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Gene Review

LOC406146  -  hyaluronoglucosaminidase

Apis mellifera

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Disease relevance of LOC406146

  • Expression of the cloned cDNA in Escherichia coli yielded a 41-kDa polypeptide that had hyaluronidase activity [1].
  • The inhibitor had no effect on Streptomyces hyaluronidase, indicating that inhibition was not through protection of the hyaluronan substrate [2].
  • These results demonstrate that alternative mRNA splicing controls cellular expression of enzymatically active hyaluronidase and may explain the elevated hyaluronidase levels in bladder/prostate cancer [3].
  • In vitro IgE binding was similar in nHya and the enzyme from baculovirus but markedly lower in Hya expressed in E. coli [4].
  • The measurement of the venom-specific IgG, the ratio of IgG/IgE, and (for bee patients) the serum antibody titer against the bee venom components phospholipase A and hyaluronidase did not improve the diagnosis of a current hypersensitivity against insect venom [5].

High impact information on LOC406146

  • The mRNA encoding hyaluronidase could also be detected in testes from drones [1].
  • The deduced amino acid sequence showed that bee venom hyaluronidase is a polypeptide composed of 349 amino acids containing four cysteines and three potential sites for N-glycosylation [1].
  • By using degenerate oligonucleotides derived from the amino-terminal sequence of this hyaluronidase reported by others, clones encoding the precursor for this enzyme could be isolated from a cDNA library prepared from venom glands of worker bees [1].
  • Hyaluronidase is a hyaluronic acid-degrading endoglycosidase that is present in many toxins and the levels of which are elevated in cancer [3].
  • Stable transfection and HYAL1v1-specific antibody confirmed that the HYAL1 sequence from aa 301 to 330 is critical for hyaluronidase activity [3].

Chemical compound and disease context of LOC406146


Biological context of LOC406146

  • Sera from honeybee-reactive patients, who had weak cross-reactions with yellow jacket venom, demonstrated strong IgE binding to purified V. maculifrons hyaluronidase and Vmacl [6].

Anatomical context of LOC406146

  • Inter-alpha-inhibitor, found in the hyaluronan-rich cumulus mass surrounding mammalian ova and the coat of fibroblasts and mesothelial cells, may function to stabilize such matrices by protecting against hyaluronidase degradation [2].
  • In BALB/c mice, Dol m 2 and bee hyaluronidase showed cross-reactivity at both antibody and T cell levels [7].
  • METHODS: In Escherichia coli Hya was produced as inclusion body 6 x His-fusion protein [4].
  • Phospholipase A2 (Api m 1), hyaluronidase (Api m 2) and melittin (Api m 3) fragments with overlapping amino acids were assembled in a different order in the Api m (1/2/3) chimeric protein, which preserved entire T cell epitopes, whereas B cell epitopes of all three allergens were abrogated [8].
  • PH-20 appears to be a multifunctional protein; it is a hyaluronidase, a receptor for HA-induced cell signaling, and a receptor for the zona pellucida surrounding the oocyte [9].

