Comparison of cysteine peptidase activities in Trichobilharzia regenti and Schistosoma mansoni cercariae
Jazyk angličtina Země Anglie, Velká Británie Médium print-electronic
Typ dokumentu srovnávací studie, časopisecké články, práce podpořená grantem
Grantová podpora
072255/Z/03/Z
Wellcome Trust - United Kingdom
PubMed
17517170
DOI
10.1017/s0031182007002910
PII: S0031182007002910
Knihovny.cz E-zdroje
- MeSH
- cysteinové endopeptidasy účinky léků metabolismus MeSH
- diazomethan analogy a deriváty farmakologie MeSH
- gelová chromatografie MeSH
- inhibitory proteas farmakologie MeSH
- keratiny metabolismus MeSH
- kolagen metabolismus MeSH
- koncentrace vodíkových iontů MeSH
- leucin analogy a deriváty metabolismus MeSH
- Schistosoma mansoni enzymologie MeSH
- Schistosomatidae enzymologie MeSH
- vazebná místa MeSH
- želatina metabolismus MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- práce podpořená grantem MeSH
- srovnávací studie MeSH
- Názvy látek
- benzyloxycarbonylphenylalanylalanine diazomethyl ketone MeSH Prohlížeč
- cysteinové endopeptidasy MeSH
- DCG 04 MeSH Prohlížeč
- diazomethan MeSH
- inhibitory proteas MeSH
- keratiny MeSH
- kolagen MeSH
- leucin MeSH
- želatina MeSH
Cercariae of the bird schistosome Trichobilharzia regenti and of the human schistosome Schistosoma mansoni employ proteases to invade the skin of their definitive hosts. To investigate whether a similar proteolytic mechanism is used by both species, cercarial extracts of T. regenti and S. mansoni were biochemically characterized, with the primary focus on cysteine peptidases. A similar pattern of cysteine peptidase activities was detected by zymography of cercarial extracts and their chromatographic fractions from T. regenti and S. mansoni. The greatest peptidase activity was recorded in both species against the fluorogenic peptide substrate Z-Phe-Arg-AMC, commonly used to detect cathepsins B and L, and was markedly inhibited (> 96%) by Z-Phe-Ala-CHN2 at pH 4.5. Cysteine peptidases of 33 kDa and 33-34 kDa were identified in extracts of T. regenti and S. mansoni cercariae employing a biotinylated Clan CA cysteine peptidase-specific inhibitor (DCG-04). Finally, cercarial extracts from both T. regenti and S. mansoni were able to degrade native substrates present in skin (collagen II and IV, keratin) at physiological pH suggesting that cysteine peptidases are important in the pentration of host skin.
Citace poskytuje Crossref.org
Avian schistosomes and outbreaks of cercarial dermatitis
Cercarial dermatitis, a neglected allergic disease
Pathogenicity of Trichobilharzia spp. for Vertebrates