Abstract:
:The aim of this study was to isolate and purify Rhizoma Pinelliae trypsin inhibitor (RPTI), determine its N-terminal amino acid sequence and evaluate its inhibitory effect on the proliferation of poorly differentiated BGC-823 human gastric adenocarcinoma cells. RPTI was separated and purified from a 40% (NH4)2SO4 precipitate of crude protein extract of Pinellia ternata tuber using affinity chromatography with trypsin as the ligand. The N-terminal amino acid sequence of RPTI was determined using the Edman degradation method. The inhibitory effect of RPTI on BGC-823 cell proliferation was detected in vitro using the MTT method and in vivo in tumour-bearing mice. The purified RPTI showed a single band under SDS-PAGE, its molecular weight was 14 kDa and its N-terminal amino acid sequence was DPVVDG. RPTI inhibited trypsin activity, with an inhibition ratio of 1:6.78 (mass). RPTI significantly inhibited the proliferation of BGC-823 cells in vitro. The IC50 of RPTI was 16.96 μg/ml within 48 h after treatment and 9.61 μg/ml within 72 h after treatment. Subcutaneous injection of RPTI around the tumour significantly inhibited BGC-823 tumour growth in mice. The tumour inhibitory effect was concentration- and dose-dependent. RPTI did not significantly influence the spleen coefficient of the mice. In conclusion, RPTI is a serine proteinase inhibitor with antitumour activity.
journal_name
Exp Ther Medjournal_title
Experimental and therapeutic medicineauthors
Zu G,Wang H,Wang J,Dou Y,Zhao W,Sun Ydoi
10.3892/etm.2014.1701subject
Has Abstractpub_date
2014-07-01 00:00:00pages
248-254issue
1eissn
1792-0981issn
1792-1015pii
etm-08-01-0248journal_volume
8pub_type
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journal_title:Experimental and therapeutic medicine
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journal_title:Experimental and therapeutic medicine
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journal_title:Experimental and therapeutic medicine
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