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  1. Article: Ultrasensitive internally quenched substrates of human cathepsin L

    Łęgowska, Monika / Adam Lesner / Krzysztof Rolka / Magdalena Wysocka / Michał Pikuła / Timo Burster

    Analytical biochemistry. 2014 Dec. 01, v. 466

    2014  

    Abstract: Internally quenched cathepsin L (Cat L) substrate ABZ-Bip-Arg-Ala-Gln-Tyr(3-NO2)-NH2 with high specificity constant (kcat/KM=2.6×107M−1s−1) was synthesized. The resultant compound displayed high selectivity over other members of the cathepsin family (B, ... ...

    Abstract Internally quenched cathepsin L (Cat L) substrate ABZ-Bip-Arg-Ala-Gln-Tyr(3-NO2)-NH2 with high specificity constant (kcat/KM=2.6×107M−1s−1) was synthesized. The resultant compound displayed high selectivity over other members of the cathepsin family (B, S, X, V, C, K, H, F, D, and A). Activity of Cat L at picomolar (pM) concentrations was found using this substrate. Moreover, it was established that the presence of the selective Cat L inhibitor suppressed the proteolysis of the substrate to a non-detectable level. Incubation of the synthesized compound with a cell lysate of healthy and cancer cell lines indicated significant differences in Cat L activity. Based on the obtained results, it is proposed that this substrate could be used for selective monitoring of Cat L activity in biological systems.
    Keywords cathepsin L ; cell lines ; humans ; monitoring ; neoplasm cells ; proteolysis
    Language English
    Dates of publication 2014-1201
    Size p. 30-37.
    Publishing place Elsevier Inc.
    Document type Article
    ZDB-ID 1110-1
    ISSN 1096-0309 ; 0003-2697
    ISSN (online) 1096-0309
    ISSN 0003-2697
    DOI 10.1016/j.ab.2014.08.010
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  2. Article ; Online: Pegylated fluorescent peptides as substrates of proteolytic enzymes.

    Wysocka, Magdalena / Lesner, Adam / Popow, Jadwiga / Łegowska, Monika / Rolka, Krzysztof

    Protein and peptide letters

    2012  Volume 19, Issue 12, Page(s) 1237–1244

    Abstract: In this work the efficient and simple method of improvement specificity and solubility of low molecular weight proteinase substrates is described. The series of fluorescent substrates of selected proteolytic enzymes (neutrophil elastase, cathepsin G and ... ...

    Abstract In this work the efficient and simple method of improvement specificity and solubility of low molecular weight proteinase substrates is described. The series of fluorescent substrates of selected proteolytic enzymes (neutrophil elastase, cathepsin G and proteinase 3 along with human airway trypsin like protease) were synthesized and modified by selective pegylation by the attachment of 2-(2-(2-aminoethoxy)ethoxy)acetic acid. Modification of the C-terminal carboxyl group resulted in the decrease in the specificity constants (k(cat)/K(M)) for all obtained analogues. The covalent attachment of PEG to N-terminal amino group has the opposite effect, as the increase in specificity constant was observed for all studied compounds. This outcome was pronounced the most for proteinase 3 substrate PEG-ABZ-Tyr-Tyr-Abu-ANB-NH2, whose catalytic constant (k(cat)) increased over three fold. The introduction of PEG moieties at both C- and N-terminal yielded the substrates with lower specificity constants. For substrate (ABZ-Arg-Gln-Asp-Arg-ANB-NH2) the influence of the PEG chain length on its kinetic parameters was investigated. Elongation of the PEG chain at N-terminal of this peptide decreased the specificity constant. In addition to the effect of pegylation on the kinetic parameters of the studied substrates, the introduced modifications significantly improved their solubility in buffer solutions applied for enzymatic investigations.
    MeSH term(s) 4-Aminobenzoic Acid/chemistry ; Chromogenic Compounds/analysis ; Chromogenic Compounds/chemistry ; Chromogenic Compounds/metabolism ; Fluorescent Dyes/analysis ; Fluorescent Dyes/chemistry ; Fluorescent Dyes/metabolism ; Humans ; Nitrobenzoates/chemistry ; Oligopeptides/chemistry ; Oligopeptides/metabolism ; Polyethylene Glycols/chemistry ; Serine Endopeptidases/metabolism ; Solubility ; Spectrophotometry, Ultraviolet
    Chemical Substances Chromogenic Compounds ; Fluorescent Dyes ; Nitrobenzoates ; Oligopeptides ; 5-amino-2-nitrobenzoic acid (13280-60-9) ; Polyethylene Glycols (3WJQ0SDW1A) ; Serine Endopeptidases (EC 3.4.21.-) ; 4-Aminobenzoic Acid (TL2TJE8QTX)
    Language English
    Publishing date 2012-04-28
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1280776-x
    ISSN 1875-5305 ; 0929-8665
    ISSN (online) 1875-5305
    ISSN 0929-8665
    DOI 10.2174/092986612803521684
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 4452: Show issues Location:
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  3. Article ; Online: Ultrasensitive internally quenched substrates of human cathepsin L.

