Wyniki wyszukiwania

1

Serodiagnosis of Fasciola gigantica infection in buffaloes with native cathepsin-L proteases and recombinant cathepsin L1-D

100%

Aftab A., Lall R., Bisen S., Anandanarayanan A., Rialch A., Chamuah J. K., Yadav S., Silamparasan M., Raina O. K.

Acta Parasitologica

|

2020

|

tom 65

|

nr 2

2

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

84%

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

Journal of Physiology and Pharmacology. Supplement

|

2006

|

tom 57

|

nr 8

61-72

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.

3

Molecular cloning and bioinformatic characterisation of FhPcW1, a new isoform of cathepsin L from adult Fasciola hepatica

84%

Jaros S., Zygner W., Januszkiewicz K., Jaros D., Wedrychowicz H.

Bulletin of the Veterinary Institute in Puławy

|

2010

|

tom 54

|

nr 4

The aim of this study was to clone new secretory antigen of Fasciola hepatica and to predict its availability for immune system. The new cathepsin L - FhPcW1 (F. hepatico cysteine proteinase Warsaw 1), GenBank accession: EF407948, cDNA was cloned from adult F. hepatica flukes using RACE-PCR method. FhPcW1 is encoded by a 1,066 bp mRNA with a predicted open reading frame (ORF) of 326 amino acids (predicted pl = 5.41, m.w. = 37.137 kDa). Performed bioinformatic analysis included alignments of the nucleotide and amino acid sequences, the ExPASy (Expert Protein Analysis System) proteomics server of the Swiss Institute of Bioinformatics and National Center for Biotechnology Information. Performed analyses allowed to suppose that FhPcW1 is a secreted protein, which contains signal peptide, serine, threonine, tyrosine phosphorylation sites and four tyrosine sulfation sites, and does not contain glycosylation sites. The ORF corresponding to FhPcW1 exhibited strong similarity to previously cloned cathepsins L from the F. hepatico as well as F. gigantica. Predicted biochemical characteristics fits to the described before F. hepatica cathepsin Ls. Moreover, three dimensional model and MHC types ligation strength prediction were performed. Analysis of MHC type I and II peptide binding suggests that FhPcW1 may have significant immunogenic potential. The potential HLA II epitopes are situated at the outer surface of this protein. Thus, these epitopes seems to be available for immune response, especially for antibodies. This result may show that FhPcW1 seems to be a promising antigen for vaccination against F. hepatica.

4

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

84%

Gacko M., Worowska A., Glowinski S.

Bulletin of the Polish Academy of Sciences. Biological Sciences

|

2000

|

tom 48

|

nr 1

5

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

67%

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

6

Control of active B and L cathepsins in tissues of colorectal cancer using cystatins isolated from chicken egg proteins: in vitro studies

67%

Hap A., Kielan W., Grzebieniak Z., Siewinski M., Rudnicki J., Tarnawa R., Rudno-Rudzinska J., Agrawal A. K.

Folia Histochemica et Cytobiologica

|

2011

|

tom 49

|

nr 4

7

Influence of retinoids on the lysosomal system in mouse liver

67%

Krol T.

Acta Biologica Cracoviensia. Series Zoologia

|

2000

|

tom 42

8

Activity of the lysosomal system in mouse liver after hydrocortisone administration

67%

Krol T., Kolataj A.

Acta Biologica Cracoviensia. Series Zoologia

|

2000

|

tom 42

9

Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik

Muscle cathepsins of marine fish and invertebrates

51%

Kolodziejska I., Sikorski Z. E.

Polish Journal of Food and Nutrition Sciences

|

1995

|

tom 04

|

nr 3

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.

Ograniczanie wyników

Serodiagnosis of Fasciola gigantica infection in buffaloes with native cathepsin-L proteases and recombinant cathepsin L1-D

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

Molecular cloning and bioinformatic characterisation of FhPcW1, a new isoform of cathepsin L from adult Fasciola hepatica

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

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

Control of active B and L cathepsins in tissues of colorectal cancer using cystatins isolated from chicken egg proteins: in vitro studies

Influence of retinoids on the lysosomal system in mouse liver

Activity of the lysosomal system in mouse liver after hydrocortisone administration

Muscle cathepsins of marine fish and invertebrates