Wyniki wyszukiwania - Biblioteka Nauki

1

Regulatory role of cathepsin D in apoptosis

100%

Minarowska A. , Miarowski L. , Karwowska A. , Gacko M.

Folia Histochemica et Cytobiologica

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2007

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tom 45

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nr 3

2

Tumor budding intensity in relation to cathepsin D expression and some clinicopathological features of colorectal cancer

88%

Guzinska-Ustymowicz K. , Famulski W. , Sulkowska M. , Chabowski A. , Zalewski B. , Sulkowski S. , Gnojnicki J.

Folia Histochemica et Cytobiologica. Supplement

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2001

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tom 39

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nr 1

3

Immunohistochemical evaluation of cathepsin D expression in colorectal cancer

88%

Chabowski A. , Sulkowska M. , Sulkowski S. , Famulski W. , Skrzydlewska E. , Kisielewski W.

Folia Histochemica et Cytobiologica

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2001

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tom 39

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nr 2

4

Protective effect of 6-shogaol against endotoxin-induced periodontitis in rats

75%

Qi H. , Han B.

Acta Poloniae Pharmaceutica - Drug Research

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2018

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tom 75

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nr 6

1391-1398

EN

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.

5

The activity of cathepsin D and alpha-1 antitrypsin in hip and knee osteoarthritis

75%

Olszewska-Slonina D. , Matewski D. , Jung S. , Olszewski K. J. , Czajkowski R. , Braszkiewicz J. , Wozniak A. , Kowaliszyn B.

Acta Biochimica Polonica

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2013

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tom 60

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nr 1

99-106

EN

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.

6

Molecular characterization, tissue distribution, and expression profiling of the CTSD gene during goose ovarian follicle development

75%

Zhu J. , Hu S. , Lu Y. , Rong Y. , Qing E. , Li L. , Wang J.

Folia Biologica

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2021

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tom 69

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nr 1

7

Asymmetric peptidomimetics containing L-tartaric acid core inhibit the aspartyl peptidase activity and growth of Leishmania amazonensis promastigotes

75%

Santos A. L. S. , Matteoli F. P. , Sangenito L. S. , Branquinha M. H. , Cotrim B. A. , Resende G. O.

Acta Parasitologica

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2018

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tom 63

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nr 1

8

Wpływ kąpieli w zimnej wodzie na powysiłkową aktywność a1-antytrypsyny i wybranych enzymów lizosomalnych we krwi zdrowych mężczyzn – doniesienia wstępne

63%

Pawłowska M. , Mila- Kierzenkowska C. , Boraczyński T. , Boraczyński M. , Sutkowy P. , Paprocki J. , Woźniak A.

Polish Journal of Sports Medicine

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2017

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tom 33(3)

193-201

EN

Background. The aim of the study was to determine the effect of winter bath after physical exercise on the activity of α1-antitrypsin (AAT) and selected lysosomal enzymes: arylsulfatase (ASA), acid phosphatase (AcP) and cathepsin D (CTS D) in healthy males’ blood. Material and methods. 22 males participated in two session of aerobic physical exercise. After one session the subjects rested in room temperature while after the other session they bathed in cold water (3 minutes, 8ºC; experiment 2). During each stage they had blood taken from the basilic vein prior to physical exercise and 2 and 20 minutes after the exercise. The activity of AAT, ASA, AcP and CTS D was assayed in blood serum. The obtained results were subjected to statistical analysis using ANOVA test. The changes at the level p<0.05 were regarded as statistically significant. Results. A statistically significant increase in AcP and CTS D activity was found as well as a decrease in AAT activity following physical exercise and resting at room temperature as compared with the activity of the assayed parameters prior to physical exercise. Conversely, no statistically significant differences in protease inhibitor activity (AAT) and lysosomal enzyme activity were noted after physical exercise and cold water bath as compared with their activity measured prior to 30-minute long physical exercise. Conclusions. Hot water bath applied after physical exercise increases the stability of lysosomal membranes and may result in a decrease of post-exercise muscle damage.

PL

Wstęp. Celem pracy było określenie wpływu kąpieli w zimnej wodzie zastosowanej po wysiłku fizycznym na aktywność α1-antytrypsyny (AAT) oraz wybranych enzymów lizosomalnych: arylosulfatazy (ASA), kwaśnej fosfatazy (AcP) i katepsyny D (CTS D) we krwi zdrowych mężczyzn. Materiał i metody. 22 mężczyzn poddano dwóm sesjom 30-min. aerobowego wysiłku fizycznego. Po jednym z nich mężczyźni odpoczywali w temperaturze pokojowej, podczas gdy po drugim poddano ich kąpieli w zimnej wodzie (3 min, 8ºC; doświadczenie 2). W każdym z etapów krew pobrano trzykrotnie z żyły odłokciowej: przed wysiłkiem fizycznym oraz 2 i 20 min. po zakończeniu wysiłku. W surowicy krwi oznaczono aktywności AAT, ASA, AcP i CTS D. Uzyskane wyniki poddano analizie statystycznej za pomocą testu ANOVA. Zmiany na poziomie p<0,05 uznano za istotne statystycznie. Wyniki. Wykazano istotny statystycznie wzrost aktywności AcP i CTS D oraz obniżenie aktywności AAT po wysiłku fizycznym i odpoczynku w temperaturze pokojowej w porównaniu do aktywności oznaczanych parametrów przed wysiłkiem fizycznym. Nie odnotowano natomiast istotnych statystycznie różnic aktywności inhibitora proteaz (AAT) oraz oznaczanych enzymów lizosomalnych po wysiłku fizycznym i kąpieli w zimnej wodzie w porównaniu z ich aktywnością przed 30-minutowym wysiłkiem. Wnioski. Kąpiel w zimnej wodzie zastosowana po wysiłku fizycznym zwiększa stabilność błon lizosomalnych i może skutkować zmniejszeniem powysiłkowych uszkodzeń mięśni.