    Lęgowska, Monika / Wysocka, Magdalena / Burster, Timo / Pikuła, Michał / Rolka, Krzysztof / Lesner, Adam

    Analytical biochemistry

    2014  Volume 466, Page(s) 30–37

    Abstract: Internally quenched cathepsin L (Cat L) substrate ABZ-Bip-Arg-Ala-Gln-Tyr(3-NO2)-NH2 with high specificity constant (kcat/KM=2.6×10(7)M(-1)s(-1)) was synthesized. The resultant compound displayed high selectivity over other members of the cathepsin ... ...

    Abstract Internally quenched cathepsin L (Cat L) substrate ABZ-Bip-Arg-Ala-Gln-Tyr(3-NO2)-NH2 with high specificity constant (kcat/KM=2.6×10(7)M(-1)s(-1)) was synthesized. The resultant compound displayed high selectivity over other members of the cathepsin family (B, S, X, V, C, K, H, F, D, and A). Activity of Cat L at picomolar (pM) concentrations was found using this substrate. Moreover, it was established that the presence of the selective Cat L inhibitor suppressed the proteolysis of the substrate to a non-detectable level. Incubation of the synthesized compound with a cell lysate of healthy and cancer cell lines indicated significant differences in Cat L activity. Based on the obtained results, it is proposed that this substrate could be used for selective monitoring of Cat L activity in biological systems.
    MeSH term(s) Biological Assay ; Cathepsin L/metabolism ; Cathepsins/metabolism ; Cell Line ; Cell Line, Tumor ; Humans ; Hydrogen-Ion Concentration ; Limit of Detection ; Peptides/chemical synthesis ; Peptides/chemistry ; Peptides/metabolism ; Substrate Specificity ; Tyrosine/analogs & derivatives ; Tyrosine/metabolism ; ortho-Aminobenzoates/metabolism
    Chemical Substances Peptides ; ortho-Aminobenzoates ; 3-nitrotyrosine (3604-79-3) ; Tyrosine (42HK56048U) ; Cathepsins (EC 3.4.-) ; Cathepsin L (EC 3.4.22.15)
    Language English
    Publishing date 2014-12-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1110-1
    ISSN 1096-0309 ; 0003-2697
    ISSN (online) 1096-0309
    ISSN 0003-2697
    DOI 10.1016/j.ab.2014.08.010
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    In stock of ZB MED Cologne/Königswinter

    Zs.A 389: Show issues Location:
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  4. Article ; Online: Development of the first internally-quenched fluorescent substrates of human cathepsin C: The application in the enzyme detection in biological samples.

    Łęgowska, Monika / Hamon, Yveline / Wojtysiak, Anna / Grzywa, Renata / Sieńczyk, Marcin / Burster, Timo / Korkmaz, Brice / Lesner, Adam

    Archives of biochemistry and biophysics

    2016  Volume 612, Page(s) 91–102

    Abstract: Cathepsin C is a widely expressed cysteine exopeptidase that is mostly recognized for the activation of the granule-associated proinflammatory serine proteases in neutrophils, cytotoxic T lymphocytes and mast cells. It has been shown that the enzyme can ... ...

