Newly synthesised metalloproteinases are available in the form of inactive zymogens
(pro-MMPs) that include specific pro-peptide, called also pro-domain, in their structure.
Another protective mechanism to prevent the premature activation of trypsinogen to trypsin inside the pancreatic duct is rapidly sweeping out zymogens
from the pancreas.
Cathepsin B can activate trypsinogen and trypsin can active the other zymogens
known as Colocalization hypothesis.
IA is a common precursor for gastricsin and human pepsin, and (b) Zymogen
IA consists of two zymogens
, pepsinogen and a zymogen
for gastric sin.
Pepsinogens are the zymogens
of pepsins, the major gastric acid peptidases involved in food protein digestion under acidic conditions.
PCD promoting signals have been suggested to induce inactive zymogens
to active proteases, and trigger irreversible proteolysis cascade leading to cell death (Stephenson & Rubinstein, 1998).
The activity levels of each of the 4 vitamin K-dependent zymogens
(II, VII, IX, and X) decreased as the INR level increased.
In the family, Caspase-3 in its inactive zymogens
, pro-caspase-3 is a remarkable protein as the enzyme shows a large substrate diversity, as a variety of proteins have been cleaved in cell maintenance.
Comparison of the primary structures of acidic proteases and their zymogens
Thrombin, factors Xa and VIIa, in addition to their roles in activating coagulation protein zymogens
, can interact with specific cell receptors and activate intracellular signaling pathways that mediate inflammatory responses.
MMPs are synthesized as enzymatically inactive zymogens
(pro-MMPs) and are activated by the "cysteine switch," which disrupts the interaction between a cysteine in the pro-domain and the Zinc ion in the active site .
Apoptosis is usually executed by caspases, a family of highly conserved aspartate-specific cysteine proteases which are constitutively expressed as zymogens
(Li and Yuan 2008).
In addition, because MMPs are regulated at the protein level by the proteolytic cleavage of the prodomain for activation and by the endogenous tissue inhibitors of metalloproteinases, the act of homogenization may have artificially brought MMP zymogens
in contact with activating enzymes or inhibitors, thus producing a false gelatinase signature in the homogenates (Galis et al.
Type 1 and type 2 KLK8 mRNA variants (KLK8-T1 and KLK8-T2) produce 2 zymogens
that differ only in their propeptide sequences.
This is in bold contrast to deoxyribonucleic acid and protein concentrations, which show that when zymogens
have damaged the acinar tissue, the protein synthesis has greatly decreased.