Wyniki wyszukiwania - Biblioteka Nauki

1

Was the serine protease cathepsin G discovered by S. G. Hedin in 1903 in bovine spleen?

100%

Palesch D. , Sieńczyk M. , Oleksyszyn J. , Reich M. , Wieczerzak E. , Boehm B. O. , Burster T.

Acta Biochimica Polonica

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2011

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tom 58

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nr 1

39-44

EN

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.

2

MiR-491-3p is down-regulated in postmenopausal osteoporosis and affects growth, differentiation and apoptosis of hFOB1.19 cells through targeting CTSS

75%

Hu W.-X. , Li H. , Jiang J.-Z.

Folia Histochemica et Cytobiologica

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2020

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tom 58

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nr 1

3

The 3' untranslated region of mRNAs from the ciliate Nyctotherus ovalis

75%

Destables E. , Thomas N. A. , Boxma B. , Van Alen T. A. , Van der Staay G. W. M. , Hackstein J. H. P. , McEwan N. R.

Acta Protozoologica

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2005

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tom 44

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nr 3

4

A comparison of methanol and ethanol effects on the activity and distribution of lysosomal proteases

75%

Skrzydlewska E. , Roszkowska A. , Moniuszko-Jakoniuk J.

Polish Journal of Environmental Studies

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1999

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tom 08

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nr 4

EN

The activity of lysosomal proteolytic enzymes (cathepsin A, B, C, D and E) in cytosol and in the liver homogenate and in the blood plasma of rats intoxicated with methanol and ethanol was measured 6, 12 and 24 h and 2, 5 and 7 days after the intoxication. The activity of all proteases was increased in the cytosol from 12h to 5 days of alcohols intoxication, whereas the activity of these enzymes was decreased in the liver homogenate during the same time. Ethanol caused a higher increase in cytosol proteases activity than methanol. The magnitude of the decrease in proteolytic activity in the liver homogenate depends on the amino acid active center of the enzyme and on the kind of alcohol. The greatest decrease was observed for sulfhydryl and hydroxyl proteases and a smaller one for carboxyl proteases. Moreover methanol caused a greater decrease than ethanol. It was shown that the lysosomal proteases activity in the plasma was increased from 12 h to 5 days after alcohols intoxication and ethanol caused only a little less changes than methanol. The increase in the liver lipid peroxidation products examined as tiobarbituric acid reactive substances was also observed at the same time. These results indicate that during methanol and ethanol intoxication the cellular and lysosomal membranes are impaired and proteases are translocated into the blood. However, changes in proteases activities and proteases distribution within the hepatocytes may lead to disturbances in the catabolism of cell proteins and to destruction of liver cells.

5

Macrophage stimulation and proteinase inhibitors balance during inflammation

75%

Korolenko T. A. , Safina A. F. , Vereschagin E. I. , Dushkin M. I.

Folia Histochemica et Cytobiologica

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1992

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tom 30

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nr 4

6

Activity of liver proteases in experimental methanol intoxication

75%

Skrzydlewska E. , Skrzydlewski Z. , Worowski K.

Acta Biochimica Polonica

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1997

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tom 44

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nr 2

EN

Intoxication of rats with methanol (1.5 and 3.0 g/kg body weight) led to a significant, time- and dose-dependent decrease in the activities of cathepsins A, B and C, while the activity of cathepsin D was unaffected. The decrease was associated with a different partial release of individual cathepsins to the post-lysosomal fraction.

7

Surface plasmon resonance imaging biosensor for cystatin determination based on the application of bromelain, ficin and chymopapain

63%

Gorodkiewicz E. , Breczko J. , Sankiewicz A.

Folia Histochemica et Cytobiologica

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2012

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tom 50

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nr 1

8

Cathepsins and BID are involved in the molecular switch between apoptosis and autophagy in breast cancer MCF-7 cells exposed to camptothecin

63%

Lamparska-Przybysz M. , Gajkowska B. , Motyl T.

Journal of Physiology and Pharmacology. Supplement

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2005

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tom 56

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nr 3

159-179

EN

The details of molecular switching points between apoptosis and autophagy in tumor cells have still not been fully elucidated. This study focused on the role of cathepsin B and its substrate, BID as molecular links between apoptosis and autophagy in human breast cancer MCF-7 cells exposed to camptothecin. Apoptosis occurred rapidly with a peak in 60 min after drug administration, whereas autophagy developed at a much slower rate with continuous progression during 24 h of cell exposure to the drug. CPT induced very rapid activation of cathepsin B. Inhibition of cathepsins by E64d prevented CPT-induced BAX and BID aggregation on mitochondria and reduced significantly reduced apoptotic cell number. The above effects were accompanied by an increase in autophagosome formation, measured by expression of MAP I LC3. BID knock down resulted in strong suppression of CPT-induced apoptosis and a shift of cell death towards autophagy, manifesting with an increase of Beclin 1 and MAP I LC3 cellular content.

