Calpain as one of the calcium signal mediators in the cell

Kastrykina, T. F.; Malysheva, M. K.

doi:10.1007/bf02515178

Cited by 5 publications

(5 citation statements)

References 121 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Apparently, this enzyme takes an active part in mediating calcium signals in the cells of different tissues [9][10][11]. Recently, numerous studies showed that calpain plays an essential role in nerve cells (in particular, it is involved in structural and functional reorganization of synapses related to long-term potentiation of synaptic transmission [12]).…”

Section: Introductionmentioning

confidence: 99%

“…Recently, numerous studies showed that calpain plays an essential role in nerve cells (in particular, it is involved in structural and functional reorganization of synapses related to long-term potentiation of synaptic transmission [12]). Changes in the activity of this enzyme seem to be significant factors in various pathologies of the nervous system (Alzheimer's disease, multiple sclerosis, neurotoxicosis, and cerebral ischemia) [10,[13][14][15]. It is suggested that calpain also regulates cell membrane fusion by splitting proteins taking part in this process [16][17][18].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Activity of calpain in subcellular fractions of the rat brain

Kolchinskaya

Malysheva

2004

Neurophysiology

Self Cite

View full text Add to dashboard Cite

We studied the activity of a calcium-dependent proteinase, calpain, in subcellular fractions obtained from rat brain tissue. The rates of calpain-mediated hydrolysis of fluorescein isothiocyanate (FITC)-labeled substrates, casein and fodrin, were comparable; in the former case the rate was higher. This fact stipulated the choice of fluorescent-labeled casein as an adequate substrate. The greatest enzyme activity of calpain (87% of total) was found in the cytoplasmic fraction. At the same time, quite detectable enzyme activities were observed in the investigated membrane fractions obtained from rat brain tissue (coarse mitochondrial fraction, microsomes, and myelin). The highest specific calpain activity was registered in the cytoplasmic fraction. The enzyme activity was efficiently suppressed in the presence of calpain inhibitor I and increased after purification of the preparations from an endogenous calpain inhibitor, calpastatin.

show abstract

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Activity of calpain in subcellular fractions of the rat brain

Kolchinskaya

Malysheva

2004

Neurophysiology

Self Cite

View full text Add to dashboard Cite

show abstract

“…Calpain, an intracellular neutral proteinase that is characterized by absolute dependence of its activity on the concentration of calcium ions, is one of the most important agents responsible for transformation of calcium signals in biochemical and physiological responses of the cell [16,17]. Cytoskeletal and membrane proteins, receptors, hormones, myelin proteins, and many enzymes play the role of substrates of calpain in the cell.…”

Section: Introductionmentioning

confidence: 99%

Age Peculiarities of the Calpain/Calpastatin Cerebral System in Rats: Relation to the Hypothesis of Brain Aging

2009

Self Cite

View full text Add to dashboard Cite

We studied age-related changes in the activity of calpain, those in the activity of its endogenous inhibitor calpastatin, and the ratio of these indices in the brain of rats of four age groups (2-3 weeks, 2-3, 5-6, and 24 months). The activity of calpain was estimated using FITC casein as the substrate. In a soluble fraction of the brain homogenate, the enzyme activity in general increased with age. In mature rats (5 to 6 months old), this index exceeded 3.65 times the corresponding index in juvenile (2 to 3 weeks old) animals, while in old animals this index somewhat decreased. In the fraction obtained after separation of calpain from other components using DEAE-cellulose chromatography, the age-related trend toward an increase in the activity of calpain was preserved, but it was much more moderate. The activity of calpastatin demonstrated an opposite direction of age changes: it was the maximum in 2-3-week-old animals and gradually decreased (by 27%) in old rats. We also found that the efficacy of inhibitory action of calpastatin in the cerebral tissue with respect to the activity of calpain was, as a rule, redundant. In this case, the ratio of inhibitor/enzyme activities decreased with age; this index was 1.65, 1.33, 1.1, and 1.0 or less in 2-3-week-old, 2-month-old, mature, and old animals. Therefore, we found that the intensity of calpain-mediated proteolysis in the rat brain increases from the juvenile period to the mature age and somewhat decreases in old individuals. Such alterations are developed at the expense of both an increase in the activity of the enzyme and weakening of the action of its inhibitor (calpastatin).

show abstract

“…For optimal activity of the enzymes belonging to these subgroups, the corresponding micro-or millimolar concentrations of calcium are necessary. Many studies demonstrated that calpains play important roles in mediation of calcium signalling in cells of various tissues [1][2][3]. Proteins of cytoskeleton, different enzymes (kinases, phosphatases, and phospholipases), and also proteins of membrane receptors and transporters [4] are substrates for the above enzymes.…”

Section: Introductionmentioning

confidence: 99%

“…Calpains are involved in numerous processes that are realized in cells of the nerve tissues under normal conditions (e.g., structural and functional reorganization of synapses related to long-term potentiation of synaptic transmission and the control of neurotransmitter release) [8,9]. Modifications of the activity of calpains are observed in different pathologies of the nervous system (Alzheimer's disease, multiple sclerosis, neurotoxicoses, and cerebral ischemia) [2,[10][11][12]. In recent years, studies are concentrated on the possibility of using inhibitors of calpains for correction of a number of pathological states, including neurological diseases [13,14].…”

Section: Introductionmentioning

confidence: 99%

Effect of Lipids on the Activity of Calpain in Subcellular Fractions Obtained from the Rat Brain

et al. 2009

Self Cite

View full text Add to dashboard Cite

We studied the effect of lipids on the activity of a neutral cysteine proteinase, calpain, in subcellular fractions obtained from the rat brain. Extraction of nearly 23% of membrane cholesterol from the coarse mitochondrial fraction did not result in modifications of specific activity of calpain in this fraction. Detergents (digitonin or Triton Х-100) used in 0.3% concentration enhanced the activity of calpain in the coarse mitochondrial fraction. Examination of the effects of preparations of different phospholipids on the activity of calpain in the cytoplasm demonstrated that only phosphatidylcholine, but not phosphatidylserine and/or cardiolipin, insignificantly increased the activity of calpain (independently of the size and structure of phospholipid vesicles). We hypothesize that the mechanisms underlying interaction between calpain and lipids are not universal; in native cells and model experiments, they can differ noticeably from each other and are modified depending on the corresponding conditions.

show abstract

Calpain as one of the calcium signal mediators in the cell

Cited by 5 publications

References 121 publications

Activity of calpain in subcellular fractions of the rat brain

Activity of calpain in subcellular fractions of the rat brain

Age Peculiarities of the Calpain/Calpastatin Cerebral System in Rats: Relation to the Hypothesis of Brain Aging

Effect of Lipids on the Activity of Calpain in Subcellular Fractions Obtained from the Rat Brain

Contact Info

Product

Resources

About