Caspase-1 recognizes extended cleavage sites in its natural substrates.

ABSTRACT:

Objective

The preferred amino acids in the proteolytic sites have been considered to be similar between caspase-1 and caspase-9, which do not support their differential functions in inflammatory pyroptosis and apoptosis. We attempted to solve this problem.

Methods

We analyzed the flanking 20 amino acid residues in the cleavage sites in 34 caspase-1 and 11 capase-9 experimentally identified substrates.

Results

This study has made the following findings: first, we verified that caspase-1 and caspase-9 shared 100% aspartic acid in the P1 position. However, the structures in the cleavage sites of most caspase-1 substrates are different from that of caspase-9 substrates in the following three aspects, (a) the amino acid residues with the statistically high frequencies; (b)

SUBMITTER: Shen J 

PROVIDER: S-EPMC2917068 | biostudies-literature | 2010 Jun

REPOSITORIES: biostudies-literature