9

Charakterystyka i znaczenie proteinaz cysteinowych w procesie nowotworzenia

63%

Młudzik P. , Mirowski M.

Folia Medica Lodziensia

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2015

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tom 42

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nr 2

93-106

EN

Cysteine proteases also known as thiol or sulfhydryl proteases are enzymes responsible for catalyzing the hydrolysis of peptide bonds in proteins. They take part in many physiological and pathological processes. Their abnormal activity can lead to a number of disease states including tumor growth. They are involved in the process of carcinogenesis at multiple levels– they participate in the invasion, transformation, angiogenesis, apoptosis and metastasis. The best characterised cysteine proteases are the lysosomal cathepsins, that belong to the papain family. So far 11 cysteine cathepsins have been identified: B, L, H, S, K, F, V, X, W, O and C. They take part in the activation of many proenzymes and prohormones, MHC–II–mediated antigen presentation, bone remodeling, reproduction and apoptosis. Research on the role of cysteine proteases in carcinogenesis showed elevated expression of mRNA or enzymatic activity of cathepsins in many human cancers, eg. breast, lung, brain, gastrointestinal tract, head and neck and melanoma. Cancer procoagulant also belongs to the group of cysteine proteases, however its structure and functions are still the subject of research for many scientists. Elevated levels of activity and concentrations of cancer procoagulant in the serum and tissues from patients with cancer disease compared to those observed in healthy people, provides the possibility of using this factor in the diagnosis of cancer. Many preclinical studies have shown that achieving a stop proliferation and reducing the metastatic potential of tumor cells is possible with the use of cysteine proteinases inhibitors. That gives great hope for the possibility of their application in anticancer therapy.

PL

Proteinazy cysteinowe, nazywane również proteinazami tiolowymi lub sulfhydrolowymi, to enzymy odpowiedzialne za katalizowanie reakcji hydrolizy wiązań peptydowych w białkach. Biorą udział w licznych procesach fizjologicznych oraz patologicznych. Ich nieprawidłowa aktywność może prowadzić do wielu stanów chorobowych, w tym rozwoju nowotworów. Zaangażowane są one w proces kancerogenezy na wielu poziomach – uczestniczą w inwazji, transformacji nowotworowej, angiogenenezie, apoptozie i powstawaniu przerzutów. Najlepiej scharakteryzowanymi proteinazami cysteinowymi są, należące do rodziny papainy, lizosomalne katepsyny. Dotychczas poznano 11 ludzkich katepsyn cysteinowych: B, L, H, S, K, F, V, X, W, O i C. Biorą one udział w aktywacji wielu proenzymów i prohormonów, pośredniczą w prezentacji antygenu MHC–II, przebudowie kości, procesie reprodukcji oraz apoptozie. Badania nad udziałem proteinaz cysteinowych w procesie kancerogenezy wykazały podwyższoną ekspresję mRNA lub aktywność enzymatyczną katepsyn w wielu ludzkich nowotworach np. raku piersi, płuc, mózgu, żołądkowo–jelitowym, głowy, szyi oraz czerniaku. Do grupy proteinaz cysteinowych należy również prokoagulant nowotworowy, którego struktura, jak i pełnione przez niego funkcje są wciąż przedmiotem badań wielu naukowców. Podwyższony poziom aktywności, jak i stężenia antygenu prokoagulanta nowotworowego w surowicy krwi osób z chorobą nowotworową oraz w pooperacyjnym materiale tkankowym w stosunku do wartości obserwowanych u ludzi zdrowych, świadczy o możliwości wykorzystania tego czynnika w diagnostyce onkologicznej. Liczne badania przedkliniczne dowiodły, że zatrzymanie proliferacji oraz obniżenie potencjału metastatycznego komórek nowotworowych jest prawdopodobne przy użyciu inhibitorów proteinaz cysteinowych. Daje to duże nadzieje na możliwość zastosowania ich w terapii przeciwnowotworowej.

10

Effect of 3-hydroxy-3-methylbutyrate [HMB] on muscle cathepsins and calpain activities during the post-dexamethasone recovery period in young rats

63%

Jank M. , Ostaszewski P. , Rosochacki S. , Wilczak J. , Balasinska B.

