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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 
MeSH Review

Forsythia

 
 
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Disease relevance of Forsythia

  • CIP shows a very variable activity according to anaerobic bacteria species, being particularly inactive against P. gingivalis and very efficient against T. forsythia and P. micros [1].
 

High impact information on Forsythia

  • In this study, the approximately 32-kDa NAD-dependent secoisolariciresinol dehydrogenase, which catalyzes the enantiospecific conversion of (-)-secoisolariciresinol into (-)-matairesinol in Forsythia intermedia, was purified >6,000-fold to apparent homogeneity [2].
  • (+)-Pinoresinol/(+)-lariciresinol reductase from Forsythia intermedia. Protein purification, cDNA cloning, heterologous expression and comparison to isoflavone reductase [3].
  • The enzyme was found in Forsythia intermedia and catalyzes the presumed regulatory branch-points in the pathway leading to benzylaryltetrahydrofuran, dibenzylbutane, dibenzylbutyrolactone, and aryltetrahydronaphthalene lignans [4].
  • In vivo labeling experiments of Forsythia intermedia plant tissue with [8-14C]- and [9,9-2H2,OC2H3]coniferyl alcohols revealed that the lignans, (-)-secoisolariciresinol and (-)-matairesinol, were derived from two coniferyl alcohol molecules; no evidence for the formation of the corresponding (+)-enantiomers was found [5].
  • The antibodies predominantly recognized a protein band with a molecular mass of 28 kD on western analysis of tissue extracts from zinnia, forsythia (Forsythia suspensa), tobacco (Nicotiana tabacum), alfalfa (Medicago sativa), and soybean (Glycine max) [6].
 

Biological context of Forsythia

 

Anatomical context of Forsythia

  • Chromoplasts having a globular inner structure in the petals of Forsythia suspensa can form starch grains in their stroma when incubated with glucose solution [8].
 

Associations of Forsythia with chemical compounds

 

Gene context of Forsythia

  • P. gingivalis and T. forsythia induced an increase in RANTES secretion, whereas T. denticola alone or in combination resulted in a significant decrease in RANTES levels [14].
  • These results suggested that Forsythia suspense consisted of both negative and positive regulatory components on RANTES and MCP-1 secretion in H1N1-infected A549 cells, respectively [15].
  • RESULTS: NDM dose-dependently inhibited the proteinases of P. gingivalis, T. forsythia and T. denticola as well as type I collagen and transferrin degradation by P. gingivalis [16].
  • METHODS: The effect of NDM on gingipain and dipeptidyl peptidase IV (DPP IV) activities of P. gingivalis, trypsin-like activity of T. forsythia and chymotrypsin-like activity of T. denticola was evaluated using synthetic chromogenic peptides [16].

References

  1. Antimicrobial susceptibility variation of 50 anaerobic periopathogens in aggressive periodontitis: an interindividual variability study. Lakhssassi, N., Elhajoui, N., Lodter, J.P., Pineill, J.L., Sixou, M. Oral Microbiol. Immunol. (2005) [Pubmed]
  2. Secoisolariciresinol dehydrogenase purification, cloning, and functional expression. Implications for human health protection. Xia, Z.Q., Costa, M.A., Pelissier, H.C., Davin, L.B., Lewis, N.G. J. Biol. Chem. (2001) [Pubmed]
  3. (+)-Pinoresinol/(+)-lariciresinol reductase from Forsythia intermedia. Protein purification, cDNA cloning, heterologous expression and comparison to isoflavone reductase. Dinkova-Kostova, A.T., Gang, D.R., Davin, L.B., Bedgar, D.L., Chu, A., Lewis, N.G. J. Biol. Chem. (1996) [Pubmed]
  4. Stereospecificity of (+)-pinoresinol and (+)-lariciresinol reductases from Forsythia intermedia. Chu, A., Dinkova, A., Davin, L.B., Bedgar, D.L., Lewis, N.G. J. Biol. Chem. (1993) [Pubmed]
  5. Formation of lignans (-)-secoisolariciresinol and (-)-matairesinol with Forsythia intermedia cell-free extracts. Umezawa, T., Davin, L.B., Lewis, N.G. J. Biol. Chem. (1991) [Pubmed]
  6. Association of caffeoyl coenzyme A 3-O-methyltransferase expression with lignifying tissues in several dicot plants. Ye, Z.H. Plant Physiol. (1997) [Pubmed]
  7. Purification and characterisation of an antifreeze protein from Forsythia suspensa (L.). Simpson, D.J., Smallwood, M., Twigg, S., Doucet, C.J., Ross, J., Bowles, D.J. Cryobiology (2005) [Pubmed]
  8. Light and electron microscopic investigation of in vitro starch synthesis in chromoplasts. Keresztes, A., Schróth, A. Cytobios (1979) [Pubmed]
  9. Reduction of coenzyme A thioesters of cinnamic acids with an enzyme preparation from lignifying tissue of Forsythia. Gross, G.G., Kreiten, W. FEBS Lett. (1975) [Pubmed]
  10. Formation of the lignan, (-) secoisolariciresinol, by cell free extracts of Forsythia intermedia. Umezawa, T., Davin, L.B., Lewis, N.G. Biochem. Biophys. Res. Commun. (1990) [Pubmed]
  11. Preparative isolation and purification of phillyrin from the medicinal plant Forsythia suspensa by high-speed counter-current chromatography. Li, H.B., Chen, F. Journal of chromatography. A. (2005) [Pubmed]
  12. Effects of forsythia fruit extracts and lignan on lipid metabolism. Cho, S.H., Rhee, S.J., Choi, S.W., Choi, Y. Biofactors (2004) [Pubmed]
  13. Studies on the Chinese crude drug "Forsythiae Fructus." VI. The structure and antibacterial activity of suspensaside isolated from Forsythia suspensa. Nishibe, S., Okabe, K., Tsukamoto, H., Sakushima, A., Hisada, S., Baba, H., Akisada, T. Chem. Pharm. Bull. (1982) [Pubmed]
  14. Inflammatory responses of a macrophage/epithelial cell co-culture model to mono and mixed infections with Porphyromonas gingivalis, Treponema denticola, and Tannerella forsythia. Bodet, C., Chandad, F., Grenier, D. Microbes Infect. (2006) [Pubmed]
  15. Dual regulatory effect of plant extracts of Forsythia suspense on RANTES and MCP-1 secretion in influenza A virus-infected human bronchial epithelial cells. Ko, H.C., Wei, B.L., Chiou, W.F. Journal of ethnopharmacology. (2005) [Pubmed]
  16. Inhibition of periodontopathogen-derived proteolytic enzymes by a high-molecular-weight fraction isolated from cranberry. Bodet, C., Piché, M., Chandad, F., Grenier, D. J. Antimicrob. Chemother. (2006) [Pubmed]
 
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