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Cathepsin C (cathepsin + c)
Selected AbstractsArginine-based structures are specific inhibitors of cathepsin CFEBS JOURNAL, Issue 11 2000Application of peptide combinatorial libraries Novel synthetic peptide inhibitors of lysosomal cysteine proteinase cathepsin C have been designed through the use of soluble peptide combinatorial libraries. The uncovered structural inhibitory module consists of the N-terminal cluster of l -arginine residues. Its modification with d -amino acids or arginine derivatives did not increase the inhibition strength. Inhibitory potency of oligoarginines improves with the elongation of peptide chain reaching a maximum for octa- l -arginine. The oligoarginines specifically interact with the cathepsin C active site as shown by competitive-type inhibition kinetics (Ki , 10,5 m) and intrinsic fluorescence measurements. The inhibitory interaction of oligoarginines is established through the specific spatial contact of a net of guanidino groups in the arginine side-chains, as indicated by comparison with inhibitory action of low molecular mass guanidine derivatives (Ki , 10,3 m). Nonarginine polyionic compounds cannot mimic the inhibitory effect of oligoarginines. The arginine-based peptide inhibitors were selective towards cathepsin C among other cysteine proteinases tested. [source] New syndrome of hypotrichosis, striate palmoplantar keratoderma, acro-osteolysis and periodontitis not due to mutations in cathepsin CBRITISH JOURNAL OF DERMATOLOGY, Issue 3 2002M.A.M. Van Steensel Summary We report a mother and daughter with a syndrome of hypotrichosis, striate palmoplantar keratoderma, onychogryphosis, periodontitis, acro-osteolysis and psoriasis-like skin lesions. The syndrome resembles Papillon,Lefèvre syndrome (PLS), characterized by palmoplantar keratoderma, periodontitis and psoriasis-like skin lesions, and particularly Haim,Munk syndrome, an allelic variant of PLS with acro-osteolysis. Both are caused by mutations in the cathepsin C gene (CTSC). Our patients differ in the unique nature of the palmar keratoderma and hypotrichosis. We have sequenced CTSC in the mother without finding mutations in either coding or non-coding parts of the gene. We propose that our patients suffer from a new syndrome possibly caused by mutations in a gene that has a functional or structural relation with CTSC. [source] Identification of the human salivary cystatin complex by the coupling of high-performance liquid chromatography and ion-trap mass spectrometryPROTEINS: STRUCTURE, FUNCTION AND BIOINFORMATICS, Issue 4 2003Alessandro Lupi Abstract Human salivary cystatins, five major (S, S1, S2, SA, SN) and two minor (C and D), are multifunctional proteins playing a different role in the oral environment. Salivary cystatin SN is able to effectively inhibit lysosomal cathepsins B, C, H and L and cystatin SA inhibits cathepsins C and L in vitro. These activities suggest, particularly for cystatin SN, an important role in the control of proteolytic events in vivo. Differently, cystatins S are involved, together with statherin, in the mineral balance of the tooth. Due to their distinct role, a reliable method for identification and quantification of the different cystatins, as well as of possible truncated and derived forms, could be helpful for the assessment of the status of the oral cavity. To this purpose high-performance liquid chromatography electrospray ionization mass spectrometry (HPLC-ESI MS) was applied to the analysis of human saliva obtained from healthy subjects. All known salivary cystatins, with the exception of cystatin C, were detected. Strong evidence was also obtained for the presence in saliva of post-translational modified isoforms of cystatins, which may be related to donor habits. Cystatin SN and cystatins S, S1 and S2 were well separated by HPLC-ESI MS coupling from other components and thus this approach can be successfully applied to their quantification. [source] | ||||||||||