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Wyświetlanie 1-15 z 27
Tytuł:
Store-operated calcium entry in physiology and pathology of mammalian cells
Autorzy:
Targos, Berenika
Barań0ska, Jolanta
Pomorski, Paweł
Powiązania:
https://bibliotekanauki.pl/articles/1041419.pdf
Data publikacji:
2005
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
store-operated calcium entry
store-operated channels
calcium stores
calcium signaling
Opis:
One of the numerous calcium-involving processes in mammalian cells is store-operated calcium entry (SOCE) - the process in which depletion of calcium stores in the endoplasmic reticulum (ER) induces calcium influx from the extracellular space. Previously supposed to function only in non-excitable cells, SOCE is now known to play a role also in such excitable cells as neurons, muscles and neuroendocrine cells and is found in many different cell types. SOCE participates not only in processes dependent on ER calcium level but also specifically regulates some important processes such as cAMP production, T lymphocyte activation or induction of long-term potentiation. Impairment of SOCE can be an element of numerous disorders such as acute pancreatitis, primary immunodeficiency and, since it can take part in apoptosis or cell cycle regulation, SOCE may also be partially responsible for such serious disorders as Alzheimer disease and many types of cancer. Even disturbances in the 'servant' role of maintaining ER calcium level may cause serious effects because they can lead to ER homeostasis disturbance, influencing gene expression, protein synthesis and processing, and the cell cycle.
Źródło:
Acta Biochimica Polonica; 2005, 52, 2; 397-409
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The network of calcium regulation in muscle.
Autorzy:
Martonosi, Anthony
Pikula, Slawomir
Powiązania:
https://bibliotekanauki.pl/articles/1043643.pdf
Data publikacji:
2003
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
sodium:calcium exchanger
calcium pump
calcium homeostasis
calcium channel
skeletal and cardiac muscles
mitochondria
sarcoplasmic reticulum
excitation-contraction coupling
Opis:
In this review the molecular characteristics and reaction mechanisms of different Ca2+ transport systems associated with various membranes in muscle cells will be summarized. The following topics will be discussed in detail: a brief history of early observations concerning maintenance and regulation of cellular Ca2+ homeostasis, characterization of the Ca2+ pumps residing in plasma membranes and sarco(endo)plasmic reticulum, mitochondrial Ca2+ transport, Ca2+-binding proteins, coordinated expression of Ca2+ transport systems, a general background of muscle excitation-contraction coupling with emphasis to the calcium release channels of plasma membrane and sarcoplasmic reticulum, the structure and function of dihydropyridine and ryanodine receptors of skeletal and cardiac muscles, and finally their disposition in various types of muscles.
Źródło:
Acta Biochimica Polonica; 2003, 50, 1; 1-30
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
The structure of the Ca2+-ATPase of sarcoplasmic reticulum.
Autorzy:
Martonosi, Anthony
Pikula, Slawomir
Powiązania:
https://bibliotekanauki.pl/articles/1043610.pdf
Data publikacji:
2003
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
calcium pump
calcium homeostasis
calcium transport
skeletal and cardiac muscles
sarcoplasmic reticulum
excitation-contraction coupling
Opis:
In this article the morphology of sarcoplasmic reticulum, classification of Ca2+-ATPase (SERCA) isoenzymes presented in this membrane system, as well as their topology will be reviewed. The focus is on the structure and interactions of Ca2+-ATPase determined by electron and X-ray crystallography, lamellar X-ray and neutron diffraction analysis of the profile structure of Ca2+-ATPase in sarcoplasmic reticulum multilayers. In addition, targeting of the Ca2+-ATPase to the sarcoplasmic reticulum is discussed.
