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Cysteine protease homologues

The N-terminal sequence of one peptide from the 35 kDa zone of H-gal-GP showed some homology to cathepsin B-like cysteine proteases. Molecular cloning has also identified a thrombospondin homologue associated with the diffusely staining region between zones A and B, a galectin associated with zone D (Newlands et al., 1999) and a low molecular weight (approximately 13 kDa) cysteine protease inhibitor, cystatin. [Pg.263]

Finken-Eigen, M. and Kunz, W. (1 997) Schistosoma mansoni gene structure and localization of a homologue to cysteine protease ER60. Experimental Parasitology 86, 1-7. [Pg.168]

Arabidopsis thaliana (mouse-ear cress) (Brassicaceae) Cysteine protease inhibitor (CPI) protein homologues (genes) (11-51 kDa proproteins) Cysteine protease inhibitor protein homologues [141- 146]... [Pg.592]

Solatium tuberosum (Solanaceae) [tuber] Potato Cysteine Protease Inhibitors (PCPIs) (20-25 kDa Kunitz PI homologues - for details see Table 12 ) Cysteine proteases (e.g. Papain, Cathepsins B, H L) - for details see Table 12 [185- 188]... [Pg.593]

While most Kunitz PIPs inhibit serine proteases, some Kunitz PIP homologues inhibit aspartic proteases or cysteine proteases. Thus various... [Pg.602]

Solanum Cysteine Protease Inhibitor (PCPI) (22 kDa) Solanum tuberosum (Solanaceae) [tuber] STI (KPI) homologue (CYSPR)... [Pg.554]

In the execution phase of apoptosis, caspase proteases are activated by various apoptotic stimuli. Caspases belong to the cysteine protease family and were originally identified as homologues of the ced- i (cell death abnormal) gene product (an executor of apoptosis in Caenorhabdi-tis elegans). Indeed, most caspases induce apoptosis if they are overexpressed in growing cells and cell death can be blocked by caspase-specific inhibitors. Therefore, caspases are accepted as executors for apoptosis in mammals and this pathway appears to be conserved between species. [Pg.6]


See other pages where Cysteine protease homologues is mentioned: [Pg.264]    [Pg.267]    [Pg.268]    [Pg.268]    [Pg.271]    [Pg.412]    [Pg.356]    [Pg.25]    [Pg.127]    [Pg.129]    [Pg.103]    [Pg.67]    [Pg.74]    [Pg.288]    [Pg.211]   
See also in sourсe #XX -- [ Pg.600 ]




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