Human and mouse perforin are processed in part through cleavage by the lysosomal cysteine proteinase cathepsin L
Spela Konjar, Vivien R Sutton, Sabine Hoves, Urska Repnik, Hideo Yagita, Thomas Reinheckel, Christoph Peters, Vito Turk, Boris Turk, Joseph A Trapani, Natasa Kopitar-Jerala
Immunology | WILEY | Published : 2010
Awarded by Research Agency of the Republic of Slovenia
Awarded by National Health and Medical Research Council (NHMRC) of Australia
Awarded by NMHRC
Awarded by Deutsche Forschungsgemeinschaft
The authors thank Eric Vivier and Phillip Bird for NK-92 and K562 cells; Mark Smyth for the YT 5 cell line, Garnett Suck for KHYG1, Frank Carbone for EL-4, Marko Mihelic for active recombinant mouse Cat L, James Powers for granzyme B substrate, and Jose Villadangos for making the CatL<SUP>-/-</SUP> mice available for Australian investigators. This work was supported by the Research Agency of the Republic of Slovenia, grant P-0140 (to V.T. and B.T.) and S.K. was supported by Slovenian human resources development and scholarship foundation, Slovenia. J.A.T. and V.R.S. are supported by a programme grant from the National Health and Medical Research Council (NHMRC; 454569) of Australia. J.A.T. received a senior fellowship (288999) from NMHRC. S.H. was supported by Deutsche Forschungsgemeinschaft (Ho 4007/1-1).