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Squamous cell carcinoma antigen 1 is an inhibitor of parasite‐derived cysteine proteases
Author(s) -
Kanaji Sachiko,
Tanaka Yoko,
Sakata Yasuhisa,
Takeshita Kohei,
Arima Kazuhiko,
Ohta Shoichiro,
Hansell Elizabeth J.,
Caffrey Conor,
Mottram Jeremy C.,
Lowther Jonathan,
Donnelly Sheila,
Stack Colin,
Kadowaki Tomoko,
Yamamoto Kenji,
McKerrow James H.,
Dalton John P.,
Coombs Graham H.,
Izuhara Kenji
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.07.072
Subject(s) - proteases , cysteine protease , cysteine , biology , trypanosoma cruzi , cathepsin , cysteine proteinase inhibitors , antigen , cathepsin l , biochemistry , protease , trypanosoma , cystatin , parasite hosting , cathepsin b , ovalbumin , microbiology and biotechnology , enzyme , immunology , virology , cystatin c , programmed cell death , apoptosis , caspase , renal function , world wide web , computer science
The physiological significance of the squamous cell carcinoma antigens 1 (SCCA1) and SCCA2, members of the ovalbumin serpin family, remains unresolved. In this study, we examined whether SCCA1 or SCCA2 inhibits protozoa‐ or helminth‐derived cysteine proteases. SCCA1, but not SCCA2, potently inhibited the cysteine protease activities of CPB2.8 from Leishmania mexicana , cruzain from Trypanosoma cruzi , rhodesain from Trypanosoma brucei rhodesience , and cathepsin L2 from Fasciola hepatica . The inhibitory activities of SCCA1 were due to its resistance to cleavage by the cysteine proteases. The findings indicate that induction of cysteine protease inhibitors might be a novel defense mechanism against parasite development.