Wyniki wyszukiwania

1

Activity of mi and m-calpain in regenerating fast and slow twitch skeletal muscle

100%

Moraczewski J., Piekarska E., Zimowska M., Sobolewska M.

Acta Biochimica Polonica

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1996

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tom 43

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nr 4

Calpains — non-lysosomal intracellular calcium-activated neutral proteinases, form a family consisting of several distinct members. Two of the isoenzymes: ji (calpain I) and m (calpain II) responded differently to the injury during complete regeneration of Extensor digitorum longus (EDL) muscle and partial regeneration of Soleus muscle. In the crushed EDL the level of m-calpain on the 3rd and 7th day of regeneration was higher than in non-operated muscles, whereas the activity of this calpain in injured Soleus decreased. The level of n-calpain in EDL oscillated irregularly during regeneration whereas in Soleus of both injured and contralateral muscles its level rapidly rose. Our results support the hypothesis that m-calpain is involved in the process of fusion of myogenic cells whereas u-calpain plays a significant but indirect role in muscle regeneration.

2

Large-conductance K+ channel openers induce death of human glioma cells

86%

Debska-Vielhaber G., Godlewski M. M., Kicinska A., Skalska J., Kulawiak B., Piwonska M., Zablocki K., Kunz W. S., Szewczyk A., Motyl T.

Journal of Physiology and Pharmacology

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2009

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tom 60

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nr 4

27-36

Large-conductance Ca2+-activated K+ channels (BKCa channels) are highly expressed in human glioma cells. It has been reported that BKCa channels are present in the inner mitochondrial membrane of the human glioma cell line LN229. In the present study we investigated whether BKCa-channel openers, such as CGS7181 (ethyl 2-hydroxy-1-[[(4-methylphenyl)amino]oxo]-6-trifluoromethyl-1H-indole-3-carboxylate) and CGS7184 (ethyl 1-[[(4-chlorophenyl) amino]oxo]-2-hydroxy-6-trifluoromethyl-1H-indole-3-carboxylate), affect the functioning of LN229 glioma cell mitochondria in situ. In the micromolar concentration range CGS7181 and CGS7184 induced glioma cell death. Morphological and cytometric analyses confirmed that both substances trigger the glioma cell death. This effect was not inhibited by the pan-caspase inhibitor z-VAD-fmk. Lack of DNA laddering, PARP cleavage, and caspase 3 activation suggested that glioma cell death was not of the apoptotic type. We examined the effect of CGS7184 on mitochondrial membrane potential and mitochondrial respiration. Potassium channel opener CGS7184 increased cell respiration and induced mitochondrial membrane depolarization. The latter was dependent on the presence of Ca2+ in the external medium. It was shown that CGS7184 induced an increase of cytosolic Ca2+ concentration due to endoplasmic reticulum store depletion. In conclusion, our results show that CGS7181 and CGS7184 induce glioma cell death by increasing the cytosolic calcium concentration followed by activation of calpains.

3

Bovine my-calpain [CAPN1] gene: new SNP within intron 14

86%

Juszczuk-Kubiak E., Sakowski T., Flisikowski K., Wicinska K., Oprzadek J., Rosochacki S. J.

Journal of Applied Genetics

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2004

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tom 45

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nr 4

4

Caspase and calpain mediated proteolysis of nonerythroid spectrin subunits in neuronal cells undergoing apaptosis

86%

Wang K. K. W., Rathna N., Rand P., McGinnis K., Glantz S. B., Morrow J. S.

Cellular and Molecular Biology Letters

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1998

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tom 03

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nr 2

5

Inhibition of calpain but not caspase activity by spectrin fragments

72%

Rolius R., Antoniou C., Nazarova L. A., Kim S. H., Cobb G., Gala P., Rajaram P., Li Q., Fung L. W.-M.

