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)

In the present study streptococci of serological group B isolated from canines (n=48) and felines (n=7) were comparatively investigated with group B streptococci from humans and bovines for cultural, biochemical and serological properties for antibiotic resistancies and by molecular analysis. An identification was performed with group B-specific antiserum, biochemical reactions, by PCR amplification and subsequent endonuclease digestion of the 16S rRNA gene and by amplification of species-specific parts of the 16S rDNA the 16S-23S rDNA intergenic spacer region and the CAMP factor gene cfb. Phenotypic similarities of group B streptococci of canine and feline origin with group B streptococci from humans and differences to group B streptococci of bovine origin could be observed in lactose fermentation, serotype patterns, pigmentation, growth properties of the bacteria in fluid medium and soft agar, hemagglutination reactions and in minocycline and tetracycline resistance. A negative hyaluronidase plate test, a hylB amplicon with a size of 4.6 kb and an insertion sequence 1548 could be observed among canine, feline and human group B streptococci of serotype III. The remaining hyaluronidase positive strains, also including all isolates of bovine origin, had a hylB gene with a size of 3.3 kb. Further genotypic differences could be observed in the occurrence of the genes lmb and scpB which appeared generally among canine, feline and human group B streptococci, but less pronounced among bovine isolates of this species. According to the presented data group B streptococci of canine and feline origin seemed to be more related to human than to bovine isolates of this species possibly indicating some epidemiological relation.
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PMID:Pheno- and genotypic properties of streptococci of serological group B of canine and feline origin. 1211 33

The aim of this study was to investigate the phenotypic and genotypic characteristics of Streptococcus uberis isolated from subclinical mastitis (SCM) cases, and to examine the possible association between both characteristics. A total of 32 S. uberis were isolated from 772 quarter milk samples (SCM > 250,000 cells/ml) collected from 195 cows selected randomly from 18 dairy farms located in Argentina. The S. uberis strains were characterized phenotypically by the presence of virulence factors as plasminogen activator factor (PAF), hyaluronidase (HYA), capsule (CAP) and CAMP factor, and were further characterized genotypically by pulsed-field gel electrophoresis (PFGE). S. uberis strains expressed plasminogen activator factor, hyaluronidase or capsule (65.5 %, 56.3 %, 59.4 %, respectively), but only 25 % of isolates were CAMP factor positive. Thirteen different virulence profiles were identified on the basis of the combination of virulence factors. Eighteen PFGE patterns with 90% of similarity were identified among 32 S. uberis. A great diversity of virulence profiles and PFGE patterns were present among dairy farms. S. uberis strains with the same PFGE pattern showed different virulence profiles. Bovine S. uberis strains causing SCM included in the present study showed heterogeneity in regard to their phenotypic and genotypic characteristics, and the PFGE patterns are not associated with the virulence profiles.
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PMID:Phenotypic and genotypic characterization of Streptococcus uberis isolated from bovine subclinical mastitis in Argentinean dairy farms. 2243 Sep 96

Hyaluronan (HA) in the endothelial glycocalyx serves as a mechanotransducer for high-shear-stress-stimulated endothelial nitric oxide synthase (eNOS) phosphorylation and nitric oxide (NO) production. Low shear stress (LSS) has been shown to contribute to endothelial inflammation and atherosclerosis by impairing the barrier and mechanotransduction properties of the glycocalyx. Here we focus on the possible role of hyaluronidase 2 (HYAL2) in LSS-induced glycocalyx impairment and the resulting alterations in eNOS phosphorylation and NO production in human umbilical vein endothelial cells (HUVECs). We show that LSS strongly activates HYAL2 to degrade HA in the glycocalyx. The dephosphorylation of eNOS-Ser-633 under LSS was triggered after HA degradation by hyaluronidase and prevented by repairing the glycocalyx with high-molecular weight hyaluronan. Knocking down HYAL2 in HUVECs protected against HA degradation in the glycocalyx by inhibiting the expression and activity of HYAL2 and further blocked the dephosphorylation of eNOS-Ser-633 and the decrease in NO production in response to LSS. The LSS-induced dephosphorylation of PKA was completely abrogated in HYAL2 siRNA-transfected HUVECs. The LSS-induced dephosphorylation of eNOS-Ser-633 was also reversed by the PKA activator 8-Br-cAMP. We thus suggest that LSS inhibits eNOS-Ser-633 phosphorylation and, at least partially, NO production by activating HYAL2 to degrade HA in the glycocalyx.
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PMID:The role of HYAL2 in LSS-induced glycocalyx impairment and the PKA-mediated decrease in eNOS-Ser-633 phosphorylation and nitric oxide production. 2779 30


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