Wyniki wyszukiwania

1

Lysosomal acid phosphatase activity and progesterone secretion by porcine corpora lutea at various periods of the luteal phase

100%

Gregoraszczuk E. L., Sadowska J.

Folia Histochemica et Cytobiologica

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1997

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tom 35

|

nr 1

2

The lysosomal cell complex as a stress response indicator

86%

Kolataj A., Sliwa-Jozwik A., Jozwik A.

Animal Science Papers and Reports

|

2001

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tom 19

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nr 3

3

A lysosomal high molecular weight multienzyme complex

86%

Ostrowska H., Jedynasta-Kozlowska W., Kalinowska J.

Cellular and Molecular Biology Letters

|

2002

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tom 07

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nr Suppl.

4

Effect of reduced glutathione [GSH] on activity of lysosomal system in subcellular fractions of mouse kidney

86%

Sliwa-Jozwik A., Jozwik A., Fronczyk W., Guszkiewicz A., Kolataj A.

Animal Science Papers and Reports

|

2004

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tom 22

|

nr 2

Investigated was the effect of intraperitoneal injections (twice daily for seven consecutive days) of reduced glutathione (GSH) on activity of selected lysosomal hydrolases (alanine aminopeptidase, leucine aminopeptidase, cathepsins D and L, acid phosphatase and N-acetyl-β-D-glucosaminidase) in lysosomal, microsomal and cytosol fractions of mouse kidney. Most notable effect of exogenous GSH on the activity of the enzymes considered was observed in lysosomal, while the least in microsomal fraction. After a series of GSH injections the activity of enzymes increased significantly mainly In lysosomal fraction. It is assumed that the increase in activity of lysosomal enzymes following the GSH injections results from a physiological response of renal cells to this antioxidant.

5

The activation and inactivation of lysosomal and extralysosomal compartments - a simple general model

86%

Turski W. A., Zaslonka J., Szram S., Mussur M.

Cellular and Molecular Biology Letters

|

2002

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tom 07

|

nr Suppl.

6

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

72%

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

7

Effects of paclitaxel on lysosomal enzyme activity and ultrastructure of mouse liver cells

72%

Krol T.

Acta Biologica Cracoviensia. Series Zoologia

|

2002

|

tom 44

8

The lysosomal apparatus of peripheral blood lymphocytes reactivity in bursectomized or thymectomized chickens, after lipopolysaccharide E.coli [LPS] administration

72%

Graczyk S.

Bulletin of the Polish Academy of Sciences. Biological Sciences

|

1998

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tom 46

|

nr 2

9

Assessment of biological activity of new compounds designated to act as lysosomotropes

72%

Kleszczynska H., Bonarska D., Luczynski J., Witek S., Sarapuk J.

Polish Journal of Environmental Studies

|

2005

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tom 14

|

nr 6

This work contains the results of studies on the influence of new lysosomotropic substances on an erythrocyte membrane. The compounds studied were hydrochlorides of N,N-dimethylglycine alkyl esters (DMG-n) and N,N-dimethylalanine alkyl esters (DMAL-n) having two different-length alkyl chains (n = 12 and 16), oxalates of dimethylaminoalaninates (DMALs -n; n = 8, 10, 12, 14 and 16) and methobromides of glycinates and alaninates (DMALM-12 and DMGM-12). They were found to hemolyze erythrocytes, to change their osmotic resistance and to influence erythrocyte membrane fluidity. The results obtained indicate that observed changes were dependent on lipophilicities of the compounds. It was especially evident in the case of hemolytic efficiencies of the homologous series of alanine oxalates. Also, DMG-n and DMAL-n compounds significantly differed in their hemolytic properties. Again, slightly better hemolytic efficiency of DMG compounds in comparison with corresponding compounds having the same alkyl chain, DMAL, confirm such a conclusion. However, their hemolytic efficiencies were found to be moderate, which makes them potentially useful membrane modifiers. That feature is important for lysosomotropic compounds and its confirmation was the primary aim of the presented work. It is worth mentioning that DMGM and DMALM compounds exhibited better hemolytic efficiencies than all other compounds studied – which is probably caused by the fact that they were used as bromides. Bromides are commonly found to be more active than compounds with other counterions.

10

The formation of primary and secondary lysosomes in Balantidium coli, Ciliata

72%

Skotarczak B.

Folia Histochemica et Cytobiologica

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1999

|

tom 37

|

nr 4

11

Lysosomal high molecular weight multienzyme complex

72%

Ostrowska H., Krukowska K., Kalinowska J., Orlowska M., Lengiewicz I.

