Study of response of Swiss Webster mice to light subunit of mushroom tyrosinase

Ismaya, Wangsa T.; Efthyani, Alida; Retnoningrum, Debbie Soefie; Lai, Xuelei; Dijkstra, Bauke W.; Tjandrawinata, Raymond R.; Rachmawati, Heni

doi:10.1080/10520295.2017.1339912

Cited by 7 publications

(6 citation statements)

References 12 publications

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“…A preliminary immunogenicity test in Swiss Webster mice suggested that Abmb does not evoke a response of the immune system [20]. Further toxicity and immunogenicity tests with the inbreed and outbreed mice showed that Abmb was safe after prolonged administration at an elevated dose [64,65]. These results strengthen the safety profile of Abmb.…”

Section: Abmbmentioning

confidence: 66%

Lectins from the Edible Mushroom Agaricus bisporus and Their Therapeutic Potentials

Ismaya¹,

Tjandrawinata²,

Rachmawati

2020

Molecules

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The mushroom Agaricus bisporus secretes biologically active compounds and proteins with benefits for human health. Most reported proteins from A. bisporus are tyrosinases and lectins. Lectins are of therapeutic or pharmaceutical interest. To date, only limited information is available on A. bisporus lectins and lectin-like proteins. No therapeutic products derived from A. bisporus lectin (ABL) are available on the market despite its extensive exploration. Recently, A. bisporus mannose-binding protein (Abmb) was discovered. Its discovery enriches the information and increases the interest in proteins with therapeutic potential from this mushroom. Furthermore, the A. bisporus genome reveals the possible occurrence of other lectins in this mushroom that may also have therapeutic potential. Most of these putative lectins belong to the same lectin groups as ABL and Abmb. Their relationship is discussed. Particular attention is addressed to ABL and Abmb, which have been explored for their potential in medicinal or pharmaceutical applications. ABL and Abmb have anti-proliferative activities toward cancer cells and a stimulatory effect on the immune system. Possible scenarios for their use in therapy and modification are also presented.

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Section: Abmbmentioning

confidence: 66%

Lectins from the Edible Mushroom Agaricus bisporus and Their Therapeutic Potentials

Ismaya¹,

Tjandrawinata²,

Rachmawati

2020

Molecules

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“…Production and Purification of rLSMT rLSMT was prepared according to the previous report. 9) Briefly, E. coli BL21 (DE3)-rLSMT was grown at 37°C in LB medium containing 100 µg/mL ampicillin for 10-12 h (overnight). Protein expression was induced by the addition of IPTG to a final concentration of 0.05 mM.…”

Section: Methodsmentioning

confidence: 99%

“…Permeability Study The permeability study was performed by the non-everted gut sac method as previously reported. 9) First, a Wistar rat was acclimatized without food but with free access to drink water for 12 h prior to sacrificing it in a CO 2 chamber (3-4 min at 30% CO 2 ). The jejunum was collected and immediately divided into three of five-centimeter segments.…”

Section: Methodsmentioning

confidence: 99%

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Bioconjugation of Captopril–Light Subunit of <i>Agaricus bisporus</i> Mushroom Tyrosinase: Characterization and Potential Use as a Drug Carrier for Oral Delivery

Diana

Ismaya²,

Meidianto³

et al. 2018

Biological & Pharmaceutical Bulletin

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We show that a lectin like protein from the mushroom Agaricus bisporus (LSMT) is capable to permeate the epithelial monolayer barrier of the intestine ex vivo. The protein is not toxic or immunogenic upon prolonged administration and elevated dose in mice. Thus, it could be a candidate as a drug carrier for oral administration. However, its permeability should be tested after the protein has been modified, mimicking the condition in which it is used as a drug carrier. The protein was conjugated to captopril, the selected model of a Biopharmaceutical Classification System (BCS) class III drug, with high solubility but poor permeability. The drug was conjugated to LSMT that had been modified with 4-succinimidyloxycarbonyl-alpha-methyl-2-pyridyldithiotoluene (SMPT) as a linker. The success of LSMT modification was confirmed with TLC and MS; the latter also indicated the amount of captopril molecule linked. The modified LSMT could permeate through the intestinal monolayer barrier, and thus could be absorbed in the intestine after modification. The modified protein appears to remain stable after incubation in simulated gastrointestinal fluids. This pioneering work provides an essential basis for further development of the protein as a drug carrier for oral administration.

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“…In particular, tyrosinase from common white button mushrooms Agaricus bisporus ( TyrAB ), with broad availability compared with human tyrosinase, has been used in the development of TYR–inhibitors compounds [ 25 ]. Recently, it has been described that novel functions or novel activities of some part of them, especially light subunit Orf239342, are very important in cancer proliferation inhibition [ 26 , 27 , 28 , 29 ].…”

Section: Introductionmentioning

confidence: 99%

In Vitro Antiviral Activity of Tyrosinase from Mushroom Agaricus bisporus against Hepatitis C Virus

et al. 2021

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Tyrosinases from a commercial Agaricus bisporus protein extract and directly isolated from white mushrooms were purified in order to obtaining the well-known tyrosinase from A. bisporus (TyrAB) of 45 kDa and a newly discovered 50 kDa tyrosinase isoform (Tyr50 kDa), and tested showing high antiviral activity against the hepatitis C virus for the first time. Cell toxicity and antiviral activity of tyrosinases were determined in cultured Huh 5-2 liver tumor cells transfected with a replicon system (a plasmid that includes all non-structural hepatitis C virus proteins and replicates autonomously). TyrAB was able to inhibit the replication of the hepatitis C virus without inducing toxicity in liver cells. In addition, the post-translational isoform Tyr50 kDa showed higher antiviral capacity than the former (up to 10 times greater), also exhibiting 10 times higher activity than the commercial drug Ribavirin®. This antiviral activity was directly proportional to the enzymatic activity of tyrosinases, as no antiviral capacity was observed in the inactive form of the enzymes. The tyrosinases approach could represent a new antiviral inhibition mechanism, through a plausible catalytic mechanism of selective hydroxylation of the key role of tyrosine residues in viral proteases.

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Study of response of Swiss Webster mice to light subunit of mushroom tyrosinase

Cited by 7 publications

References 12 publications

Lectins from the Edible Mushroom Agaricus bisporus and Their Therapeutic Potentials

Lectins from the Edible Mushroom Agaricus bisporus and Their Therapeutic Potentials

Bioconjugation of Captopril–Light Subunit of <i>Agaricus bisporus</i> Mushroom Tyrosinase: Characterization and Potential Use as a Drug Carrier for Oral Delivery

In Vitro Antiviral Activity of Tyrosinase from Mushroom Agaricus bisporus against Hepatitis C Virus

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