cathepsin c造句

• Jones'dissertation research involved the catalytic properties of cathepsin C, a type of protease.
• The translated prepro-cathepsin C is processed into the mature form by at least four cleavages of the polypeptide chain.
• Once activated by cathepsin C, the proteases are capable of degrading various extracellular matrix components, which can lead to tissue damage and chronic inflammation.
• The cDNAs encoding rat, human, murine, bovine, dog and two " Schistosome " cathepsin Cs have been cloned and sequenced and show that the enzyme is highly conserved.
• Unlike the other members of the papain family, mature cathepsin C consists of four subunits, each composed of the N-terminal proregion fragment, the heavy chain and the light chain.
• Cathepsin C functions as a key enzyme in the activation of granule serine peptidases in inflammatory cells, such as elastase and cathepsin G in neutrophils cells and chymase and tryptase in mast cells.
• The signal peptide is removed during translocation or secretion of the pro-enzyme ( pro-cathepsin C ) and a large N-terminal proregion fragment ( also known as the exclusion domain ), which is retained in the mature enzyme, is separated from the catalytic domain by excision of a minor C-terminal part of the pro-region, called the activation peptide.
• Members of Fruton's lab studied cathepsin C and several other peptidases, as well as proteinases that catalyzed Mary Ellen Jones, Melvin Fried, Hannelore W黵z, Peter Heinrich, Karen Nilsson, Bob Metrione, Yoshihiro Okuda, George Taborsky, Christine Zioudrou, Maxine Singer, Louis Cohen, Frederick Newth, John Thanassi, Charles Drey, Derek George Smyth, Atsuo Nagamatsu, and Milton Winitz.
• The human and rat cathepsin C cDNAs encode precursors ( prepro-cathepsin C ) comprising signal peptides of 24 residues, pro-regions of 205 ( rat cathepsin C ) or 206 ( human cathepsin C ) residues and catalytic domains of 233 residues which contain the catalytic residues and are 30-40 % identical to the mature amino acid sequences of papain and a number of other cathepsins including cathepsins, S.
• The human and rat cathepsin C cDNAs encode precursors ( prepro-cathepsin C ) comprising signal peptides of 24 residues, pro-regions of 205 ( rat cathepsin C ) or 206 ( human cathepsin C ) residues and catalytic domains of 233 residues which contain the catalytic residues and are 30-40 % identical to the mature amino acid sequences of papain and a number of other cathepsins including cathepsins, S.
• The human and rat cathepsin C cDNAs encode precursors ( prepro-cathepsin C ) comprising signal peptides of 24 residues, pro-regions of 205 ( rat cathepsin C ) or 206 ( human cathepsin C ) residues and catalytic domains of 233 residues which contain the catalytic residues and are 30-40 % identical to the mature amino acid sequences of papain and a number of other cathepsins including cathepsins, S.
• The human and rat cathepsin C cDNAs encode precursors ( prepro-cathepsin C ) comprising signal peptides of 24 residues, pro-regions of 205 ( rat cathepsin C ) or 206 ( human cathepsin C ) residues and catalytic domains of 233 residues which contain the catalytic residues and are 30-40 % identical to the mature amino acid sequences of papain and a number of other cathepsins including cathepsins, S.
• 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.