    Abstract Cathepsin C is a widely expressed cysteine exopeptidase that is mostly recognized for the activation of the granule-associated proinflammatory serine proteases in neutrophils, cytotoxic T lymphocytes and mast cells. It has been shown that the enzyme can be secreted extracellularly; however, its occurrence in human bodily fluids/physiological samples has not been thoroughly studied. In the course of this study, the first fluorescence resonance energy transfer peptides for the measurement of the activity of human cathepsin C were designed and synthesized. Two series of tetra- and pentapeptide substrates enabled the detailed S' specificity study of cathepsin C, which has been examined for the first time. The extensive enzymatic studies of the obtained compounds resulted in the selection of the highly specific and selective substrate Thi-Ala(Mca)-Ser-Gly-Tyr(3-NO
    MeSH term(s) Catalytic Domain ; Cathepsin C/chemistry ; Cathepsin L/chemistry ; Fluorescence Resonance Energy Transfer ; Humans ; Hydrogen-Ion Concentration ; Inflammation ; Kinetics ; Mast Cells/cytology ; Microscopy, Fluorescence/methods ; Molecular Conformation ; Molecular Docking Simulation ; Neutrophils/metabolism ; Peptides/chemistry ; Protein Binding ; Recombinant Proteins/chemistry ; Substrate Specificity ; T-Lymphocytes, Cytotoxic/cytology
    Chemical Substances Peptides ; Recombinant Proteins ; Cathepsin C (EC 3.4.14.1) ; Cathepsin L (EC 3.4.22.15)
    Language English
    Publishing date 2016-12-15
    Publishing country United States
    Document type Journal Article
    ZDB-ID 523-x
    ISSN 1096-0384 ; 0003-9861
    ISSN (online) 1096-0384
    ISSN 0003-9861
    DOI 10.1016/j.abb.2016.10.007
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    Uc I Zs.237: Show issues Location:
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  5. Article ; Online: Exploiting the S4-S5 Specificity of Human Neutrophil Proteinase 3 to Improve the Potency of Peptidyl Di(chlorophenyl)-phosphonate Ester Inhibitors: A Kinetic and Molecular Modeling Analysis.

    Guarino, Carla / Gruba, Natalia / Grzywa, Renata / Dyguda-Kazimierowicz, Edyta / Hamon, Yveline / Łȩgowska, Monika / Skoreński, Marcin / Dallet-Choisy, Sandrine / Marchand-Adam, Sylvain / Kellenberger, Christine / Jenne, Dieter E / Sieńczyk, Marcin / Lesner, Adam / Gauthier, Francis / Korkmaz, Brice

    Journal of medicinal chemistry

    2018  Volume 61, Issue 5, Page(s) 1858–1870

    Abstract: The neutrophilic serine protease proteinase 3 (PR3) is involved in inflammation and immune response and thus appears as a therapeutic target for a variety of infectious and inflammatory diseases. Here we combined kinetic and molecular docking studies to ... ...

    Abstract The neutrophilic serine protease proteinase 3 (PR3) is involved in inflammation and immune response and thus appears as a therapeutic target for a variety of infectious and inflammatory diseases. Here we combined kinetic and molecular docking studies to increase the potency of peptidyl-diphenyl phosphonate PR3 inhibitors. Occupancy of the S1 subsite of PR3 by a nVal residue and of the S4-S5 subsites by a biotinylated Val residue as obtained in biotin-VYDnV
    MeSH term(s) Animals ; Binding Sites ; Humans ; Inflammation ; Kinetics ; Macaca ; Models, Molecular ; Molecular Docking Simulation ; Myeloblastin/chemistry ; Organophosphonates/antagonists & inhibitors ; Protein Binding ; Rodentia ; Substrate Specificity
    Chemical Substances Organophosphonates ; Myeloblastin (EC 3.4.21.76)
    Language English
    Publishing date 2018-02-26
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 218133-2
    ISSN 1520-4804 ; 0022-2623
    ISSN (online) 1520-4804
    ISSN 0022-2623
    DOI 10.1021/acs.jmedchem.7b01416
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    Zs.B 151: Show issues Location:
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  6. Article ; Online: Therapeutic targeting of cathepsin C: from pathophysiology to treatment.

