Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.2.1.36 (hyaluronidase)
 4,606 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Invasion of chicken embryo fibroblast (CEF) cells by the virulent encapsulated Pasteurella multocida strains P-1059 (serovar A:3) and X-73 (serovar A:1) and an avirulent noncapsulated derivative P-1059B (serovar -:3) was investigated. The number of intracellular bacteria increased for all the strains after 2, 4 and 6 h post-inoculation to CEF cells. By 6 h post-inoculation, the number of invaded bacteria of encapsulated strains was significantly higher than noncapsulated strain and reached 150- and 112-fold for strains P-1059 and X-73, respectively, while it was 9-fold for strain P-1059B as compared to the number of invaded bacteria recovered after 2 h post-inoculation. Electron microscopy of invasion by encapsulated strains showed that the bacteria were adhering to CEF cells membrane after 1 h of inoculation. By 4-h, one or two bacteria were detected within membrane-bound vacuoles of the intracellular space. The number of intracellular bacteria markedly increased at 14 h post-inoculation. Invasion of all strains was inhibited significantly when the monolayers were treated with periodic acid (P<0.001) or trypsin (P<0.05). The treatment of bacteria with hyaluronidase did not affect invasion. The present results indicate that avian P. multocida capsular type A strains are invasive and that the receptor on CEF cell surface might be glycoprotein.
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PMID:Invasion of chicken embryo fibroblast cells by avian Pasteurella multocida. 1553 Jul 39

We have identified an 80 kDa protein in ejaculated bull spermatozoa (p80) which is found in acrosomal and post-acrosomal areas of the head. It has a hyaluronidase activity and shares homologies with PH-20, a sperm surface glycoprotein involved in sperm-egg interaction. The aim of the present study was to characterize bull sperm p80 protein at the nucleic and amino acid levels to determine whether it is the bovine PH-20 ortholog. The complete nucleotide sequence determined by RT-PCR, 3' and 5' RACE show that bull p80, displays identity with the PH-20 nucleotide and amino acid sequences. Messenger RNA and protein expressions determined by Northern blot and immunohistochemistry revealed that the protein is testicular (expressed in spermatocytes and spermatids). The localization of p80 on spermatozoa, determined by indirect immunofluorescence using a monoclonal antibody, shows the protein in acrosomal and post acrosomal areas of the head with an increase in the signal intensity as sperm progress through the epididymis. Post-translational modifications of the protein were investigated during the epididymal maturation by Western blot on protein extracts from sperm collected in the caput, corpus and cauda portions of bull epididymis. Glycolysation status of sperm p80 protein on proteins from ejaculated and epididymidal sperm was investigated. Result show that the glycosylation status is modified as spermatozoa migrate through the epididymis. Hyaluronidase activity evaluated in protein extracts from spermatozoa of the three different epididymal sections revealed that the activity is higher at pH 7 than 4 and is not affected by epididymal maturation. These data strongly suggest that p80 is the bovine PH-20.
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PMID:Identification of the bull sperm p80 protein as a PH-20 ortholog and its modification during the epididymal transit. 1589 45

Hyaluronidase (E.C. 3.2.1.35), one of the three major allergens of yellow jacket venom, is a glycoprotein of 45 kDa that is largely responsible for the cross-reactivity of wasp and bee venoms with sera of allergic patients. The asparagine-linked carbohydrate often appears to constitute the common IgE-binding determinant. Using a combination of MALDI MS and HPLC of 2-aminopyridine-labelled glycans, we found core-difucosylated paucimannosidic glycans to be the major species in the 43-45 kDa band of Vespula vulgaris and also in the corresponding bands of venoms from five other wasp species (V. germanica, V. maculifrons, V. pensylvanica, V. flavopilosa and V. squamosa). 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. De novo sequencing by tandem MS revealed the predominating peptides to resemble a different, yet homologous, sequence. cDNA cloning retrieved a sequence with 58 and 59% homology to the previously known isoform and to the Dolichovespula maculata and Polistes annularis hyaluronidases. Close homologues of this new, putative hyaluronidase b (Ves v 2b) were also the major isoform in the other wasp venoms.
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PMID:The N-glycans of yellow jacket venom hyaluronidases and the protein sequence of its major isoform in Vespula vulgaris. 1621 50