Cellular and Molecular Biology Letters

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2010

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tom 15

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nr 3

395-405

Calpains and caspases are ubiquitous cysteine proteases that are associated with a variety of cellular pathways. Calpains are involved in processes such as long term potentiation, cell motility and apoptosis, and have been shown to cleave non-erythroid (brain) α- and β-spectrin and erythroid β-spectrin. The cleavage of erythroid α-spectrin by calpain has not been reported. Caspases play an important role in the initiation and execution of apoptosis, and have been shown to cleave non-erythroid but not erythroid spectrin. We have studied the effect of spectrin fragments on calpain and caspase activities. The erythroid and non-erythroid spectrin fragments used were from the N-terminal region of α-spectrin, and C-terminal region of β-spectrin, both consisting of regions involved in spectrin tetramer formation. We observed that the all spectrin fragments exhibited a concentration-dependent inhibitory effect on calpain, but not caspase activity. It is clear that additional studies are warranted to determine the physiological significance of calpain inhibition by spectrin fragments. Our findings suggest that calpain activity is modulated by the presence of spectrin partial domains at the tetramerization site. It is not clear whether the inhibitory effect is substrate specific or is a general effect. Further studies of this inhibitory effect may lead to the identification and development of new therapeutic agents specifically for calpains, but not for caspases. Proteins/peptides with a coiled coil helical conformation should be studied for potential inhibitory effects on calpain activity.

6

Relationships between calpains and glutamateor kainate-induced apoptosis in Xenopus laevis tadpoles

72%

Brun C., Moudilou E., Bouchot C., Abrouk-Verot L., Exbrayat J.-M.

Folia Histochemica et Cytobiologica

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2013

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tom 51

|

nr 4

7

A note on restriction fragment length polymorphism for HhaI in the bovine calpain gene

72%

Juszczuk-Kubiak E., Rosochacki S. J., Wicinska K.

Animal Science Papers and Reports

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2002

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tom 20

|

nr 3

8

Myocardial necrosis due to vitamin D3 overdose - scanning electron microscopic observations

72%

Walentynowicz O., Kubasik-Juraniec J., Rudzinska-Kisiel T.

Folia Morphologica

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2004

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tom 63

|

nr 4

Our studies were carried out on the hearts of virgin female Wistar rats treated with 100.000 i.u. of vitamin D₃ (calciol) per os for 3 consecutive days. Multifocal cardionecrosis was established macroscopically in 70% of the vitamin D-treated rats on the 7th day of the experiment when the rats were in the acute phase of intoxication. Using a scanning electron microscopy (SEM), we received three-dimensional information about the structural changes to the rat myocardium damaged by high doses of vitamin D₃. The images of necrotic hearts revealed significant disruption of the structural integrity of the myocardium linked to fragmentation of the cardiac muscle bundles and a visible disruption of the extracellular matrix (ECM) components. In healthy hearts, the structural integrity of the myocardium and the dense network of the extracellular matrix were well preserved. In parallel, the effect of an increasing concentration of free Ca²⁺ on the total proteolytic activity of the heart muscle homogenate of the healthy and necrotic rats was investigated at neutral pH. These data showed that following vitamin D₃ intoxication, the proteolytic processes in the rat hearts occurred in Ca²⁺ overload or saturation. On the basis of our morphological and biochemical results we can suggest that calcium-activated neutral proteinases may have contributed to the structural alteration of the extracellular matrix components and were in this way involved in vitamin D-induced cardionecrosis.

9

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

72%

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

|

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.

10

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Rola kalpain w procesie kruszenia miesa

58%

Nowak M.