Źródło:
Acta Biochimica Polonica; 2003, 50, 2; 337-365
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
A novel member of the thermolysin family, cloning and biochemical characterization of metalloprotease from Staphylococcus pseudintermedius
Autorzy:
Wladyka, Benedykt
Bista, Michal
Sabat, Artur
Bonar, Emilia
Grzeszczuk, Sabina
Hryniewicz, Waleria
Dubin, Adam
Powiązania:
https://bibliotekanauki.pl/articles/1040710.pdf
Data publikacji:
2008
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
staphylococcus
calcium
metalloprotease
pathogen
Opis:
Thermolysins constitute a family of secreted bacterial metalloproteases expressed, among others, by several pathogens. Strains of Staphylococcus pseudintermedius isolated from diseased dogs and judged as protease-positive, by skim milk agar plate culture, were investigated for protease content. No proteolytic activity was detected when the bacteria were grown in regular liquid media. Unexpectedly, supplementation of the medium with calcium ions resulted in expression of a metalloprotease and profound changes in the profile of extracellular proteins. On the basis of homology to other staphylococcal metalloproteases, the nucleotide sequence of the gene encoding this protease (Pst) and its flanking regions was determined. The full-length pst codes for a protein with an open reading frame of 505 amino acids. The internal region contains the HEXXH catalytic domain that is conserved in members of the thermolysin family. Regardless of the presence of calcium in the medium, the expression of the protease gene was of the same intensity. This suggests that regulation of the metalloprotease production by calcium ions is at a post-transcriptional level. Isolates of S. pseudintermedius exhibit a proteolytic phenotype due to the metalloprotease expression, however only in presence of calcium ions, which most probably stabilize the structure of the protease.
Źródło:
Acta Biochimica Polonica; 2008, 55, 3; 525-536
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Regulation of Ca2+ release from internal stores in cardiac and skeletal muscles.
Autorzy:
Wrzosek, Antoni
Powiązania:
https://bibliotekanauki.pl/articles/1044313.pdf
Data publikacji:
2000
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
Ca2+-induced Ca2+ release
calcium channels
dihydropyridine receptor
calcium sparks
excitation-contraction coupling
ryanodine receptor
Opis:
It is widely accepted that Ca2+ is released from the sarcoplasmic reticulum by a specialized type of calcium channel, i.e., ryanodine receptor, by the process of Ca2+-induced Ca2+ release. This process is triggered mainly by dihydropyridine receptors, i.e., L-type (long lasting) calcium channels, directly or indirectly interacting with ryanodine receptor. In addition, multiple endogenous and exogenous compounds were found to modulate the activity of both types of calcium channels, ryanodine and dihydropyridine receptors. These compounds, by changing the Ca2+ transport activity of these channels, are able to influence intracellular Ca2+ homeostasis. As a result not only the overall Ca2+ concentration becomes affected but also spatial distribution of this ion in the cell. In cardiac and skeletal muscles the release of Ca2+ from internal stores is triggered by the same transport proteins, although by their specific isoforms. Concomitantly, heart and skeletal muscle specific regulatory mechanisms are different.
Źródło:
Acta Biochimica Polonica; 2000, 47, 3; 705-723
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Toxicological and cytophysiological aspects of lanthanides action.
Autorzy:
Pałasz, Artur
Czekaj, Piotr
Powiązania:
https://bibliotekanauki.pl/articles/1044234.pdf
Data publikacji:
2000
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
gadolinium
cytochrome P450.
calcium
lanthanides
metals
Opis:
Lanthanides, also called rare-earth elements, are an interesting group of 15 chemically active, mainly trivalent, f-electronic, silvery-white metals. In fact, lanthanides are not as rare as the name implies, except for promethium, a radioactive artificial element not found in nature. The mean concentrations of lanthanides in the earth's crust are comparable to those of life-important elements like iodine, cobalt and selenium. Many lanthanide compounds show particular magnetic, catalytic and optic properties, and that is why their technical applications are so extensive. Numerous industrial sources enable lanthanides to penetrate into the human body and therefore detailed toxicological studies of these metals are necessary. In the liver, gadolinium selectively inhibits secretion by Kupffer cells and it decreases cytochrome P450 activity in hepatocytes, thereby protecting liver cells against toxic products of xenobiotic biotransformation. Praseodymium ion (Pr3+) produces the same protective effect in liver tissue cultures. Cytophysiological effects of lanthanides appear to result from the similarity of their cationic radii to the size of Ca2+ ions. Trivalent lanthanide ions, especially La3+ and Gd3+, block different calcium channels in human and animal cells. Lanthanides can affect numerous enzymes: Dy3+ and La3+ block Ca2+-ATPase and Mg2+-ATPase, while Eu3+ and Tb3+ inhibit calcineurin. In neurons, lanthanide ions regulate the transport and release of synaptic transmitters and block some membrane receptors, e.g. GABA and glutamate receptors. It is likely that lanthanides significantly and uniquely affect biochemical pathways, thus altering physiological processes in the tissues of humans and animals.
