3.4.14.1	additional information	-	
3.4.14.1	additional information	the enzyme is involved in the processing of murine mast cell prochymase and procathepsin G, but does not process mast cell pro-carboxypeptidase A or protryptase	
3.4.14.1	additional information	,n high affinity interaction between heparin and prochymase allows the 2 residue propeptide to be cleaved by dipeptidylpeptidase I	
3.4.14.1	additional information	enzyme is involved in intracellular degradation of proteins	
3.4.14.1	additional information	the enzyme is involved in lysosomal protein degradation	
3.4.14.1	additional information	the enzyme may be involved in mediating cell-cell intercommunication in Dictyostelium and in controlling cell movement during morphogenesis	
3.4.14.1	additional information	together with other proteases the enzyme plays a major part in degradation of ingested substances after endocytosis and in tissue damage following enzyme release	
3.4.14.1	additional information	the enzyme plays a requisite role in the post-translational processing and activation of members of the family of granule serine proteases expressed in bone marrow-derived effector cells	
3.4.14.1	additional information	cathepsin C gene is a direct target for induction by interferon regulatory factor-8	
3.4.14.1	additional information	cathepsin C is required for granzyme B activation in unstimulated human natural killer cells. However in vitro activation of Papillon-Lefevre syndrome natural killer cells with interleukin-2 restores cytolytic function and granzyme B activity by a cathepsin C-independent mechanism	
3.4.14.1	additional information	dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradation, the enzyme is important for asexual proliferation	
3.4.14.1	additional information	DPPI activates granule-associated serine proteases, several of which play important roles in host responses to bacterial infection. DPPI is a key regulator of survival from septic peritonitis	
3.4.14.1	additional information	loss of DPPI activity in patients with Papillon-Lefevre syndrome is associated with severe reduction in the activity and stability of neutrophil-derived serine proteases	
3.4.14.1	additional information	mutation in the cathepsin C gene are not the cause of all early-onset periodontal disease, and currently there is no evidence for the existence of a class of patients who do not have the full Papillon-Lefevre syndrome disease phenotype, but suffer isolated aggressive periodontitis because they have a low-activity cathepsin C gene variant	
3.4.14.1	additional information	Papillon-Lefèvre syndrome is a rare autosomal recessive disease that involves severe periodontitis and hyperkeratosis of the hand palms and foot soles. Gene analysis of the CTSC gene in two families with Papillon-Lefèvre syndrome demonstrates that in the patients with Papillon-Lefèvre syndrome the absence of cathepsin C activity coincides with absence of activity of the serine proteinases elastase, cathepsin G and proteinase 3	
3.4.14.1	additional information	the enzyme is involved in the final stages of oocyte maturation in crustacean species	
3.4.14.1	additional information	the enzyme may play a role in converting the endogenous beta-MSH(5-22) to more potent peptides that regulate energy homeostasis in the hypothalamus	
3.4.14.1	additional information	cathepsin C has a broad substrate specificity being able to hydrolyse out nearly every possible dipeptide unit, with the exception of those containing basic amino acids (Arg or Lys) at N-terminal position or Pro on either side of the scissile bond	
3.4.14.1	additional information	cathepsin C may stimulate the sorting to the lysosome, at least in part, contributing to the degradation of intestinal alkaline phosphatase in Caco-2 cells, the propeptide of cathepsin C interacts with heat shock cognate protein 70 which is required for a step in chaperone-mediated lysosomal protein degradation	
3.4.14.1	additional information	DPPI and neutrophils play a critical role in Sendai virus-induced asthma phenotype as a result of a DPPI-dependent neutrophil recruitment and cytokine response