Temat: cathepsin - Prolib Integro

Skocz do pozycji: 1.

Tytuł:: Muscle cathepsins of marine fish and invertebrates
Autorzy:: Kolodziejska, I.
Sikorski, Z.E.
Tematy:: invertebrate
endopeptidase
fish
structure
protease
extracellular matrix
lysosome
exopeptidase
cathepsin C
cathepsin A
muscle protein
myofibrillar protein
lysosomal protease
marine fish
protein
myofibril
muscle cathepsin
food preservation
sarcoplasm
cathepsin L
carboxypeptidase A
cathepsin B; Pokaż więcej
Wydawca:: Instytut Rozrodu Zwierząt i Badań Żywności Polskiej Akademii Nauk w Olsztynie
Powiązania:: https://bibliotekanauki.pl/articles/1372835.pdf Link otwiera się w nowym oknie
Opis:: Muscle proteases are located mainly in the lysosomes, in the sarcoplasm, and in the extracellular matrix of the connective tissue surrounding each cell. The lysosomal proteases, cathepsins, have optimum activity in the acidic range, although many of them retain high activity also 1 or 2 pH units away from the optimum value. Among the cathepsins there are endopeptidases and exopeptidases. Most cathepsins hydrolyse several proteins of the myofibrils. The major protease of the lysosomes in fish and squid muscles is cathepsin D, an aspartyl endoproteinase. Although it is present in the muscle fibre itself, its generally rather low activity at low temperature limits its significance in tenderization of refrigerated fish of most species. Cathepsin L, a cysteinyl protease, is involved in autolysis and softening in matured chum salmon. Cathepsin B, a cysteinyl carboxypeptidase, is capable to attack also some myofibrillar proteins. Cathepsin A or carboxypeptidase A, and cathepsin C, a dipeptidyl hydrolase and dipeptidyl transferase, contribute to the hydrolysis of muscle proteins in a concerted action with the other cathepsins.
Dostawca treści:: Biblioteka Nauki

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Tytuł:: Protective effect of 6-shogaol against endotoxin-induced periodontitis in rats
Autorzy:: Qi, HongYan
Han, Bing
Tematy:: periodontitis
anti-oxidants
cathepsin D
β-glucuronidase
cathepsin B
6-Shogaol; Pokaż więcej
Wydawca:: Polskie Towarzystwo Farmaceutyczne
Powiązania:: https://bibliotekanauki.pl/articles/895573.pdf Link otwiera się w nowym oknie
Opis:: Periodontal diseases are the most prevalent bacterial ailments, affecting 10–15% of the global population, and eventually leading to tooth loss if left untreated. Shogaols obtained from ginger (Zingiber officinale) exhibit significant anti-inflammatory activity. However, the antibacterial potential of shogaols against periodontitis remains unexplored. Therefore, we investigated the effects of 6-shogaol (6-SH) on various factors responsible for periodontitis such as inflammation. Escherichia coli endotoxin was used to induce experimental periodontitis, and the effects of 6-SH on hydrogen peroxide, superoxide anion, myeloperoxidase activity, and lipid peroxides were estimated together with cathepsin B, cathepsin D, β-glucuronidase, acid phosphatase, and C-reactive protein activity in serum. In addition, the levels of ascorbic acid, α-tocopherol, ceruloplasmin, reduced glutathione, superoxide dismutase, catalase, glutathione peroxidase, and glutathione S-transferase were estimated in serum after 6-SH treatment. Reactive oxygen species and lipid peroxide levels were significantly reduced in the 6-SH-treated group. Moreover, lysosomal enzyme (cathepsin B, cathepsin D, β-glucuronidase and acid phosphatase) and acute-phase protein (C-reactive protein and fibrinogen) levels significantly declined after administration of 6-SH. Meanwhile, non-enzymatic antioxidant systems (e.g., ascorbic acid, α-tocopherol, ceruloplasmin, and reduced glutathione) and antioxidant enzymes (e.g., catalase, superoxide dismutase, glutathione peroxidase, and glutathione S-transferase) were significantly increased in the 6-SH-treated group. These results suggest a protective effect of 6-SH against experimental periodontitis via the regulation of key disease markers.
Dostawca treści:: Biblioteka Nauki