    Korkmaz, Brice / Caughey, George H / Chapple, Iain / Gauthier, Francis / Hirschfeld, Josefine / Jenne, Dieter E / Kettritz, Ralph / Lalmanach, Gilles / Lamort, Anne-Sophie / Lauritzen, Conni / Łȩgowska, Monika / Lesner, Adam / Marchand-Adam, Sylvain / McKaig, Sarah J / Moss, Celia / Pedersen, John / Roberts, Helen / Schreiber, Adrian / Seren, Seda /
    Thakker, Nalin S

    Pharmacology & therapeutics

    2018  Volume 190, Page(s) 202–236

    Abstract: Cathepsin C (CatC) is a highly conserved tetrameric lysosomal cysteine dipeptidyl aminopeptidase. The best characterized physiological function of CatC is the activation of pro-inflammatory granule-associated serine proteases. These proteases are ... ...

    Abstract Cathepsin C (CatC) is a highly conserved tetrameric lysosomal cysteine dipeptidyl aminopeptidase. The best characterized physiological function of CatC is the activation of pro-inflammatory granule-associated serine proteases. These proteases are synthesized as inactive zymogens containing an N-terminal pro-dipeptide, which maintains the zymogen in its inactive conformation and prevents premature activation, which is potentially toxic to the cell. The activation of serine protease zymogens occurs through cleavage of the N-terminal dipeptide by CatC during cell maturation in the bone marrow. In vivo data suggest that pharmacological inhibition of pro-inflammatory serine proteases would suppress or attenuate deleterious effects mediated by these proteases in inflammatory/auto-immune disorders. The pathological deficiency in CatC is associated with Papillon-Lefèvre syndrome (PLS). The patients however do not present marked immunodeficiency despite the absence of active serine proteases in immune defense cells. Hence, the transitory pharmacological blockade of CatC activity in the precursor cells of the bone marrow may represent an attractive therapeutic strategy to regulate activity of serine proteases in inflammatory and immunologic conditions. A variety of CatC inhibitors have been developed both by pharmaceutical companies and academic investigators, some of which are currently being employed and evaluated in preclinical/clinical trials.
    MeSH term(s) Animals ; Autoimmune Diseases/drug therapy ; Autoimmune Diseases/physiopathology ; Cathepsin C/antagonists & inhibitors ; Cathepsin C/metabolism ; Drug Development/methods ; Humans ; Inflammation/drug therapy ; Inflammation/physiopathology ; Papillon-Lefevre Disease/drug therapy ; Papillon-Lefevre Disease/physiopathology ; Serine Proteases/metabolism
    Chemical Substances Serine Proteases (EC 3.4.-) ; Cathepsin C (EC 3.4.14.1)
    Language English
    Publishing date 2018-05-26
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 194735-7
    ISSN 1879-016X ; 0163-7258
    ISSN (online) 1879-016X
    ISSN 0163-7258
    DOI 10.1016/j.pharmthera.2018.05.011
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    Zs.A 1183: Show issues Location:
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  7. Article ; Online: Neutrophilic Cathepsin C Is Maturated by a Multistep Proteolytic Process and Secreted by Activated Cells during Inflammatory Lung Diseases.

    Hamon, Yveline / Legowska, Monika / Hervé, Virginie / Dallet-Choisy, Sandrine / Marchand-Adam, Sylvain / Vanderlynden, Lise / Demonte, Michèle / Williams, Rich / Scott, Christopher J / Si-Tahar, Mustapha / Heuzé-Vourc'h, Nathalie / Lalmanach, Gilles / Jenne, Dieter E / Lesner, Adam / Gauthier, Francis / Korkmaz, Brice

    The Journal of biological chemistry

    2016  Volume 291, Issue 16, Page(s) 8486–8499

    Abstract: The cysteine protease cathepsin C (CatC) activates granule-associated proinflammatory serine proteases in hematopoietic precursor cells. Its early inhibition in the bone marrow is regarded as a new therapeutic strategy for treating proteolysis-driven ... ...

