[HTML][HTML] Carboxyl-terminal Prodomain-deleted Human Leukocyte Elastase and Cathepsin G Are Efficiently Targeted to Granules and Enzymatically Activated in the …
U Gullberg, A Lindmark, G Lindgren… - Journal of Biological …, 1995 - ASBMB
The hematopoietic neutral serine proteases leukocyte elastase and cathepsin G are
synthesized as inactive precursors, but become activated by removal of an amino-terminal
dipeptide and are stored in granules. Moreover, the pro forms of elastase and cathepsin G
show carboxyl-terminal prodomains of 20 and 11 amino acids, respectively, which are not
present in the mature enzymes. To investigate mechanisms for processing, activation, and
granular targeting, we have utilized transgenic expression of myeloid serine proteases in the …
synthesized as inactive precursors, but become activated by removal of an amino-terminal
dipeptide and are stored in granules. Moreover, the pro forms of elastase and cathepsin G
show carboxyl-terminal prodomains of 20 and 11 amino acids, respectively, which are not
present in the mature enzymes. To investigate mechanisms for processing, activation, and
granular targeting, we have utilized transgenic expression of myeloid serine proteases in the …