The most widely conserved mammalian sperm antigen is sperm adhesion molecule 1, SPAM1/PH-20, which is also the major testicular hyaluronidase. This multifunctional glycosyl phosphatidylinositol (GPI)-linked protein plays several roles in fertilization and is encoded by a gene that resides among hyaluronidase family members in a cluster on human 7q31/mouse 6A2. In the human cluster, SPAM1 is the only functional hyaluronidase and of all six hyaluronidases in the genome it is the best characterized, both structurally and functionally. While SPAM1 transcripts are abundantly expressed only in the testis, specifically in spermatids, the RNA and protein are present in the male reproductive tract and accessory organs and in the female tract of mice. Our investigation of the post-testicular expression of SPAM1 shows that the protein is widely expressed in the epididymis. Like testicular SPAM1, epididymal SPAM1 (ES) has hyaluronidase activity and is conserved in at least five species (mouse, rat, bull, macaque, and human) all of which have putative androgen response elements in the gene promoters, consistent with androgen regulation. Testicular lumicrine factors have also been implicated in ES regulation. Based on regional expression, the protein is likely to play a role in both sperm maturation and storage. A minor secretory glycoprotein, ES is present in the epididymal luminal fluid in both a soluble and insoluble form (epididymosomes), with the latter having an intact lipid anchor. Genetic approaches have provided evidence for sperm uptake of ES in vivo, and in vitro uptake has been demonstrated with the use of Spam1 null mice. In vitro acquisition of ES on the sperm surface results in a pattern that mimics the wild-type distribution. More importantly it significantly increases the ability of null sperm to penetrate the cumulus of oocytes via hyaluronidase activity, directly relating ES uptake with fertilizing ability and indicating that ES is a marker of sperm maturation.
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PMID:Epididymal SPAM1 and its impact on sperm function. 1642 Sep 70

Venom hyaluronidases help in rapid spreading of the toxins by destroying the integrity of the extra-cellular matrix of the tissues in the victims. A hyaluronidase inhibitor (WSG) is purified from a folk medicinal plant, Withania somnifera. The glycoprotein inhibited the hyaluronidase activity of cobra (Naja naja) and viper (Daboia russelii) venoms, which was demonstrated by zymogram assay and staining of the skin tissues for differential activity. WSG completely inhibited the activity of the enzyme at a concentration of 1:1 w/w of venom to WSG. Thus we are able to demonstrate that the glycoprotein inhibits hyaluronidase activity of the venoms. External application of the plant extract as an antidote in rural parts of India to snakebite victims appears to have a scientific basis.
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PMID:A glycoprotein from a folk medicinal plant, Withania somnifera, inhibits hyaluronidase activity of snake venoms. 1651 28

Hyaluronectin (HN) is a glycoprotein with a high affinity to hyaluronic acid (HA) and known to be a component of the extracellular matrix of tumours. Clinical studies have shown that a low level of HN correlates to tumours with poor prognosis, whereas a high level of HN correlates to tumours with good prognosis. We previously demonstrated in vitro that hyaluronidase activity, which promotes tumour progression and metastatic spread by degradation of HA into angiogenic oligosaccharides, was inhibited or promoted by HN, according to the level of HN-expression. This raises the question of the role played by HN in cancer, and particularly if high and low levels of HN-expression could trigger opposite effects on tumour growth and/or metastatic spread. To address this issue, we used a model of spontaneous lung fluorescent metastases that we characterised previously. We stably transfected the human HN cDNA into fluorescent H460MGFP cells and selected two clones characterised by different levels of HN-expression: HN110 and HN704, with a high and a low level of HN-expression, respectively. In vitro, we demonstrated that HN704 cell migration was significantly increased. Inoculation of clones to nude mice had no significant effect on tumour growth, but clearly revealed opposite effects on metastatic spread: HN110 significantly decreased the number of fluorescent metastases whereas HN704 significantly increased it. We also analysed HN, HA and hyaluronidase contents in sera and tumours. These results demonstrate that HN can play a role as either a suppressor or promoter of metastatic spread.
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PMID:Hyaluronectin modulation of lung metastasis in nude mice. 1693 Sep 92

The venoms of stinging insects belong to the most dangerous allergen sources and can cause fatal anaphylactic reactions. Reliable prediction of a patient's risk to anaphylactic reactions is vital, and diagnosis requires the knowledge of the relevant allergens. Recently, a new hyaluronidase -like glycoprotein from Vespula vulgaris (Ves v 2b) was identified. This led us to investigate hyaluronidases and also other major allergens from V. germanica and four additional Vespula species. By MALDI-Q-TOF-MS, the new hyaluronidase-like protein was shown to be the major component of the 43-kDa band in all Vespula species studied. LC-ESI-Q-TOF-MS/MS sequencing of Ves g 2a and Ves g 2b facilitated the cloning of their cDNA. Ves v 2b and Ves g 2b turned out to be essentially identical on protein level. Whereas the less abundant "a" form displayed enzymatic activity, the new "b" homologue did not. This is probably caused by amino acid exchanges in the active site, and it raises questions about the physiological role of this protein. Sequence comparisons by MS/MS of antigen 5 and phospholipases from V. vulgaris, germanica, maculifrons, pensylvanica, flavopilosa and squamosa revealed the latter as a taxonomic outlier and led to the discovery of several not previously reported amino acid differences.
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PMID:A proteomic study of the major allergens from yellow jacket venoms. 1744 42

