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

• Superior biologic activity of the recombinant bee venom allergen hyaluronidase expressed in baculovirus-infected insect cells as compared with Escherichia coli [4].

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

• Sequence identity and antigenic cross-reactivity of white face hornet venom allergen, also a hyaluronidase, with other proteins [7].
• The reaction product was a polysaccharide of about 20 kDa, which was further hydrolyzed to small oligosaccharides by the sperm hyaluronidase [10].
• 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 [11].
• Sulphated oligosaccharides like verbascose, planteose and neomycin showed comparable inhibition on all hyaluronidases, thereby possessing 100 - 500 times the activity of the widely accepted hyaluronidase inhibitor apigenin [12].
• The method was tested on proteins with N-glycans of known structure, i.e., as horseradish peroxidase, zucchini ascorbate oxidase, soybean agglutinin, honeybee venom hyaluronidase, bovine ribonuclease B, and bovine fetuin [13].

Other interactions of LOC406146

• METHODS: By genetic engineering, we produced a fusion protein composed of the 2 major bee venom allergens: phospholipase A 2 (Api m 1) and hyaluronidase (Api m 2) [14].
• All patients were insensitive to the hyaluronidase and apamin preparations [15].
• Phospholipase A, acid phosphatase, hyaluronidase and melittin were demonstrated in the immunoprecipitates using zymographic techniques and direct hemolysis of sheep erythrocytes [16].

Analytical, diagnostic and therapeutic context of LOC406146

• A value of 50 000 was obtained by ultracentrifugation assuming a partial specific volume of 0.73 cm3/g. Hyaluronidase was found to be a minor allergen in bee venom allergic patients [17].
• Determination of hyaluronidase activity in venoms using capillary electrophoresis [18].
• Changes in the levels of anti-phospholipase A2 and hyaluronidase antibodies during bee venom immunotherapy [19].
• Concomitant peptide mapping of the V. vulgaris 43 kDa band identified the known hyaluronidase, Ves v 2 (SwissProt P49370), but only as a minor component [20].
• The response of 15 strongly bee-venom-allergic patients to highly purified venom allergens was compared using skin prick test titration, peripheral blood leukocyte (PBL) histamine release and radioallergosorbent test with three highly purified bee venom allergens: phospholipase (PLA2), hyaluronidase (HYAL) and acid phosphatase (ACID P) [21].

References