Żywność Nauka Technologia Jakość

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2005

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tom 12

|

nr 1

5-17

Kruchość mięsa oraz czynniki na nią wpływające od dawna są przedmiotem badań. Istnieje kilka teorii wyjaśniających proces kruszenia mięsa. Za najbardziej prawdopodobną uznana została kalpainowa teoria tenderyzacji. Kalpainy spełniają podstawowe kryteria stawiane czynnikom wpływającym na proces kruszenia mięsa. Enzymy te są obecne w komórce mięśniowej, a w doświadczeniach przeprowadzanych in vitro prowadzą do tych samych produktów degradacji białek, jakie wykrywane są w mięsie po okresie dojrzewania. Mają one dostęp do miofibryli w komórce. Aktywność kalpain oraz stosunek aktywności kalpainy do aktywnocśi kalpastatyny są skorelowane z twardością mięsa. Im wyższa jest aktywność kalpain i im wyższy stosunek kalpaina/kalpastatyna, tym bardziej kruche mięso otrzymuje się. Warunki w jakich enzymy te wykazują aktywności zbliżone do warunków panujących w tkance mięśniowej po śmierci zwierzęcia. Na aktywność kalpain w mięsie działają zarówno czynniki przyżyciowe, w tym genetyczne, jak i pośmiertne. Mimo, że mechanizm działania kalpain nie jest całkowicie wyjaśniony, na podstawie wyników licznych doświadczeń można stwierdzić, że kalpainy pełnią ważną rolę w procesie tenderyzacji mięsa. W artykule scharakteryzowano kalpainy i opisano niektóre z czynników wpływających na ich aktywność.

11

Ex vivo measurement of calpain activation in human peripheral blood lymphocytes by detection of immunoreactive products of calpastatin degradation

58%

Mikosik A., Zaremba A., Puchalska Z., Daca A., Smolenska Z., Lopatniuk P., Mital A., Hellmann A., Bryl E., Witkowski J. M.

Folia Histochemica et Cytobiologica

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2007

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tom 45

|

nr 4

343-347

12

Conventional calpains and programmed cell death

58%

Lopatniuk P., Witkowski J. M.

Acta Biochimica Polonica

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2011

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tom 58

|

nr 3

The evidence on the crucial role of a family of calcium-dependent cysteine proteases called calpains in programmed cell death is rich and still growing. However, understanding of the mechanisms of their functions in apoptosis is not full yet. Calpains have been implicated in both physiological and pathological cell death control, especially in various malignancies, but also in the immune system development and function. There is also growing evidence on calpain involvement in apoptosis execution in certain pathological conditions of the central nervous system, in cardiovascular diseases, etc. Understanding of the clinical significance of calpain activation pathways, after intense studies of the influence of calpain activity on drug-induced apoptosis, seems especially important lately, as calpains have become noticed as potential therapeutic targets. To allow pharmacological targeting of these enzymes, thorough knowledge of their patterns of activation and further interactions with already known apoptotic pathways is necessary. A comprehensive summary of both well established and recently obtained information in the field is an important step that may lead to future advances in the use of calpain-targeted agents in the clinic.

13

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

58%

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

Polish Journal of Veterinary Sciences

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2001

|

tom 04

|

nr 2

14

Enzyme activity in pig meat of different meatiness

58%

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

Annals of Animal Science. Supplement

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2002

|

nr 2

15

Phosphorylation of protein kinase C substrate proteins in rat hippocampal slices-effect of calpain inhibition

58%

Domanska-Janik K., Zablocka B., Zalewska T., Zajac H.

Acta Neurobiologiae Experimentalis

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1998

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tom 58

|

nr 4

Ograniczanie wyników

Activity of mi and m-calpain in regenerating fast and slow twitch skeletal muscle

Large-conductance K+ channel openers induce death of human glioma cells

Bovine my-calpain [CAPN1] gene: new SNP within intron 14

Caspase and calpain mediated proteolysis of nonerythroid spectrin subunits in neuronal cells undergoing apaptosis

Inhibition of calpain but not caspase activity by spectrin fragments

Relationships between calpains and glutamateor kainate-induced apoptosis in Xenopus laevis tadpoles

A note on restriction fragment length polymorphism for HhaI in the bovine calpain gene

Myocardial necrosis due to vitamin D3 overdose - scanning electron microscopic observations

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

Rola kalpain w procesie kruszenia miesa

Ex vivo measurement of calpain activation in human peripheral blood lymphocytes by detection of immunoreactive products of calpastatin degradation

Conventional calpains and programmed cell death

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

Enzyme activity in pig meat of different meatiness

Phosphorylation of protein kinase C substrate proteins in rat hippocampal slices-effect of calpain inhibition