RRC ID 72864
著者 Fujii H, Nakajima M, Aoyagi T, Tsuruo T.
タイトル Inhibition of tumor cell invasion and matrix degradation by aminopeptidase inhibitors.
ジャーナル Biol Pharm Bull
Abstract We investigated the effects of several types of aminopeptidase inhibitors on tumor cell-associated aminopeptidase activity and invasion. The aminopeptidase expressed by the human metastatic HT1080 fibrosarcoma cells was effectively suppressed by actinonin A, bestatin, leuhistin and matlystatin A, which are capable of inhibiting the purified aminopeptidase N, but not by arphamenine B specific for aminopeptidase B. The aminopeptidase N inhibitors inhibited HT1080 cells from degrading the subendothelial matrix and from invading into Matrigel in parallel with their aminopeptidase inhibitory activities. Matlystatin A, with multiple inhibitory activity against both aminopeptidase N and matrix metalloproteinases (MMP), was the most effective inhibitor of invasion. However, leuhistin and bestatin, without MMP inhibitory activity, also exhibited significant inhibition of invasion. The results suggest that aminopeptidase N plays a crucial role in the degradation and invasion of extracellular matrices by fibrosarcoma cells and that aminopeptidase inhibitors may be useful for preventing the spread of malignant tumors.
巻・号 19(1)
ページ 6-10
公開日 1996-1-1
DOI 10.1248/bpb.19.6
PMID 8820902
MeSH Aminopeptidases / antagonists & inhibitors* Antineoplastic Agents / pharmacology* Endothelium, Vascular / cytology Endothelium, Vascular / drug effects Endothelium, Vascular / enzymology Enzyme Inhibitors / pharmacology* Extracellular Matrix / drug effects* Fibrosarcoma / drug therapy Fibrosarcoma / pathology Gelatinases / antagonists & inhibitors Humans Neoplasm Invasiveness Tumor Cells, Cultured
IF 1.863
リソース情報
ヒト・動物細胞 THP-1(RCB1189)