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Tytuł:: Was the serine protease cathepsin G discovered by S. G. Hedin in 1903 in bovine spleen?
Autorzy:: Palesch, David
Sieńczyk, Marcin
Oleksyszyn, Jozef
Reich, Michael
Wieczerzak, Ewa
Boehm, Bernhard
Burster, Timo
Tematy:: spleen cells
Hedin
cathepsin
proteases; Pokaż więcej
Wydawca:: Polskie Towarzystwo Biochemiczne
Powiązania:: https://bibliotekanauki.pl/articles/1039945.pdf Link otwiera się w nowym oknie
Opis:: In the beginning of the 20th century, enzymes with proteolytic activity were classified as peptidases, Erepsin, and proteases. Among these, pepsin, trypsin, and autolytic enzymes were of the protease class. Spleen-derived proteases were poorly characterized until Sven Gustaf Hedin performed several digestion experiments with bovine spleen. He incubated minced bovine spleen under acidic or neutral conditions and characterized two active proteases; the results were published in 1903. The first protease was named α-protease and was active under neutral conditions. The second was named β-protease and was active under acidic conditions. We replicated Hedin's experiments according to his methods and found, by using activity-based probes to visualize proteases, that the historical α-protease is the present-day serine protease cathepsin G (CatG), which is known to be important in several immune processes, including antigen processing, chemotaxis, and activation of surface receptors. The β-protease, however, comprised different proteases including CatX, B, S, and D. We suggest that Hedin described CatG activity in bovine spleen over 100 years ago.
Dostawca treści:: Biblioteka Nauki

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Tytuł:: Fluorogenic peptide substrates for carboxydipeptidase activity of cathepsin B.
Autorzy:: Stachowiak, Krystyna
Tokmina, Monika
Karpińska, Anna
Sosnowska, Renata
Wiczk, Wiesław
Tematy:: fluorogenic substrate
cathepsin B
cystatins; Pokaż więcej
Wydawca:: Polskie Towarzystwo Biochemiczne
Powiązania:: https://bibliotekanauki.pl/articles/1043322.pdf Link otwiera się w nowym oknie
Opis:: Cathepsin B is a lysosomal cysteine protease exhibiting mainly dipeptidyl carboxypeptidase activity, which decreases dramatically above pH 5.5, when the enzyme starts acting as an endopeptidase. Since the common cathepsin B assays are performed at pH 6 and do not distinguish between these activities, we synthesized a series of peptide substrates specifically designed for the carboxydipeptidase activity of cathepsin B. The amino-acid sequences of the P5-P1 part of these substrates were based on the binding fragments of cystatin C and cystatin SA, the natural reversible inhibitors of papain-like cysteine protease. The sequences of the P'1-P'2 dipeptide fragments of the substrates were chosen on the basis of the specificity of the S'1-S'2 sites of the cathepsin B catalytic cleft. The rates of hydrolysis by cathepsin B and papain, the archetypal cysteine protease, were monitored by a continuous fluorescence assay based on internal resonance energy transfer from an Edans to a Dabcyl group. The fluorescence energy donor and acceptor were attached to the C- and the N-terminal amino-acid residues, respectively. The kinetics of hydrolysis followed the Michaelis-Menten model. Out of all the examined peptides Dabcyl-R-L-V-G-F- E(Edans) turned out to be a very good substrate for both papain and cathepsin B at both pH 6 and pH 5. The replacement of Glu by Asp turned this peptide into an exclusive substrate for cathepsin B not hydrolyzed by papain. The substitution of Phe by Nal in the original substrate caused an increase of the specificity constant for cathepsin B at pH 5, and a significant decrease at pH 6. The results of kinetic studies also suggest that Arg in position P4 is not important for the exopeptidase activity of cathepsin B, and that introducing Glu in place of Val in position P2 causes an increase of the substrate preference towards this activity.
Dostawca treści:: Biblioteka Nauki

