Wyniki wyszukiwania

1

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

100%

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

Folia Histochemica et Cytobiologica

|

2020

|

tom 58

|

nr 1

2

Macrophage stimulation and proteinase inhibitors balance during inflammation

100%

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

Folia Histochemica et Cytobiologica

|

1992

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tom 30

|

nr 4

3

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

100%

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

Polish Journal of Environmental Studies

|

1999

|

tom 08

|

nr 4

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.

4

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

100%

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

|

nr 3

5

Activity of liver proteases in experimental methanol intoxication

100%

Skrzydlewska E., Skrzydlewski Z., Worowski K.

Acta Biochimica Polonica

|

1997

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tom 44

|

nr 2

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.

6

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

84%

Gorodkiewicz E., Breczko J., Sankiewicz A.

Folia Histochemica et Cytobiologica

|

2012

|

tom 50

|

nr 1

7

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

84%

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

Journal of Physiology and Pharmacology. Supplement

|

2005

|

tom 56

|

nr 3

159-179

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.

8

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

84%

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

Polish Journal of Veterinary Sciences

|

2000

|

tom 03

|

nr 4

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.

9

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

84%

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

Cellular and Molecular Biology Letters

|

1999

|

tom 04

|

nr 2

10

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

67%

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

Polish Journal of Veterinary Sciences

|

2001

|

tom 04

|

nr 2

11

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

67%

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

|

2013

|

tom 31

|

nr 4

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.

12

Enzyme activity in pig meat of different meatiness

67%

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

Annals of Animal Science. Supplement

|

2002

|

nr 2

13

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

67%

Gacko M., Worowska A., Glowinski S.

Bulletin of the Polish Academy of Sciences. Biological Sciences

|

2000

|

tom 48

|

nr 3

14

Ustalanie rozmieszczenia i oznaczanie aktywnosci proteinaz w hepatocytach w zatruciu kadmem

51%

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

Acta Poloniae Toxicologica. Suplement

|

1994

|

tom 02

|

nr 1

83-88

15

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

51%

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

Bromatologia i Chemia Toksykologiczna

|

2008

|

tom 41

|

nr 3

262-264

16

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

51%

Karwowska A., Gacko M., Worowska A.

Bromatologia i Chemia Toksykologiczna

|

2008

|

tom 41

|

nr 3

258-261

Ograniczanie wyników

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

Macrophage stimulation and proteinase inhibitors balance during inflammation

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

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

Activity of liver proteases in experimental methanol intoxication

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

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

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

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

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

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

Enzyme activity in pig meat of different meatiness

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

Ustalanie rozmieszczenia i oznaczanie aktywnosci proteinaz w hepatocytach w zatruciu kadmem

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

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