Polish Journal of Veterinary Sciences

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2000

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tom 03

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nr 4

EN

This study was conducted to assess the effect of the leucine metabolite, 3-hydroxy-3-methylbutyrate (HMB) on animal performance, and also cathepsins and calpain II activities in the gastrocnemius muscle in young rats undergoing dexamethasone (DX) treatment and subsequent recovery. Five days of DX administration resulted in an increase in calpain activity. During 5 days of recovery alone, calpain activity was still elevated whereas HMB treatment decreased calpain activity to the values observed in the control group. DX treatment increased the total lysosomal proteolytic activity. HMB administration during the recovery period accelerated return of the proteolytic enzymes activity to the control values. The use of selective inhibitors of thiol and aspartic cathepsins (leupeptin and pepstatin, respectively) allowed us to determine the type of cathepsin responsible for the DX-induced proteolysis observed. Since DX treatment decreased cathepsin D activity (which returned to the control values during recovery) it is assumed that thiol cathepsins are involved in the increase of lysosomal proteolysis observed. We have demonstrated that lysosomal and Ca+2-dependent proteinases involved in myofibryllar protein degradation differ in their activity due to DX treatment. It has been concluded that HMB modifies muscle proteolysis through changes in the activity of the proteolytic enzymes. Practical applications of this phenomenon are discussed.

11

Interaction of cysteine proteinase inhibitor with liposomes. II. Effect on the inhibition of cathepsin

63%

Gutowicz J. , Saleh J. , Pola A. , Siewinski M.

Cellular and Molecular Biology Letters

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1999

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tom 04

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nr 2

12

The effect of cystatin B gene (CSTB) on productive traits in pigs

51%

Urbanski P. , Pierzchala M. , Terman A. , Kamyczek M. , Kapelanski W. , Bocian M. , Kawka M. , Parada R. , Roszczyk A. , Rozycki M. , Kuryl J.

Animal Science Papers and Reports

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2013

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tom 31

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nr 4

EN

Cystatin B gene is a candidate gene for carcass and meat quality traits of pigs and belongs to the family 1 of cysteine proteinase inhibitors. The enzyme is a cathepsin inhibitor and the proteolytic cystatin/cathepsin system plays an important role in the growth and development of muscles.Investigations presented here covered 707 pigs from different genetic groups reared in Poland. The aim of this study was to characterise the polymorphism of the CSTB gene identified with restriction endonuclease: TaqI and PvuII, and to analyse the relation between the CSTB genotypes and carcass traits. All tested animals proved to be monomorphic at the CSTB/TaqI locus. All three possible genotypes were observed with regard to the second CSTB/PvuII locus. In Polish Large White and Polish Landrace pigs the highest frequency was reported for BB homozygotes. The association between CSTB and carcass traits was found only in Polish Landrace pigs for the meat content of carcass, meat content of valuable cuts and weight of the loin.

13

Leucine metabolite 3-hydroxy-3-methylbutyrate (HMB) does not affect muscle cathepsin and calpain activities during impaired post-dexamethasone recovery in old rats

51%

Jank M. , Ostaszewski P. , Rosochacki S. J. , Wilczak J. , Balasinska B.

Polish Journal of Veterinary Sciences

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2001

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tom 04

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nr 2

14

The activity of enzymes of different subcellular localization in the wall of aortic aneurysm and parietal thrombus

51%

Gacko M. , Worowska A. , Glowinski S.

Bulletin of the Polish Academy of Sciences. Biological Sciences

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2000

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tom 48

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nr 3

15

Enzyme activity in pig meat of different meatiness

51%

Szalata M. , Pospiech E. , Lyczynski A. , Borzuta K.

Annals of Animal Science. Supplement

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2002

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nr 2

16

Hamowanie aktywnosci pepsyny i aktywnosci katepsyny D przez ekstrakty z nasion roslin spozywanych przez czlowieka

38%

Karwowska A. , Gacko M. , Worowska A.

Bromatologia i Chemia Toksykologiczna

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2008

|

tom 41

|

nr 3

258-261

17

Wplyw inhibitora katepsyny D z lupin nasion wyki siewnej na aktywnosc enzymow proteolitycznych

38%

Roszkowska-Jakimiec W. , Krupkowska A. , Bielawska K. , Milewska E.

Bromatologia i Chemia Toksykologiczna

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2008

|

tom 41

|

nr 3

262-264

18

Ustalanie rozmieszczenia i oznaczanie aktywnosci proteinaz w hepatocytach w zatruciu kadmem

38%

Skrzydlewska E. , Worowski K. , Moniuszko-Jakoniuk J. , Galazyn-Sidorczuk M.

Acta Poloniae Toxicologica. Suplement

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1994

|

tom 02

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nr 1

83-88