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Tytuł:: The activity of cathepsin D and alpha-1 antitrypsin in hip and knee osteoarthritis
Autorzy:: Olszewska-Slonina, Dorota
Matewski, Dariusz
Jung, Stanislaw
Olszewski, Krzysztof
Czajkowski, Rafal
Braszkiewicz, Joanna
Wozniak, Alina
Kowaliszyn, Bogna
Tematy:: protease
cathepsin D
alpha 1-antitrypsin
antiprotease
cartilage
osteoarthritis; Pokaż więcej
Wydawca:: Polskie Towarzystwo Biochemiczne
Powiązania:: https://bibliotekanauki.pl/articles/1039618.pdf Link otwiera się w nowym oknie
Opis:: The progress of cartilage decay during joint degeneration is not well monitored with biochemical methods. The role of cathepsin D (CAT-D) in articular cartilage deterioration remains unclear. The aim of this study is to assess the activity of CAT-D and alpha-1 antitrypsin (AAT) in blood in patients with hip or knee osteoarthritis. The activity of CAT-D and AAT in blood serum of 40 women and 21 men with hip or knee osteoarthritis was determined before total joint replacement, on the tenth day after surgery, and once in 54 healthy patients. The preoperative activity of CAT-D in patients with osteoarthritis was lower by 53.6% (11.00 ± 4.54 10-2 nM released tyrosine/mg protein/min, P < 0.001) and after surgery by 55.0% (10.67 ± 4.64 10-2 nM released tyrosine/mg protein/min, P < 0.001) when compared to its activity in healthy patients. There was no significant statistical difference between CAT-D activity before the surgery and its activity on the tenth day after it in the analyzed group (P< 0.496). Simultaneously, the preoperative activity of AAT in the OA (osteoarthritis) patients was by 25.5% (0.93 ± 0.32 mg inhibited trypsin/ml blood serum, P < 0.001) and postoperative was by 44.9% higher (1.26 ± 0.36 mg inhibited trypsin/ml blood serum, P < 0.001) than in healthy patients. The low CAT-D activity in osteoarthritis of big joints is associated with a decrease of cartilage cells during the degenerative process. The higher activity of acute phase protein AAT in OA patients' blood serum confirms the inflammatory component in the osteoarthritis process.
Dostawca treści:: Biblioteka Nauki

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Skocz do pozycji: 6.

Tytuł:: Investigation of osteoclast cathepsin K activity in osteoclastogenesis and bone loss using a set of chemical reagents
Autorzy:: Drąg, Marcin
Vizovisek, Matej
Kozieł, Joanna
Turk, Boris
Poręba, Marcin
Ciastoń, Izabela
Kasperkiewicz, Paulina
Janiszewski, Tomasz
Kołt, Sonia
Dostawca treści:: Repozytorium Uniwersytetu Jagiellońskiego

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Skocz do pozycji: 7.

Tytuł:: Lack of cathelicidin processing in Papillon-Lefèvre syndrome patients reveals essential role of LL-37 in periodontal homeostasis
Autorzy:: Eickholz, Peter
Potempa, Jan
Stennicke, Henning
Guentsch, Arndt
Schacher, Beate
Kantyka, Tomasz
Adamowicz, Karina
Hiemstra, Pieter
Puklo, Magdalena
Eick, Sigrun
Opis:: Background : Loss-of-function point mutations in the cathepsin C gene are the underlying genetic event in patients with Papillon-Lefèvre syndrome (PLS). PLS neutrophils lack serine protease activity essential for cathelicidin LL-37 generation from hCAP18 precursor. Aim : We hypothesized that a local deficiency of LL-37 in the infected periodontium is mainly responsible for one of the clinical hallmark of PLS: severe periodontitis already in early childhood. Methods : To confirm this effect, we compared the level of neutrophil-derived enzymes and antimicrobial peptides in gingival crevicular fluid (GCF) and saliva from PLS, aggressive and chronic periodontitis patients. Results : Although neutrophil numbers in GCF were present at the same level in all periodontitis groups, LL-37 was totally absent in GCF from PLS patients despite the large amounts of its precursor, hCAP18. The absence of LL-37 in PLS patients coincided with the deficiency of both cathepsin C and protease 3 activities. The presence of other neutrophilic anti-microbial peptides in GCF from PLS patients, such as alpha-defensins, were comparable to that found in chronic periodontitis. In PLS microbial analysis revealed a high prevalence of Aggregatibacter actinomycetemcomitans infection. Most strains were susceptible to killing by LL-37. Conclusions : Collectively, these findings imply that the lack of protease 3 activation by dysfunctional cathepsin C in PLS patients leads to the deficit of antimicrobial and immunomodulatory functions of LL-37 in the gingiva, allowing for infection with A. actinomycetemcomitans and the development of severe periodontal disease.
Dostawca treści:: Repozytorium Uniwersytetu Jagiellońskiego

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Skocz do pozycji: 8.

