L‑mimosine induces caspase‑9‑mediated apoptosis in human osteosarcoma cells.

07:00 EST 9th January 2018 | BioPortfolio

Summary of "L‑mimosine induces caspase‑9‑mediated apoptosis in human osteosarcoma cells."

L-mimosine is a rare plant amino acid extracted from Mimosa or Leucaena spp., and it has been reported to exhibit antitumor activity in a number of types of cancer. However, the underlying mechanisms remain to be clarified. In the present study, the effect of L‑mimosine was investigated in human osteosarcoma cells. A Cell Counting Kit‑8 assay and flow cytometry were used for toxicity detection. Hoechst staining and transmission electron microscopy (TEM), in addition to western blot analysis, were used for the examination of the associated mechanisms. The results of the present study indicated that L‑mimosine significantly inhibited cell proliferation by inducing cellular apoptosis in osteosarcoma cells. The Hoechst staining results and TEM revealed that nuclear damage increased with the concentration increase in L‑mimosine, as did the formation of apoptotic bodies. Additionally, the results of the western blot analysis confirmed that the treatment of cells with L‑mimosine was accompanied by increasing expression of cleaved caspase‑9. L‑mimosine‑induced apoptosis was inhibited by the caspase‑9 inhibitor Z‑LEHD‑FMK. In addition, the extracellular signal‑regulated kinase (ERK) signaling pathway was suppressed following treatment with L‑mimosine. In conclusion, the results of the present study suggested that L‑mimosine induced apoptosis via the mitochondrial apoptotic pathway. The ERK signaling pathway was indicated to be an additional mechanism underlying apoptosis induction. The results provided evidence for the use of L‑mimosine as a promising candidate for osteosarcoma therapy.


Journal Details

This article was published in the following journal.

Name: Molecular medicine reports
ISSN: 1791-3004


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Medical and Biotech [MESH] Definitions

An inhibitor of apoptosis protein that is translated by a rare cap-independent mechanism. It blocks caspase-mediated cellular destruction by inhibiting CASPASE 3; CASPASE 7; and CASPASE 9.

A short pro-domain caspase that plays an effector role in APOPTOSIS. It is activated by INITIATOR CASPASES such as CASPASE 7; CASPASE 8; and CASPASE 10. Isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA.

A short pro-domain caspase that plays an effector role in APOPTOSIS. It is activated by INITIATOR CASPASES such as CASPASE 3 and CASPASE 10. Several isoforms of this protein exist due to multiple alternative splicing of its MESSENGER RNA.

An APOPTOSIS-regulating protein that is structurally related to CASPASE 8 and competes with CASPASE 8 for binding to FAS ASSOCIATED DEATH DOMAIN PROTEIN. Two forms of CASP8 and FADD-like apoptosis regulating protein exist, a long form containing a caspase-like enzymatically inactive domain and a short form which lacks the caspase-like domain.

A long pro-domain caspase that contains a caspase recruitment domain in its pro-domain region. Caspase 9 is activated by pro-apoptotic factors that are released during cell stress and by CARD SIGNALING ADAPTOR PROTEINS. It activates APOPTOSIS by cleaving and activating EFFECTOR CASPASES.

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