Cellular and Molecular Biology Letters

|

2003

|

tom 08

|

nr 1

Three acidic glycosidases: β-galactosidase (β-GAL, EC 3.2.1.23), α-neuraminidase (NEUR, sialidase, EC 3.2.1.18), N-acetylaminogalacto-6-sulfate sulfatase (GALNS, EC 3.1.6.4) and serine carboxypepidase cathepsin A (EC 3.4.16.1) form a functional high molecular weight complex in the lysosomes. The major constituent of this complex is cathepsin A, the so-called “lysosomal protective protein” (PPCA). By forming a multienzyme complex, it protects the glycosidases from rapid intralysosomal proteolysis, and it is also required for the intracellular sorting and proteolytic processing of their precursors. In man, a deficiency of cathepsin A leads to a combined deficiency of β-GAL and NEUR activities, called “galactosialidosis”. Multiple mutations identified in the cathepsin A gene are the molecular basis of this lysosomal storage disease. This review describes the structural organization of the lysosomal high molecular weight multienzyme complex and the importance of the protective protein/cathepsin A in physiology and pathology.

12

Macroautophagic process was differentially modulated by long-term moderate exercise in rat brain and peripheral tissues

58%

Bayod S., Del Valle J., Pelegri C., Vilaplana J., Canudas A. M., Camins A., Jimenez A., Sanchez-Roige S., Lalanza J. F., Esorihuela R. M., Pallas M.

Journal of Physiology and Pharmacology

|

2014

|

tom 65

|

nr 2

13

Strong association between fibronectin accumulation and lowered cathepsin B activity in glomeruli of diabetic rats

58%

Wyczalkowska-Tomasik A., Bartolomiejczyk I., Gornicka B., Paczek L.

Journal of Physiology and Pharmacology

|

2012

|

tom 63

|

nr 5

14

Characteristics of weak base-induced vacuoles formed around individual acidic organelles

58%

Hiruma H., Kawakami T.

Folia Histochemica et Cytobiologica

|

2011

|

tom 49

|

nr 2

15

Specificity of Sertoli cells in isopods: the case Saduria entomon L.

58%

Gabala E.

Acta Biologica Cracoviensia. Series Botanica et Zoologia. Supplement

|

1997

|

tom 39

|

nr 1

16

Fluorogenic peptide substrates for carboxydipeptidase activity of cathepsin B

58%

Stachowiak K., Tokmina M., Karpinska A., Sosnowska R., Wiczk W.

Acta Biochimica Polonica

|

2004

|

tom 51

|

nr 1

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-FE(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.

17

Morphological and histochemical evidence for iron storage in the hindgut of Porcellio scaber Latr. [Crustacea, Isopoda]

51%

Liberkowska M., Gabala E.

Biological Bulletin of Poznań

|

1994

|

tom 31

18

Artykuł dostępny w postaci pełnego tekstu - kliknij by otworzyć plik

Muscle cathepsins of marine fish and invertebrates

44%

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

Lysosomal acid phosphatase activity and progesterone secretion by porcine corpora lutea at various periods of the luteal phase

The lysosomal cell complex as a stress response indicator

A lysosomal high molecular weight multienzyme complex

Effect of reduced glutathione [GSH] on activity of lysosomal system in subcellular fractions of mouse kidney

The activation and inactivation of lysosomal and extralysosomal compartments - a simple general model

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

Effects of paclitaxel on lysosomal enzyme activity and ultrastructure of mouse liver cells

The lysosomal apparatus of peripheral blood lymphocytes reactivity in bursectomized or thymectomized chickens, after lipopolysaccharide E.coli [LPS] administration

Assessment of biological activity of new compounds designated to act as lysosomotropes

The formation of primary and secondary lysosomes in Balantidium coli, Ciliata

Lysosomal high molecular weight multienzyme complex

Macroautophagic process was differentially modulated by long-term moderate exercise in rat brain and peripheral tissues

Strong association between fibronectin accumulation and lowered cathepsin B activity in glomeruli of diabetic rats

Characteristics of weak base-induced vacuoles formed around individual acidic organelles

Specificity of Sertoli cells in isopods: the case Saduria entomon L.

Fluorogenic peptide substrates for carboxydipeptidase activity of cathepsin B

Morphological and histochemical evidence for iron storage in the hindgut of Porcellio scaber Latr. [Crustacea, Isopoda]

Muscle cathepsins of marine fish and invertebrates