80
An antiproliferative RNase with a new N-terminal sequence was isolated from
fruiting bodies of the edible wild mushroom Russula delica. This novel RNase had
a molecular mass of 14 kDa. Its optimum pH and temperature were pH 5 and 60 °C,
respectively. The ranking of its activity toward various polyhomoribonucleotides
was poly (C) > poly (G) > poly (A) > poly (U). This RNase could inhibit proliferation of HepG2 and MCF-7 cancer cells with an IC 50 value of 8.6 μM and 7.2 μM,
respectively. It did not contain antifungal activity or inhibitory activity of HIV-1
reverse transcriptase (Zhao et al. 2010).
An RNase (14.5 kDa) was isolated from fresh fruiting bodies of the edible mushroom Lyophyllum shimeji. Its optimum pH and temperature were pH 6 and 70 °C,
respectively. It exhibited the highest ribonucleolytic potency toward poly (U), 25%
as much activity toward poly (C), and no activity toward poly (A) and poly (G) was
detectable. Its ribonucleolytic activity at 100 °C and 20 °C was similar. It inhibited
proliferation of hepatoma HepG2 cells and breast cancer MCF7 cells with an IC 50
of 10 μM and 6.2 μM, respectively and also inhibited the activity of HIV-1 reverse
transcriptase with an IC 50 of 7.2 μM (Zhang et al. 2010).
An RNase was purified from the fruiting bodies of the edible fungus Pleurotus
ostreatus. Its N-terminal sequence was different from that of the ribonucleases of
other fungi and the previously isolated Pleurotus ostreatus RNases. It exhibited a
molecular mass of 12 kDa. The RNase displayed an activity of 11,490 U/mg on
yeast tRNA. The highest ribonuclease activity was observed toward poly (U), followed by poly (A) and poly (C). No activity was shown toward poly (G). The optimum pH and temperature was 7 and 55 °C, respectively. It inhibited cell-free
translation in a rabbit reticulocyte lysate with an IC 50 of 240 nM (Ye and Ng 2003).
An RNase (29 kDa) cospecific for poly (A) and poly (U) was isolated from fruiting bodies of the mushroom Boletus griseus. Its N-terminal sequence showed some
similarity to those of RNases from the mushrooms Irpex lacteus and Lentinus
edodes. Its optimum temperature and pH were 60–70 °C and 3.5, respectively
(Wang and Ng 2006).
A 20 kDa RNase was isolated from fresh fruiting bodies of the cultured mushroom Schizophyllum commune. It exhibited maximal RNase activity at pH 6.0 and
70 °C. Its highest ribonucleolytic activity was toward poly (U) (379.5 μ/mg), the
second highest activity was toward poly (C) (244.7 μ/mg), and it had less activity
toward poly (A) (167.4 μ/mg) and toward poly (G) (114.5 μ/mg). The RNase inhibited HIV-1 reverse transcriptase with an IC 50 of 65 μM. Its N-terminal amino acid
sequence was similar to that reported for Volvariella volvacea as well as in their
optimum pH and polyhomoribonucleotide specificity, but some differences in chromatographic behavior and molecular mass were observed (Zhao et al. 2011).
5.7 Conclusions
Currently, chronic degenerative diseases are on the rise, so work must be done to
change the eating habits and sedentary lifestyle. Mushrooms are an important source
of bioactive peptides that should be included in the diet to help prevent and treat
diseases.
G. Díaz-Godínez and R. Díaz
An antiproliferative RNase with a new N-terminal sequence was isolated from
fruiting bodies of the edible wild mushroom Russula delica. This novel RNase had
a molecular mass of 14 kDa. Its optimum pH and temperature were pH 5 and 60 °C,
respectively. The ranking of its activity toward various polyhomoribonucleotides
was poly (C) > poly (G) > poly (A) > poly (U). This RNase could inhibit proliferation of HepG2 and MCF-7 cancer cells with an IC 50 value of 8.6 μM and 7.2 μM,
respectively. It did not contain antifungal activity or inhibitory activity of HIV-1
reverse transcriptase (Zhao et al. 2010).
An RNase (14.5 kDa) was isolated from fresh fruiting bodies of the edible mushroom Lyophyllum shimeji. Its optimum pH and temperature were pH 6 and 70 °C,
respectively. It exhibited the highest ribonucleolytic potency toward poly (U), 25%
as much activity toward poly (C), and no activity toward poly (A) and poly (G) was
detectable. Its ribonucleolytic activity at 100 °C and 20 °C was similar. It inhibited
proliferation of hepatoma HepG2 cells and breast cancer MCF7 cells with an IC 50
of 10 μM and 6.2 μM, respectively and also inhibited the activity of HIV-1 reverse
transcriptase with an IC 50 of 7.2 μM (Zhang et al. 2010).
An RNase was purified from the fruiting bodies of the edible fungus Pleurotus
ostreatus. Its N-terminal sequence was different from that of the ribonucleases of
other fungi and the previously isolated Pleurotus ostreatus RNases. It exhibited a
molecular mass of 12 kDa. The RNase displayed an activity of 11,490 U/mg on
yeast tRNA. The highest ribonuclease activity was observed toward poly (U), followed by poly (A) and poly (C). No activity was shown toward poly (G). The optimum pH and temperature was 7 and 55 °C, respectively. It inhibited cell-free
translation in a rabbit reticulocyte lysate with an IC 50 of 240 nM (Ye and Ng 2003).
An RNase (29 kDa) cospecific for poly (A) and poly (U) was isolated from fruiting bodies of the mushroom Boletus griseus. Its N-terminal sequence showed some
similarity to those of RNases from the mushrooms Irpex lacteus and Lentinus
edodes. Its optimum temperature and pH were 60–70 °C and 3.5, respectively
(Wang and Ng 2006).
A 20 kDa RNase was isolated from fresh fruiting bodies of the cultured mushroom Schizophyllum commune. It exhibited maximal RNase activity at pH 6.0 and
70 °C. Its highest ribonucleolytic activity was toward poly (U) (379.5 μ/mg), the
second highest activity was toward poly (C) (244.7 μ/mg), and it had less activity
toward poly (A) (167.4 μ/mg) and toward poly (G) (114.5 μ/mg). The RNase inhibited HIV-1 reverse transcriptase with an IC 50 of 65 μM. Its N-terminal amino acid
sequence was similar to that reported for Volvariella volvacea as well as in their
optimum pH and polyhomoribonucleotide specificity, but some differences in chromatographic behavior and molecular mass were observed (Zhao et al. 2011).
5.7 Conclusions
Currently, chronic degenerative diseases are on the rise, so work must be done to
change the eating habits and sedentary lifestyle. Mushrooms are an important source
of bioactive peptides that should be included in the diet to help prevent and treat
diseases.
G. Díaz-Godínez and R. Díaz