Abstract:
:Luffin-a, a single-chain Type I ribosome-inactivating protein, which is known to be the most toxic of the luffin family and apparently possesses antitumor activity, was isolated from Luffa cylindrica seeds. In the present study, mature alpha-luffin was cloned from L. cylindrica and it was found that mature alpha-luffin shared 96% amino acid similarity with luffin-a. The recombinant mature alpha-luffin was successfully expressed in a partly soluble form in Escherichia coli after optimization of expression conditions. The effects of the recombinant protein on bacterial growth and its in vitro protein synthesis inhibition activity were tested. Then, its antitumor activities against different human cancer cell lines were evaluated by CCK-8 assay and flow cytometry. The results indicated that the recombinant alpha-luffin was slightly toxic to E. coli. It could inhibit protein synthesis in the rabbit reticulocyte lysate system. At the same time, it inhibited the growth of the tumor cell lines in a dose- and time-dependent manner. Additionally, recombinant alpha-luffin was able to induce cell death by apoptosis. The cytotoxicity of alpha-luffin towards tumor cells makes it a potential antitumor agent.
journal_name
Acta Biochim Biophys Sin (Shanghai)journal_title
Acta biochimica et biophysica Sinicaauthors
Liu L,Wang R,He W,He F,Huang Gdoi
10.1093/abbs/gmq056subject
Has Abstractpub_date
2010-08-01 00:00:00pages
585-92issue
8eissn
1672-9145issn
1745-7270pii
gmq056journal_volume
42pub_type
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