Tytuł:: Structure-function relationships in class CA1 cysteine peptidase propeptides
Autorzy:: Wiederanders, Bernd
Tematy:: papain family
cathepsin L-like peptidases
processing
propeptide inhibition
foldase; Pokaż więcej
Wydawca:: Polskie Towarzystwo Biochemiczne
Powiązania:: https://bibliotekanauki.pl/articles/1043442.pdf Link otwiera się w nowym oknie
Opis:: Regulation of proteolytic enzyme activity is an essential requirement for cells and tissues because proteolysis at a wrong time and location may be lethal. Proteases are synthesized as inactive or less active precursor molecules in order to prevent such inappropriate proteolysis. They are activated by limited intra- or intermolecular proteolysis cleaving off an inhibitory peptide. These regulatory proenzyme regions have attracted much attention during the last decade, since it became obvious that they harbour much more information than just triggering activation. In this review we summarize the structural background of three functions of clan CA1 cysteine peptidase (papain family) proparts, namely the selectivity of their inhibitory potency, the participation in correct intracellular targeting and assistance in folding of the mature enzyme. Today, we know more than 500 cysteine peptidases of this family from the plant and animal kingdoms, e.g. papain and the lysosomal cathepsins L and B. As it will be shown, the propeptide functions are determined by certain structural motifs conserved over millions of years of evolution.
Dostawca treści:: Biblioteka Nauki

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Skocz do pozycji: 9.

Tytuł:: Effects of elastase and cathepsin G on the levels of membrane and soluble TNF\alpha
Autorzy:: Mężyk-Kopeć, Renata
Potempa, Jan
Bzowska, Monika
Mak, Paweł
Mickowska, Barbara
Bereta, Joanna
Bzowska, Małgorzata
Dostawca treści:: Repozytorium Uniwersytetu Jagiellońskiego

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Skocz do pozycji: 10.

Tytuł:: Effect of selected physico-chemical factors on Baltic herring meat hydrolysis rate and proteolytic enzyme activity
Wpływ niektórych czynników fizykochemicznych na aktywność enzymów proteolitycznych i szybkość hydrolizy białek mięsa śledzia bałtyckiego
Autorzy:: Fik, M.
Sypniewska, L.
Thi, N.P.
Tematy:: Baltic herring
proteolytic enzyme
protein autohydrolysis
papin
cathepsin
B-500 protease; Pokaż więcej
Wydawca:: Instytut Rozrodu Zwierząt i Badań Żywności Polskiej Akademii Nauk w Olsztynie
Powiązania:: https://bibliotekanauki.pl/articles/1396371.pdf Link otwiera się w nowym oknie
Opis:: The effect of some physico-chemical factors on the rate of Baltic herring meat protein autohydrolysis and hydrolysis due to papain and B-500 protease from Bacillus subtilis is reported.
Badano wpływ niektórych czynników fizykochemicznych (pH, temperatura, czas inkubacji, dodatek NaCl) na aktywność enzymów proteolitycznych i szybkość hydrolizy białek mięsa śledzia bałtyckiego. Stwierdzono maksimum aktywności proteinaz mięśniowych w pH 4,2 a proteinaz rozdrobnionej ryby całej w pH 3,7 i 8,3 z tym, że hydroliza w pH 3,7 była intensywniejsza niż w pH 8,3 (rys. 1). W obu przypadkach największą aktywność endogennych enzymów proteolitycznych wykazano w temp. 50°C (rys. 2). Stosowany w charakterze konserwanta chlorek sodu w stężeniach do 10 g na 100 g rozdrobnionej ryby całej powodował nieznaczne hamowanie aktywności enzymów tego surowca po krótkiej hydrolizie i wpływał na nie stymulująco po długim czasie hydrolizy (rys. 3). Większe stężenia NaCl znacznie zmniejszały szybkość hydrolizy białek. W celu zwiększenia szybkości hydrolizy białek ryby całej zastosowano papainę (rys. 4) i proteazę B-500 (rys. 5), z których ta ostatnia, pomimo większego inaktywującego wpływu chlorku sodu, była aktywniejsza niż papaina. Oba preparaty enzymatyczne charakteryzowały się mniejszą podatnością na inaktywujący wpływ NaCl, aniżeli endogenne enzymy proteolityczne surowca. Do hydrolizy śledzia w warunkach przemysłowych spośród tych dwóch preparatów lepiej nadaje się proteaza B-500.
Dostawca treści:: Biblioteka Nauki

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