Suppressive activity of protease inhibitors from buckwheat seeds against human T-acute lymphoblastic leukemia cell lines

• Published in: Applied biochemistry and biotechnology Vol. 117; no. 2; pp. 65 - 74
• Main Authors: Park, S.S, Ohba, H
• Format: Journal Article
• Language: English
• Published: Heidelberg Springer 01.05.2004; Springer Nature B.V
• Subjects: Acute lymphoblastic leukemia; Allergens - chemistry; Allergens - pharmacology; Allergens - therapeutic use; anticarcinogenic activity; Antigens, Plant; antineoplastic agents; Antineoplastic Agents - pharmacology; Antineoplastic Agents - therapeutic use; Apoptosis; Biochemistry; Biological and medical sciences; Biotechnology; Buckwheat; Cell death; Cell Line, Tumor; Chymotrypsin; Chymotrypsin - antagonists & inhibitors; DNA fragmentation; Fagopyrum esculentum; Fundamental and applied biological sciences. Psychology; Homology; Humans; Jurkat Cells; Leukemia; Leukemia-Lymphoma, Adult T-Cell - drug therapy; Lymphocytes; Lymphocytes T; Plant Proteins - chemistry; Plant Proteins - pharmacology; Plant Proteins - therapeutic use; Potatoes; Protease; Protease inhibitors; Protease Inhibitors - pharmacology; Proteinase inhibitors; Proteins; Solanum tuberosum; Studies; Subtilisin; Subtilisin - antagonists & inhibitors; Trypsin; Trypsin - chemistry; Tumor cell lines; Human; Polygonaceae; Stem cell; Hematopoietic cell; T-acute lymphoblastic leukemia; Cell line; buckwheat; Dicotyledones; Angiospermae; tumor hematopoietic stem cell; Spermatophyta; Fagopyrum esculentum; Tumor cell; Protease inhibitor; Apoptosis
• ISSN: 0273-2289; 1559-0291; 0273-2289
• DOI: 10.1385/ABAB:117:2:065

The buckwheat protease inhibitor designated BWI-1, a member of the potato inhibitor I family, inhibits trypsin, chymotrypsin, and subtilisin, whereas the buckwheat protease inhibitor designated BWI-2a, a novel protease inhibitor homologous to the vicilin family, inhibits only trypsin. We examined the suppressive activity of BWI-1 and BWI-2a against T-acute lymphoblastic leukemia (T-ALL) cells, such as JURKAT and CCRF-CEM, and human normal blood lymphocytes. Both inhibitors significantly suppressed the growth of T-ALL cells as judged by the soluble 3-(4,5-dimethylthiazol-2-yl)-2,5-diphenyl tetrazolium bromide (tetrazolium/formazan assay). JURKAT cells showed slightly higher susceptibility to buckwheat inhibitors than CCRF-CEM cells. Modification of Arg residue(s) in inhibitors by 1,2-cyclohexandione inactivated their trypsin inhibitory activity, considerably abolishing their suppressive activity. This suggests that the trypsin inhibitory activity is involved in the suppression of growth of human T-ALL cell lines. It was further found that both inhibitors triggered programmed cell death (apoptosis) of these cell strains with DNA fragmentation.