    Abstract The cysteine protease cathepsin C (CatC) activates granule-associated proinflammatory serine proteases in hematopoietic precursor cells. Its early inhibition in the bone marrow is regarded as a new therapeutic strategy for treating proteolysis-driven chronic inflammatory diseases, but its complete inhibition is elusive in vivo Controlling the activity of CatC may be achieved by directly inhibiting its activity with a specific inhibitor or/and by preventing its maturation. We have investigated immunochemically and kinetically the occurrence of CatC and its proform in human hematopoietic precursor cells and in differentiated mature immune cells in lung secretions. The maturation of proCatC obeys a multistep mechanism that can be entirely managed by CatS in neutrophilic precursor cells. CatS inhibition by a cell-permeable inhibitor abrogated the release of the heavy and light chains from proCatC and blocked ∼80% of CatC activity. Under these conditions the activity of neutrophil serine proteases, however, was not abolished in precursor cell cultures. In patients with neutrophilic lung inflammation, mature CatC is found in large amounts in sputa. It is secreted by activated neutrophils as confirmed through lipopolysaccharide administration in a nonhuman primate model. CatS inhibitors currently in clinical trials are expected to decrease the activity of neutrophilic CatC without affecting those of elastase-like serine proteases.
    MeSH term(s) Animals ; Cathepsin C/genetics ; Cathepsin C/metabolism ; Disease Models, Animal ; HL-60 Cells ; Humans ; Lung/enzymology ; Lung/pathology ; Macaca fascicularis ; Mice ; Mice, Inbred BALB C ; Neutrophils/enzymology ; Neutrophils/pathology ; Pneumonia/chemically induced ; Pneumonia/enzymology ; Pneumonia/pathology ; Rats, Sprague-Dawley ; Sputum/metabolism
    Chemical Substances CTSC protein, human (EC 3.4.14.1) ; Cathepsin C (EC 3.4.14.1) ; Ctsc protein, mouse (EC 3.4.14.1) ; Ctsc protein, rat (EC 3.4.14.1)
    Language English
    Publishing date 2016-02-16
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M115.707109
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    Uc I Zs.108: Show issues Location:
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  8. Article ; Online: New selective peptidyl di(chlorophenyl) phosphonate esters for visualizing and blocking neutrophil proteinase 3 in human diseases.

    Guarino, Carla / Legowska, Monika / Epinette, Christophe / Kellenberger, Christine / Dallet-Choisy, Sandrine / Sieńczyk, Marcin / Gabant, Guillaume / Cadene, Martine / Zoidakis, Jérôme / Vlahou, Antonia / Wysocka, Magdalena / Marchand-Adam, Sylvain / Jenne, Dieter E / Lesner, Adam / Gauthier, Francis / Korkmaz, Brice

    The Journal of biological chemistry

    2014  Volume 289, Issue 46, Page(s) 31777–31791

    Abstract: The function of neutrophil protease 3 (PR3) is poorly understood despite of its role in autoimmune vasculitides and its possible involvement in cell apoptosis. This makes it different from its structural homologue neutrophil elastase (HNE). Endogenous ... ...

