Vanier, M., De Deyn, P.P., Aubourg, P., and Cartier, N. (2006). Intracerebral adeno-associated virus-mediated gene transfer in rapidly progressive forms of metachromatic leukodystrophy. Hum. Mol. Genet. 15:53–64.
  • Viviano, B.L., Paine-Saunders, S., Gasiunas, N., Gallagher, J., and Saunders, S. (2004). Domain-specific modification of heparan sulfate by QSulf1 modulates the binding of the bone morphogenetic protein antagonist noggin. J. Biol. Chem. 279:5604–5611.
  • Uchimura, K., Morimoto-Tomita, M., Bistrup, A., Li, J., Lyon, M., Gallagher, J., Werb, Z., and Rosen, S.D. (2006). HSulf-2, an extracellular endoglucosamine-6-sulfatase, selectively mobilizes heparin-bound growth factors and chemokines: Effects on VEGF, FGF-1, and SDF-1. BMC Biochem. 7:2.
  • Gadella, B.M., Colenbrander, B., and Lopes-Cardozo, M. (1991). Arylsulfatases are present in seminal plasma of several domestic mammals. Biol. Reprod. 45:381–386.
  • Carmona, E., Weerachatyanukul, W., Xu, H., Fluharty, A., Anupriwan, A., Shoushtarian, A., Chakrabandhu, K., and Tanphaichitr, N. (2002a). Binding of arylsulfatase A to mouse sperm inhibits gamete interaction and induces the acrosome reaction. Biol. Reprod. 66:1820–1827.
  • Carmona, E., Weerachatyanukul, W., Soboloff, T., Fluharty, A.L., White, D., Promdee, L., Ekker, M., Berger, T., Buhr, M., and Tanphaichitr, N. (2002b). Arylsulfatase A is present on the pig sperm surface and is involved in sperm-zona pellucida binding. Dev. Biol. 247:182–196.
  • Tantibhedhyangkul, J., Weerachatyanukul, W., Carmona, E., Xu, H., Anupriwan, A., Michaud, D., and Tanphaichitr, N. (2002). Role of sperm surface arylsulfatase A in mouse sperm-zona pellucida binding. Biol. Reprod. 67:212–219.
  • Wu, A., Anupriwan, A., Iamsaard, S., Chakrabandhu, K., Santos, D.C., Rupar, T., Tsang, B.K., Carmona, E., and Tanphaichitr, N. (2007). Sperm surface arylsulfatase A can disperse the cumulus matrix of cumulus oocyte complexes. J. Cell Physiol. 213:201–211.
  • Akasaka, K., and Terayama, H. (1983). Sulfated glycan present in the EDTA extract of Hemicentrotus embryos (mid‐gastrula). Exp. Cell Res. 146:177–185.
  • Akasaka, K., Akimoto, Y., Sato, M., Hirano, H., and Shimada, H. (1990). Histochemical detection of arylsulfatase activity in sea urchin embryos. Dev. Growth Differ. 32:293–298.
  • Mitsunaga-Nakatsubo, K., Akasaka, K., Akimoto, Y., Akiba, E., Kitajima, T., Tomita, M., Hirano, H., and Shimada, H. (1998). Arylsulfatase exists as non-enzymatic cell surface protein in sea urchin embryos. J. Exp. Zool. 280:220–230.
  • Mitsunaga-Nakatsubo, K., Akimoto, Y., Kawakami, H., and Akasaka, K. (2009a). Sea urchin arylsulfatase, an extracellular matrix component, is involved in gastrulation during embryogenesis. Dev. Genes Evol. 219:281–288.
  • Mitsunaga-Nakatsubo, K., Kusunoki, S., Kawakami, H., Akasaka, K., and Akimoto, Y. (2009b). Cell surface arylsulfatase A and B on sinusoidal endothelial cells, hepatocytes and Kupper cells in mammalian livers. Med. Mol. Morphol. 42:63–69.
  • Laemmli, U.K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680–685.
  • Fujiwara, H., Gu, J., and Sekiguchi, K. (2004). Rac regulates integrin-mediated endothelial cell adhesion and migration on laminin-8. Exp. Cell Res. 292:67–77.
  • Wong, A.J., Pollard, T.D., and Herman, I.M. (1983). Actin filament stress fibers in vascular endothelial cells in vivo. Science 219:867–869.
  • Cavallaro, U., Tenan, M., Castelli, V., Perilli, A., Maggiano, N., Van Meir, E.G., Montesano, R., Soria, M.R., and Pepper, M.S. (2001). Response of bovine endothelial cells to FGF-2 and VEGF is dependent on their site of origin: Relevance to the regulation of angiogenesis. J. Cell Biochem. 82:619–633.
  • Abedi, H., and Zachary, I. (1997). Vascular endothelial growth factor stimulates tyrosine phosphorylation and recruitment to new focal adhesions of focal adhesion kinase and paxillin in endothelial cells. J. Biol. Chem. 272:15442–15451.
  • Hynes, R.O. (1992). Integrins: Versatility, modulation, and signaling in cell adhesion. Cell 69:11–25.
  • Berrier, A.L., and Yamada, K.M. (2007). Cell-matrix adhesion. J. Cell Physiol. 213:565–573.
  • Suzuki, S., Pierschbacher, M.D., Hayman, E.G., Nguyen, K., Ohgren, Y., and Ruoslahti, E. (1984). Domain structure of Vitronectin. J. Biol. Chem. 259:15307–15314.
  • LeBaron, R.G., Hook, A., Esko, J.D., Gay, S., and Hook, M. (1989). Binding of heparan sulfate to type V collagen. A mechanism of cell-substrate adhesion. J. Biol. Chem. 264:7950–7956.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.