Gene/Protein Disease Symptom Drug Enzyme Compound
Pivot Concepts:   Target Concepts:
Query: EC:3.4.23.5 (cathepsin D)
 4,130 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Paracetamol overdose (300 mg kg(-1)) in mice resulted in a time-dependent increase in the liver weight; no change was seen for the kidney. The total acid phosphatase activities in the two tissues increased significantly 0.5 h after paracetamol overdose and remained elevated up to 3 h. Free as well as total cathepsin D activities increased significantly in both the tissues within 2-2.5 h of paracetamol treatment. Simultaneously tyrosine positive materials in the two tissues increased. RNAse II and DNAse II activities were low in liver and kidneys of the controls. Paracetamol treatment elevated both free and total RNAse II activity in the two tissues by 0.5 h. Maximum activity of DNAse II (free and total) was seen at 2.5 h after paracetamol administration. The results suggest that concerted action of cathepsin D, RNAse II and DNAse II may be responsible for paracetamol-induced hepatotoxicity and nephrotoxicity.
 ...
PMID:Is activation of lysosomal enzymes responsible for paracetamol-induced hepatotoxicity and nephrotoxicity? 879 98

Parasin I is a potent 19-residue antimicrobial peptide isolated from the skin mucus of wounded catfish (Parasilurus asotus). Here we describe the mechanism of parasin I production from histone H2A in catfish skin mucosa on epidermal injury. Cathepsin D is found to exist in the mucus as an inactive proenzyme (procathepsin D), and a metalloprotease, induced on injury, cleaves procathepsin D to generate active cathepsin D. This activated form of cathepsin D then cleaves the Ser19-Arg20 bond of histone H2A to produce parasin I. Immunohistochemical analysis reveals that unacetylated histone H2A, a precursor of parasin I, and procathepsin D are present in the cytoplasm of epithelial mucous cells and that parasin I is produced on the mucosal surface on epidermal injury. Western blot analysis shows that parasin I is also present in the skin mucus of other fish species. Furthermore, parasin I shows good antimicrobial activity against fish-specific bacterial pathogens. Taken together, these results indicate that cathepsin D and a metalloprotease participate in the production of parasin I from histone H2A and that parasin I contributes to the innate host defense of the fish against invading microorganisms.
 ...
PMID:Cathepsin D produces antimicrobial peptide parasin I from histone H2A in the skin mucosa of fish. 1182 Dec 59