    Abstract The function of neutrophil protease 3 (PR3) is poorly understood despite of its role in autoimmune vasculitides and its possible involvement in cell apoptosis. This makes it different from its structural homologue neutrophil elastase (HNE). Endogenous inhibitors of human neutrophil serine proteases preferentially inhibit HNE and to a lesser extent, PR3. We constructed a single-residue mutant PR3 (I217R) to investigate the S4 subsite preferences of PR3 and HNE and used the best peptide substrate sequences to develop selective phosphonate inhibitors with the structure Ac-peptidyl(P)(O-C6H4-4-Cl)2. The combination of a prolyl residue at P4 and an aspartyl residue at P2 was totally selective for PR3. We then synthesized N-terminally biotinylated peptidyl phosphonates to identify the PR3 in complex biological samples. These inhibitors resisted proteolytic degradation and rapidly inactivated PR3 in biological fluids such as inflammatory lung secretions and the urine of patients with bladder cancer. One of these inhibitors revealed intracellular PR3 in permeabilized neutrophils and on the surface of activated cells. They hardly inhibited PR3 bound to the surface of stimulated neutrophils despite their low molecular mass, suggesting that the conformation and reactivity of membrane-bound PR3 is altered. This finding is relevant for autoantibody binding and the subsequent activation of neutrophils in granulomatosis with polyangiitis (formerly Wegener disease). These are the first inhibitors that can be used as probes to monitor, detect, and control PR3 activity in a variety of inflammatory diseases.
    MeSH term(s) Animals ; Apoptosis ; Biotinylation ; Cell Line ; Cell Membrane/metabolism ; Esters/chemistry ; Gene Expression Regulation, Enzymologic/drug effects ; Humans ; Hydrolysis ; Inflammation ; Insecta ; Mass Spectrometry ; Models, Chemical ; Mutation ; Myeloblastin/antagonists & inhibitors ; Myeloblastin/chemistry ; Neutrophil Activation ; Neutrophils/drug effects ; Oligopeptides/chemistry ; Organophosphonates/chemistry ; Peptides/chemistry ; Proline/chemistry ; Protease Inhibitors/chemistry ; Solvents
    Chemical Substances Esters ; Oligopeptides ; Organophosphonates ; Peptides ; Protease Inhibitors ; Solvents ; Proline (9DLQ4CIU6V) ; Myeloblastin (EC 3.4.21.76)
    Language English
    Publishing date 2014-10-06
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M114.591339
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  9. Article ; Online: Fluorescent analogs of trypsin inhibitor SFTI-1 isolated from sunflower seeds--synthesis and applications.

    Lesner, Adam / Karna, Natalia / Psurski, Mateusz / Lęgowska, Anna / Wysocka, Magdalena / Guzow, Katarzyna / Sieradzan, Adam / Sieńczyk, Marcin / Trzonkowski, Piotr / Pikuła, Michał / Zieliński, Maciej / Kosikowska, Paulina / Łukajtis, Rałał / Łęgowska, Monika / Dębowski, Dawid / Wiczk, Wiesław / Rolka, Krzysztof

    Biopolymers

    2014  Volume 102, Issue 1, Page(s) 124–135

    Abstract: This article describes the synthesis and enzymatic study of newly synthesized analogs of trypsin inhibitors SFTI-1 that were fluorescent labeled on their N-terminal amino groups. Two fluorescent derivatives of benzoxazole (3-[2-(4-diphenylaminophenyl) ... ...

    Abstract This article describes the synthesis and enzymatic study of newly synthesized analogs of trypsin inhibitors SFTI-1 that were fluorescent labeled on their N-terminal amino groups. Two fluorescent derivatives of benzoxazole (3-[2-(4-diphenylaminophenyl)benzoxazol-5-yl]-L-alanine-[(4NPh2 )Ph]Box-Ala and 3-[2-(2',4',5'-trimethoxyphenyl)benzoxazol-5-yl]-L-alanine-[2,4,5-(OMe)3Ph]Box-Ala) were used as efficient fluorescent labels. The compounds obtained preserved their inhibitory activity and were efficient inhibitors of bovine trypsin or chymotrypsin. Nevertheless, their association inhibition constants were one or two orders of magnitude lower than those determined for unlabeled monocyclic SFTI-1 or [Phe(5)]SFTI-1, respectively. The conjugates obtained were found to be proteolytically stable in the presence of cognate enzymes. Applying such fluorescent peptides, we were able to investigate enzyme-inhibitor complex formation using fluorescent techniques. We found that such compounds were rapidly internalized by the fibroblast or cancer cells with no cytotoxic effects.
    MeSH term(s) Amino Acid Sequence ; Animals ; Benzoxazoles/chemistry ; Cattle ; Cell Line ; Cell Membrane Permeability ; Chromatography, Gel ; Chromatography, High Pressure Liquid ; Flow Cytometry ; Fluorescence ; Helianthus/chemistry ; Humans ; Microscopy, Fluorescence ; Molecular Sequence Data ; Peptides, Cyclic/chemical synthesis ; Peptides, Cyclic/chemistry ; Peptides, Cyclic/isolation & purification ; Seeds/chemistry ; Time Factors ; Trypsin Inhibitors/chemical synthesis ; Trypsin Inhibitors/chemistry ; Trypsin Inhibitors/isolation & purification
    Chemical Substances Benzoxazoles ; Peptides, Cyclic ; SFTI-1 peptide, sunflower ; Trypsin Inhibitors
    Language English
    Publishing date 2014-01
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1123-x
    ISSN 1097-0282 ; 0006-3525
    ISSN (online) 1097-0282
    ISSN 0006-3525
    DOI 10.1002/bip.22442
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  10. Article ; Online: Analysis of urinary cathepsin C for diagnosing Papillon-Lefèvre syndrome.

