Euphorbia characias latex: Micromorphology of rubber particles and rubber transferase activity

Spanò, Delia; Pintus, Francesca; Esposito, Francesca; Loche, Danilo; Floris, Giovanni; Medda, Rosaria

doi:10.1016/j.plaphy.2014.12.008

Cited by 23 publications

(14 citation statements)

References 30 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Since the first isolation of cPTs, HRT1 and HRT2 from H. brasiliensis latex, as candidates for RTase (Asawatreratanakul et al, 2003), several homologous cDNAs have been isolated from other NR-producing plants, T. koksaghyz (Schmidt et al, 2010a; Schmidt et al, 2010b), L. sativa (Qu et al, 2015) and E. characias (Spanò et al, 2015). However, practical, functional identification of RTase was not accomplished to date, owing to the absence of in vitro RTase activity distinctly exhibited by recombinant cPTs.…”

Section: Discussionmentioning

confidence: 99%

“…While the recombinant proteins of HRT1 and HRT2, expressed in yeast and Arabidopsis showed significant activity, producing C 80–100 polyisoprenoids, they failed to produce longer chain products corresponding to NR (Takahashi et al, 2012). Recently, cPT homologues expressed in latex of other NR-producing plants, such as Russian dandelion ( Taraxacum koksaghyz ) (Schmidt et al, 2010a; Schmidt et al, 2010b), lettuce ( Lactuca sativa ) (Qu et al, 2015) and Euphorbia characias (Spanò et al, 2015), have been isolated, although their recombinant proteins show no RTase activity in vitro. RNA interference-mediated knock-down of cPTs expressed in the latex of Taraxacum brevicorniculatum have been shown to decrease latex rubber content (Post et al, 2012), suggesting the involvement of cPT in NR formation.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Identification and reconstitution of the rubber biosynthetic machinery on rubber particles from Hevea brasiliensis

Yamashita

Yamaguchi

Waki

et al. 2016

eLife

128

144

View full text Add to dashboard Cite

Natural rubber (NR) is stored in latex as rubber particles (RPs), rubber molecules surrounded by a lipid monolayer. Rubber transferase (RTase), the enzyme responsible for NR biosynthesis, is believed to be a member of the cis-prenyltransferase (cPT) family. However, none of the recombinant cPTs have shown RTase activity independently. We show that HRT1, a cPT from Heveabrasiliensis, exhibits distinct RTase activity in vitro only when it is introduced on detergent-washed HeveaRPs (WRPs) by a cell-free translation-coupled system. Using this system, a heterologous cPT from Lactucasativa also exhibited RTase activity, indicating proper introduction of cPT on RP is the key to reconstitute active RTase. RP proteomics and interaction network analyses revealed the formation of the protein complex consisting of HRT1, rubber elongation factor (REF) and HRT1-REF BRIDGING PROTEIN. The RTase activity enhancement observed for the complex assembled on WRPs indicates the HRT1-containing complex functions as the NR biosynthetic machinery.DOI: http://dx.doi.org/10.7554/eLife.19022.001

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Identification and reconstitution of the rubber biosynthetic machinery on rubber particles from Hevea brasiliensis

Yamashita

Yamaguchi

Waki

et al. 2016

eLife

128

144

View full text Add to dashboard Cite

show abstract

“…Among the Euphorbiaceae, the species Euphorbia characias is a typical shrub commonly occurring in vast areas of the Mediterranean basin. The plant latex has been object of extended research and its screening has revealed the presence of antioxidants and acetylcholinesterase inhibitors [ 14 ], a natural rubber [ 15 ], and various enzymes [ 16 – 18 ], some of these interacting in a common metabolism [ 19 ]. Besides the latex, recently the attention has been paid also to other parts of the plant [ 20 , 21 ].…”

Section: Introductionmentioning

confidence: 99%

Selected Enzyme Inhibitory Effects of Euphorbia characias Extracts

Fais

Era

Petrillo

et al. 2018

BioMed Research International

Self Cite

View full text Add to dashboard Cite

Extracts of aerial part of Euphorbia characias were examined to check potential inhibitors for three selected enzymes involved in several metabolic disorders. Water and ethanol extracts from leaves and flowers showed in vitro inhibitory activity toward α-amylase, α-glucosidase, and xanthine oxidase. IC50 values were calculated for all the extracts and the ethanolic extracts were found to exert the best effect. In particular, for the α-glucosidase activity, the extracts resulted to be 100-fold more active than the standard inhibitor. The inhibition mode was investigated by Lineweaver-Burk plot analysis. E. characias extracts display different inhibition behaviors toward the three enzymes acting as uncompetitive, noncompetitive, and mixed-type inhibitors. Moreover, ethanolic extracts of E. characias showed no cytotoxic activity and exhibited antioxidant capacity in a cellular model. The LC-DAD metabolic profile was also performed and it showed that leaves and flowers extracts contain high levels of quercetin derivatives. The results suggest that E. characias could be a promising source of natural inhibitors of the enzymes involved in carbohydrate uptake disorders and oxidative stress.

show abstract

“…E. characias latex has been studied with regard to its antioxidant and non-protein components ( Pintus et al, 2013 ) but several proteins have been isolated and deeply characterized ( Mura et al, 2008 ; Pintus et al, 2009 ; Pintus et al, 2011 ; Dainese et al, 2014 ; Spanò et al, in press ). It has also been identified in E. characias , a cis -prenyl transferase ( Spanò et al, 2015 ) which is the enzyme responsible of the synthesis of the natural rubber occurring in the plant latex ( Spanò et al, 2012 ).…”

Section: Introductionmentioning

confidence: 99%

Antityrosinase activity ofEuphorbia characiasextracts

Pintus

Spanò

Corona

et al. 2015

PeerJ

Self Cite

View full text Add to dashboard Cite

Tyrosinase is a well-known key enzyme in melanin biosynthesis and its inhibitors have become increasingly important because of their potential use as hypopigmenting agents. In the present study, the anti-melanogenic effect of aqueous and ethanolic extracts from Euphorbia characias leaves, stems, and flowers in cell-free and cellular systems was examined. All the extracts showed inhibitory effects against mushroom tyrosinase with leaf extracts exhibiting the lowest IC50 values of 24 and 97 µg/mL for aqueous and ethanolic extracts respectively. Enzyme kinetic analysis indicated that leaf aqueous extract acts as a mixed type inhibitor, while ethanolic extract shows a competitive inhibition effect on mushroom tyrosinase using L-DOPA as substrate. In addition, the inhibitory effect of leaf extracts on tyrosinase activity and melanin production was examined in murine melanoma B16F10 cells. Cellular tyrosinase activity as well as levels of melanin synthesis are reduced in a dose-dependent manner by extracts in cells treated with α-melanocyte stimulating hormone (α-MSH). The effects are comparable, and sometimes even better, than that of kojic acid, a well known tyrosinase inhibitor used for reference. All these results suggest that E. characias could be a great source of the natural inhibitors from tyrosinase and has the potential to be used as a whitening agent in therapeutic fields.

show abstract

Euphorbia characias latex: Micromorphology of rubber particles and rubber transferase activity

Cited by 23 publications

References 30 publications

Identification and reconstitution of the rubber biosynthetic machinery on rubber particles from Hevea brasiliensis

Identification and reconstitution of the rubber biosynthetic machinery on rubber particles from Hevea brasiliensis

Selected Enzyme Inhibitory Effects of Euphorbia characias Extracts

Antityrosinase activity ofEuphorbia characiasextracts

Contact Info

Product

Resources

About