9

Quantitative determination and localization of cathepsin D and its inhibitors

63%

Minarowska A. , Karwowska A. , Gacko M.

Folia Histochemica et Cytobiologica

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2009

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tom 47

|

nr 2

153-177

10

Stress-induced enhancement of activity of lymphocyte lysosomal enzymes in pigs of different stress-susceptibility

63%

Stojek W. , Borman A. , Glac W. , Baracz-Jozwik B. , Witek B. , Kamyczek M. , Tokarski J.

Journal of Physiology and Pharmacology. Supplement

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2006

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tom 57

|

nr 8

61-72

EN

To evaluate a possible mechanism of stress-induced lymphopenic effect we assessed the activity of lymphocyte lysosomal enzymes (LE) under immobilization. The effects of immobilization stress on LE (AP, acid phosphatase, cathepsin D and L, ß-N-acetyl-glucosamidase) activity in lymphocytes, number of lymphocytes and plasma cortisol (COR) level in the peripheral blood were examined in the cross-bred Pietrain pigs showing genotypic (presence or lack of RyR1 gene mutation) and phenotypic (reactivity to halothane) differences. It was found that immobilization stress evoked an increase in LE which was concomitant with lymphopenia and a rise of COR level. The most pronounced enhancement of LE, which may reflect a tendency to lymphocyte cytolysis, was found in the recessive homozygotes RyR1 (nn) phenotypically defined as stress/halothane susceptible as well as in the heterozygotes RyR1 (Nn) included in the group of stress/halothane resistant. Despite this individual variability the stress-induced increase in LE activity was present in all the animals. It seems that a possibility of destruction (lysis) of lymphocyte cells should not be excluded as one of the causes of stress lymphopenia.

11

Expression of syndecan-1 and cathepsins D and K in advanced esophageal squamous cell carcinoma

63%

Szumilo J. , Burdan F. , Zinkiewicz K. , Dudka J. , Klepacz R. , Dabrowski A. , Korobowicz E.

Folia Histochemica et Cytobiologica

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2009

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tom 47

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nr 4

12

Effect of heavy metal cations on the activity of cathepsin D (in vitro study)

63%

Karwowska A. , Lapinski R. , Gacko M. , Grzegorczyk E. , Zurawska J. , Karczewski J. K.

Folia Histochemica et Cytobiologica

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2012

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tom 50

|

nr 3

13

The activity and immunoexpression of cathepsin D in rat male reproductive organs

63%

Burdan F. , Szumilo J. , Dudka J. , Dabrowski A. , Maciejewski R. , Wojtowicz Z.

Folia Morphologica

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2006

|

tom 65

|

nr 2

111-115

EN

Cathepsin D is a cysteine endopeptidase that belongs to the lysosomal enzyme family. The aim of the study was to evaluate the enzyme immunoexpression and activity in selected male genital organs in mature Wistar rats. The activity of cathepsin D was measured spectrophotometrically in homogenates of the testis, epididymis, seminal vesicle and prostate. Immunohistochemical staining was also performed in the ductus deferens. Enzyme activity was found in the following sequence: testis>epididymis>dorsal prostatic lobe>seminal vesicle>lateral prostatic lobe>ventral prostatic lobe. Although there were differences in enzyme activity between various organs of the male reproductive system, cathepsin D immunoreactivity was seen exclusively in the Sertoli and Leydig cells in the testis.

14

The activity of cathepsin D in saliva of cystic fibrosis patients

63%

Minarowska A. , Minarowski L. , Karwowska A. , Sands D. , Dabrowska E.

Folia Histochemica et Cytobiologica

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2007

|

tom 45

|

nr 3

15

Cathepsin D and cathepsin L activities in the wall of aortic aneurysm and parietal thrombus determined by means of synthetic substrates

63%

Gacko M. , Worowska A. , Glowinski S.

Bulletin of the Polish Academy of Sciences. Biological Sciences

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2000

|

tom 48

|

nr 1

16

CD44 expression in colorectal cancer. An immunohistochemical study including correlation with cathepsin D and some tumour clinicopathological features

63%

Zalewski B. , Famulski W. , Sulkowska M. , Piotrowski Z. , Kisielewski W. , Guzinska-Ustymowicz K.

Folia Histochemica et Cytobiologica. Supplement

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2001

|

tom 39

|

nr 1

17

The effects of dehydroepiandrosterone on the activity of selected lysosomal enzymes in mice from different age groups

51%

Krol T. , Lysek-Gladysinska M. , Lach H. , Kochman K. , Trybus W. , Staszczyk K. , Mycinska M. , Kopacz-Bednarska A. , Trybus E. , Wieczorek A. , Gren A.

Acta Biologica Cracoviensia. Series Zoologia

|

2008

|

tom 50

37-42

18

Cathepsin D inhibitors

51%

Gacko M. , Minarowska A. , Karwowska A. , Minarowski L.

Folia Histochemica et Cytobiologica

|

2007

|

tom 45

|

nr 4

291-313

19

Human cathepsin D

51%

Minarowska A. , Gacko M. , Karwowska A. , Minarowski L.

Folia Histochemica et Cytobiologica

|

2008

|

tom 46

|

nr 1

23-38

20

Influence of retinoids on the lysosomal system in mouse liver

51%

Krol T.

Acta Biologica Cracoviensia. Series Zoologia

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2000

|

tom 42