Honeybee venom hyaluronidase (Api m 2) is a major glycoprotein allergen. Previous studies have indicated that recombinant Api m 2 expressed in insect cells has enzyme activity and IgE binding comparable with that of native Api m 2. In contrast, Api m 2 expressed in Escherichia coli does not. In this study, we characterized the carbohydrate side chains of Api m 2 expressed in insect cells, and compared our data with the established carbohydrate structure of native Api m 2. We assessed both the monosaccharide and the oligosaccharide content of recombinant Api m 2 using fluorophore-assisted carbohydrate electrophoresis and HPLC. To identify the amino acid residues at which glycosylation occurs, we digested recombinant Api m 2 with endoproteinase Glu-C and identified the fragments that contained carbohydrate by specific staining. Recombinant Api m 2 expressed in insect cells contains N-acetylglucosamine, mannose, and fucose, as well as trace amounts of glucose and galactose, and the oligosaccharide analysis is consistent with heterogeneous oligosaccharide chains consisting of two to seven monosaccharides. No sialic acid or N-acetylgalactosamine were detected. These results are similar to published data for native Api m 2, although some monosaccharide components appear to be absent in the recombinant protein. Analysis of proteolytic digests indicates that of the four candidate N-glycosylation sites, carbohydrate chains are attached at asparagines 115 and 263. Recombinant Api m 2 expressed in insect cells has enzymic activity and IgE binding comparable with the native protein, and its carbohydrate composition is very similar.
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PMID:Characterization of the N-glycans of recombinant bee venom hyaluronidase (Api m 2) expressed in insect cells. 1747 7

Although the flexor digitorum profundus (FDP) tendon's gliding resistance is low, the lubrication mechanism that enables this is unclear. The principal lubricants in joints, such as hyaluronic acid, phospholipids, and lubricin, a lubricating glycoprotein, are known to be present in the canine tendon. In this study, we assessed the effect of these lubricants in the tendon by measuring gliding resistance before and after their removal. Canine FDP tendons were treated with hyaluronidase, phospholipase, lipid solvent, and/or trypsin. The gliding resistance of FDP tendons significantly increased after all treatments (p < 0.05). The largest effect on gliding resistance was observed after trypsin digestion. Scanning electron microscopy and immunostaining for hyaluronic acid and lubricin were used to qualitatively assess the tendon surface after treatments. The trypsin digestion produced the most irregular surface, with many exposed collagen fibers. The results of this study suggest that phospholipids, hyaluronic acid, and protein components are all involved in maintaining the low gliding resistance of the FDP tendon.
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PMID:The effect of hyaluronidase, phospholipase, lipid solvent and trypsin on the lubrication of canine flexor digitorum profundus tendon. 1840 58

Yellow jacket (Vespula vulgaris) hyaluronidase (Ves v 2) is a glycoprotein and a mixture of two isoallergens, Ves v 2.01 and Ves v 2.02. Wasp and bee sensitized individuals frequently show IgE antibodies that in vitro recognize common carbohydrate structures across the hymenoptera species. The aim of the study was to characterize the glycosylation patterns in Ves v 2 isoallergens and to assess their immunological properties regarding antibody binding and T cell activation. The glycosylation sites and the carbohydrate structures were verified by use of tandem mass spectrometry (MS/MS). The immunological characterization of the N-glycan structures was assessed by antibody binding, T cell proliferation and T cell epitope assays comparing native (n) and non-glycosylated recombinant (r) Ves v 2. Analyses of the Ves v 2 glycopeptides revealed that glycan attachments were found for residues 79, 99 and 127 of Ves v 2.01, and residues 66 and 81 of Ves v 2.02. Structural analysis of the glycopeptides showed that the majority of the N-glycans contained at least one alpha1,3-fucose and/or alpha1,6-fucose residues in a structure. Interestingly, serum IgE antibodies from vespid allergic patients recognized nVes v 2 but not rVes v 2. Non-glycosylated rVes v 2, however, induced T cell and cytokine responses comparable to glycosylated nVes v 2. The present study shows that N-glycan structures are needed for the antibody recognition but not for the T cell reactivity of Ves v 2 in vitro. The occurrences of carbohydrate-specific antibodies against nVes v 2, however, suggest that non-mammalian glycan structures as in nVes v 2 may provide a link between T cells and other effector cells in allergic responses.
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PMID:Structural and immunological characterization of the N-glycans from the major yellow jacket allergen Ves v 2: the N-glycan structures are needed for the human antibody recognition. 1937 66


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