Associations of LOC406146 with chemical compounds


Other interactions of LOC406146


Analytical, diagnostic and therapeutic context of LOC406146


  1. Bee venom hyaluronidase is homologous to a membrane protein of mammalian sperm. Gmachl, M., Kreil, G. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  2. Evidence that the serum inhibitor of hyaluronidase may be a member of the inter-alpha-inhibitor family. Mio, K., Carrette, O., Maibach, H.I., Stern, R. J. Biol. Chem. (2000) [Pubmed]
  3. Regulation of hyaluronidase activity by alternative mRNA splicing. Lokeshwar, V.B., Schroeder, G.L., Carey, R.I., Soloway, M.S., Iida, N. J. Biol. Chem. (2002) [Pubmed]
  4. Superior biologic activity of the recombinant bee venom allergen hyaluronidase expressed in baculovirus-infected insect cells as compared with Escherichia coli. Soldatova, L.N., Crameri, R., Gmachl, M., Kemeny, D.M., Schmidt, M., Weber, M., Mueller, U.R. J. Allergy Clin. Immunol. (1998) [Pubmed]
  5. The evaluation of the common diagnostic methods of hypersensitivity for bee and yellow jacket venom by means of an in-hospital insect sting. Blaauw, P.J., Smithuis, L.O. J. Allergy Clin. Immunol. (1985) [Pubmed]
  6. Allergens in Hymenoptera venom XI. Isolation of protein allergens from Vespula maculifrons (yellow jacket) venom. Hoffman, D.R., Wood, C.L. J. Allergy Clin. Immunol. (1984) [Pubmed]
  7. Sequence identity and antigenic cross-reactivity of white face hornet venom allergen, also a hyaluronidase, with other proteins. Lu, G., Kochoumian, L., King, T.P. J. Biol. Chem. (1995) [Pubmed]
  8. Prevention of allergy by a recombinant multi-allergen vaccine with reduced IgE binding and preserved T cell epitopes. Karamloo, F., Schmid-Grendelmeier, P., Kussebi, F., Akdis, M., Salagianni, M., von Beust, B.R., Reimers, A., Zumkehr, J., Soldatova, L., Housley-Markovic, Z., Müller, U., Kündig, T., Kemeny, D.M., Spangfort, M.D., Blaser, K., Akdis, C.A. Eur. J. Immunol. (2005) [Pubmed]
  9. The dual functions of GPI-anchored PH-20: hyaluronidase and intracellular signaling. Cherr, G.N., Yudin, A.I., Overstreet, J.W. Matrix Biol. (2001) [Pubmed]
  10. HYAL2, a human gene expressed in many cells, encodes a lysosomal hyaluronidase with a novel type of specificity. Lepperdinger, G., Strobl, B., Kreil, G. J. Biol. Chem. (1998) [Pubmed]
  11. Hyaluronidase polymorphism detected by polyacrylamide gel electrophoresis. Application to hyaluronidases from bacteria, slime molds, bee and snake venoms, bovine testes, rat liver lysosomes, and human serum. Fiszer-Szafarz, B. Anal. Biochem. (1984) [Pubmed]
  12. Sulphated oligosaccharides as inhibitors of hyaluronidases from bovine testis, bee venom and Streptococcus agalactiae. Salmen, S., Hoechstetter, J., Käsbauer, C., Paper, D.H., Bernhardt, G., Buschauer, A. Planta Med. (2005) [Pubmed]
  13. N-Glycan analysis by matrix-assisted laser desorption/ionization mass spectrometry of electrophoretically separated nonmammalian proteins: application to peanut allergen Ara h 1 and olive pollen allergen Ole e 1. Kolarich, D., Altmann, F. Anal. Biochem. (2000) [Pubmed]
  14. A major allergen gene-fusion protein for potential usage in allergen-specific immunotherapy. Kussebi, F., Karamloo, F., Rhyner, C., Schmid-Grendelmeier, P., Salagianni, M., Mannhart, C., Akdis, M., Soldatova, L., Markovic-Housley, Z., Von Beust, B.R., Kündig, T., Kemeny, D.M., Blaser, K., Crameri, R., Akdis, C.A. J. Allergy Clin. Immunol. (2005) [Pubmed]
  15. Allergy to insect stings. II. Phospholipase A: the major allergen in honeybee venom. Sobotka, A.K., Franklin, R.M., Adkinson, N.F., Valentine, M., Baer, H., Lichtenstein, L.M. J. Allergy Clin. Immunol. (1976) [Pubmed]
  16. Crossed radioimmunoelectrophoretic studies of bee venom allergens. Aukrust, L., Einarsson, R., Ohman, S., Johansson, S.G. Allergy (1982) [Pubmed]
  17. The purification and characterisation of hyaluronidase from the venom of the honey bee, Apis mellifera. Kemeny, D.M., Dalton, N., Lawrence, A.J., Pearce, F.L., Vernon, C.A. Eur. J. Biochem. (1984) [Pubmed]
  18. Determination of hyaluronidase activity in venoms using capillary electrophoresis. Pattanaargson, S., Roboz, J. Toxicon (1996) [Pubmed]
  19. Changes in the levels of anti-phospholipase A2 and hyaluronidase antibodies during bee venom immunotherapy. Kemeny, D.M., McKenzie-Mills, M., Harries, M.G., Youlten, L.J., Lessof, M.H. Monographs in allergy. (1983) [Pubmed]
  20. The N-glycans of yellow jacket venom hyaluronidases and the protein sequence of its major isoform in Vespula vulgaris. Kolarich, D., Léonard, R., Hemmer, W., Altmann, F. FEBS J. (2005) [Pubmed]
  21. Histamine release from peripheral blood leukocytes with purified bee venom allergens: effect of hyperimmune beekeeper plasma. Clinton, P.M., Kemeny, D.M., Youlten, L.J., Lessof, M.H. Int. Arch. Allergy Appl. Immunol. (1989) [Pubmed]
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