    Hamon, Yveline / Legowska, Monika / Fergelot, Patricia / Dallet-Choisy, Sandrine / Newell, Louise / Vanderlynden, Lise / Kord Valeshabad, Ali / Acrich, Karina / Kord, Hadi / Charalampos, Tsamakis / Morice-Picard, Fanny / Surplice, Ian / Zoidakis, Jerome / David, Karen / Vlahou, Antonia / Ragunatha, Shivanna / Nagy, Nikoletta / Farkas, Katalin / Széll, Márta /
    Goizet, Cyril / Schacher, Beate / Battino, Maurizio / Al Farraj Aldosari, Abdullah / Wang, Xinwen / Liu, Yang / Marchand-Adam, Sylvain / Lesner, Adam / Kara, Elodie / Korkmaz-Icöz, Sevil / Moss, Celia / Eickholz, Peter / Taieb, Alain / Kavukcu, Salih / Jenne, Dieter E / Gauthier, Francis / Korkmaz, Brice

    The FEBS journal

    2016  Volume 283, Issue 3, Page(s) 498–509

    Abstract: Papillon-Lefèvre syndrome (PLS) (OMIM: 245000) is a rare disease characterized by severe periodontitis and palmoplantar keratoderma. It is caused by mutations in both alleles of the cathepsin C (CatC) gene CTSC that completely abrogate the proteolytic ... ...

    Abstract Papillon-Lefèvre syndrome (PLS) (OMIM: 245000) is a rare disease characterized by severe periodontitis and palmoplantar keratoderma. It is caused by mutations in both alleles of the cathepsin C (CatC) gene CTSC that completely abrogate the proteolytic activity of this cysteine proteinase. Most often, a genetic analysis to enable early and rapid diagnosis of PLS is unaffordable or unavailable. In this study, we tested the hypothesis that active CatC is constitutively excreted and can be easily traced in the urine of normal subjects. If this is true, determining its absence in the urine of patients would be an early, simple, reliable, low-cost and easy diagnostic technique. All 75 urine samples from healthy control subjects (aged 3 months to 80 years) contained proteolytically active CatC and its proform, as revealed by kinetic analysis and immunochemical detection. Of the urine samples of 31 patients with a PLS phenotype, 29 contained neither proteolytically active CatC nor the CatC antigen, so that the PLS diagnosis was confirmed. CatC was detected in the urine of the other two patients, and genetic analysis revealed no loss-of-function mutation in CTSC, indicating that they suffer from a PLS-like condition but not from PLS. Screening for the absence of urinary CatC activity soon after birth and early treatment before the onset of PLS manifestations will help to prevent aggressive periodontitis and loss of many teeth, and should considerably improve the quality of life of PLS patients.
    MeSH term(s) Adolescent ; Adult ; Aged ; Aged, 80 and over ; Cathepsin C/genetics ; Cathepsin C/metabolism ; Cathepsin C/urine ; Child ; Child, Preschool ; Female ; Healthy Volunteers ; Humans ; Infant ; Male ; Middle Aged ; Papillon-Lefevre Disease/diagnosis ; Papillon-Lefevre Disease/urine ; Phenotype ; Young Adult
    Chemical Substances CTSC protein, human (EC 3.4.14.1) ; Cathepsin C (EC 3.4.14.1)
    Language English
    Publishing date 2016-02
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2173655-8
    ISSN 1742-4658 ; 1742-464X
    ISSN (online) 1742-4658
    ISSN 1742-464X
    DOI 10.1111/febs.13605
    Database MEDical Literature Analysis and Retrieval System OnLINE

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