Loading...
  • structure
  • Cathepsin C catalyses excision of dipeptides from the N-terminus of protein and peptide substrates, except if (i) the amino group of the N-terminus is blocked, (ii) the site of cleavage is on either side of a proline residue, (iii) the N-terminal residue is lysine or arginine, or (iv) the structure of the peptide or protein prevents further digestion from the N-terminus. (wikipedia.org)
  • responsible
  • It is reported in another study that cathepsin Z may be responsible for dopamine neuron death and thus involved in the pathogenic cascade event. (wikipedia.org)
  • unique
  • Cathepsin Z is characterized by an unusual and unique 3-amino acid insertion in the highly conserved region between the glutamine of the putative oxynion hole and the active site cysteine. (wikipedia.org)
  • protein
  • When the researchers combined the two cathepsins and allowed them to attack samples of elastin, they expected to see increased degradation of the protein. (innovations-report.com)
  • Barry's modeling suggested that effects observed could occur if cathepsin S were degrading cathepsin K instead of attacking the elastin - a protein essential in arteries and the cardiovascular system. (innovations-report.com)
  • Cathepsin B seems to cause amyloid plaque, the root of Alzheimer's symptoms, when there are wild-type beta-secretase present in the system Overexpression of the encoded protein, which is a member of the peptidase C1 family, has been associated with esophageal adenocarcinoma and other tumors. (wikipedia.org)
  • Osteoclasts are the bone resorbing cells of the body, and they secrete cathepsin K in order to break down collagen, the major component of the non-mineral protein matrix of the bone. (wikipedia.org)
  • Transport of human lysosomal neuraminidase to mature lysosomes requires protective protein/cathepsin A". EMBO J. ENGLAND. (wikipedia.org)
  • The major ras induced protein in NIH3T3 cells is cathepsin L". Nucleic Acids Res. (wikipedia.org)
  • Cathepsin G is a 255-amino-acid-residue protein including an 18-residue signal peptide, a two-residue activation peptide at the N-terminus and a carboxy terminal extension. (wikipedia.org)
  • A deficiency in the levels of Cathepsin E in the body may play a part in inflammatory skin diseases such as atopic dermatitis, for which treatment would rely on fixing functionality and levels of the protein in the body. (wikipedia.org)
  • Cathepsin E plays a vital role in protein degradation, antigen processing via the MHC class II pathway and bioactive protein generation. (wikipedia.org)
  • precursor
  • Schestkowa O, Geisel D, Jacob R, Hasilik A. The catalytically inactive precursor of cathepsin D induces apoptosis in human fibroblasts and HeLa cells. (ebi.ac.uk)
  • The very long (251-amino acid residues) proregion of the cathepsin F precursor contains a C-terminal domain similar to the pro-segment of cathepsin L-like enzymes, a 50-residue flexible linker peptide, and an N-terminal domain predicted to adopt a cystatin-like fold. (wikipedia.org)
  • mature cathepsin
  • The ultimate form of mature cathepsin D is composed of 337 amino acid residues, 196 amino acid residues in the heavy chain and 141 in the light chain. (wikipedia.org)
  • Mature cathepsin B is composed of a heavy chain of 25-26 kDa and a light chain of 5kDa, which are linked by a dimer of disulfide. (wikipedia.org)
  • secrete cathepsin
  • Immune cells, including macrophages and microglia, secrete cathepsin S in response to inflammatory mediators including lipopolysaccharides, proinflammatory cytokines and neutrophils. (wikipedia.org)
  • degrade
  • The main function of cathepsin D is to degrade proteins and activate precursors of bioactive proteins in pre-lysosomal compartments. (wikipedia.org)
  • Researchers for the first time have shown that members of a family of enzymes known as cathepsins - which are implicated in many disease processes - may attack one another instead of the bodily proteins they normally degrade. (innovations-report.com)
  • The gel is then put into an activation buffer of a specific pH and left to incubate overnight at 37 °C. This activation step allows the cathepsins to degrade the gelatin substrate. (wikipedia.org)
  • induces
  • Cathepsin D enzymatic activity induces hydrolytic modification of apolipoprotein B-100-containing lipoproteins, including LDL, which means it may be involved in atherosclerosis as well. (wikipedia.org)
  • Cathepsin D deficiency induces lysosomal storage with ceroid lipofuscin in mouse CNS neurons. (ebi.ac.uk)
  • Microinjection of cathepsin d induces caspase-dependent apoptosis in fibroblasts. (ebi.ac.uk)
  • degradation
  • Using a combination of modeling and experiments, researchers from the Georgia Institute of Technology and Emory University have shown that one type of cathepsin preferentially attacks another, reducing the enzyme's degradation of collagen. (innovations-report.com)
  • That theoretical result led to additional experiments in which the researchers measured a direct correlation between an increase in the amount of cathepsin S added to the experiment and a reduction in the degradation of collagen. (innovations-report.com)
  • Cathepsins B and L are involved in matrix degradation and cell invasion. (wikipedia.org)
  • Cathepsin S participates in the degradation of the invariant or Ii chain that prevents loading the antigen into the complex. (wikipedia.org)
  • Contrary, inhibition of cathepsin S will lead to a delay in degradation of Ii and loading the antigen into MHC II as well as inappropriate presence of uncleaved Li-fragments in MHC II on the cell surface. (wikipedia.org)
  • cystatin
  • Cystatin A and B have a lower activity compared to cystatin C. The active cleavage sites -(-Val-Val-Arg-)- of cathepsin S are supposed to have at least two amino acids surrounding it from each side. (wikipedia.org)
  • residues
  • The catalytic sites of cathepsin D include two critical aspartic residues ( amino acid 33 and 231) located on the 14 kDa and 34kDa chains. (wikipedia.org)
  • A distinguishing factor of Cathepsin E in comparison with the structure of Cathepsin D and BACE1 can be seen at the formation of an extra hydrogen bond between the Asp 96 and Ser 99 residues, and absence of a hydrogen bond with Leu/Met at Asp 281. (wikipedia.org)
  • aspartic
  • This entry includes the peptidase domain of uncharacterized aspartic endopeptidases from animals with similarities to cathepsin D. (ebi.ac.uk)
  • Cathepsin D ( EC:3.4.23.5 and MEROPS identifier A01.009) is an aspartic endopeptidase located in the lysosome of animal cells. (ebi.ac.uk)
  • Molecular
  • We saw that the cathepsin K was going away much faster when there was cathepsin S present than when it was by itself," said Platt, who is also a Georgia Cancer Coalition Distinguished Scholar and a Fellow of the Keystone Symposia on Molecular and Cellular Biology. (innovations-report.com)
  • It is based on SDS-PAGE whereby samples tested for cathepsin activity are loaded into a polyacrylamide gel and then separated by molecular weight. (wikipedia.org)
  • These bands are then correlated to their respective molecular weights in order to identify which cathepsins were active in the sample. (wikipedia.org)