Źródło:
Acta Biochimica Polonica; 2000, 47, 4; 1107-1114
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Smooth muscle actomyosin promotes Ca2+-dependent interactions between annexin VI and detergent-insoluble glycosphingolipid-enriched membrane domains.
Autorzy:
Babiychuk, Victoria
Draeger, Annette
Babiychuk, Eduard
Powiązania:
https://bibliotekanauki.pl/articles/1044291.pdf
Data publikacji:
2000
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
annexins
calcium
rafts
smooth muscle
cell membrane
Opis:
The mechanical link coupling cytoskeletal and contractile proteins to the sarcolemma of smooth muscle cells is essential for transmitting tension from the cell's interior to exterior. In addition to the well-characterized actin-integrin associations present in adhaerens junctions, our recent work has postulated the existence of a reversible annexin-dependent membrane-cytoskeleton complex, forged in response to a rise in intracellular Ca2+ concentration following smooth muscle cell stimulation (Babiychuk et al., J. Biol Chem. 1999, 274, 35191-35195). Detailed biochemical characterization of the interactions responsible for the formation of this complex revealed that annexins II and VI interact with actomyosin, or detergent-insoluble glycosphingolipid-enriched membrane domains (rafts) purified from smooth muscle, in a concentration- and Ca2+-dependent manner. Annexin II interacted with lipid rafts with high Ca2+-sensitivity, while for annexin VI this interaction required non-physiologically high concentrations of free Ca2+. However, the Ca2+-sensitivity of the latter interaction strongly increased in the presence of purified smooth muscle actomyosin. The detailed biochemical analysis of the interactions occurring between annexin II, annexin VI, actomyosin and rafts suggests that annexins regulate sarcolemmal organization during smooth muscle cell contraction.
Źródło:
Acta Biochimica Polonica; 2000, 47, 3; 579-589
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Studies on sintering process of synthetic hydroxyapatite
Autorzy:
Malina, Dagmara
Biernat, Kamila
Sobczak-Kupiec, Agnieszka
Powiązania:
https://bibliotekanauki.pl/articles/1039506.pdf
Data publikacji:
2013
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
calcium phosphates
hydroxyapatite
sintering process
wet synthesis
Opis:
In this study the effect of sintering process in different temperatures on microstructure and morphological properties of sintered hydroxyapatite (HAp) was investigated. HAp powder was prepared by wet precipitation method from following reagents: Ca(OH)2 + H3PO4 in an alkaline conditions. Thermal analysis (TA), X-Ray diffraction method (XRD), FT-IR spectrometry (FT-IR) and scanning electron microscopy (SEM) were used to elaborate the phase composition and properties of sintered HAp samples and raw HAp powder as well. The total and apparent density and total porosity of sintered compacts, shrinkage and weight loss during the sintering were also measured. The results show that there is a difference in sintering behavior of synthetic hydroxyapatites depending on sintering temperature. The main differences refer to the loss of mass, shrinkage, changes in porosity and density of the investigated materials.
Źródło:
Acta Biochimica Polonica; 2013, 60, 4; 851-855
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Conformational destabilization of Bacillus licheniformis α-amylase induced by lysine modification and calcium depletion
Autorzy:
Tan, Cheau
Rahman, Raja
Kadir, Habsah
Tayyab, Saad
Powiązania:
https://bibliotekanauki.pl/articles/1039896.pdf
Data publikacji:
2011
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
salt bridges
urea
BLA
calcium
lysine
stability
conformation
Opis:
Bacillus licheniformis α-amylase (BLA) was chemically modified using 100-fold molar excess of succinic anhydride over protein or 0.66 M potassium cyanate to obtain 42 % succinylated and 81 % carbamylated BLAs. Size and charge homogeneity of modified preparations was established by Sephacryl S-200 HR gel chromatography and polyacrylamide gel electrophoresis. Conformational alteration in these preparations was evident by the larger Stokes radii (3.40 nm for carbamylated and 3.34 nm for succinylated BLAs) compared to 2.43 nm obtained for native BLA. Urea denaturation results using mean residue ellipticity (MRE) as a probe also showed conformational destabilization based on the early start of transition as well as ΔGDH2O values obtained for both modified derivatives and Ca-depleted BLA. Decrease in ΔGDH2O value from 5,930 cal/mol (for native BLA) to 3,957 cal/mol (for succinylated BLA), 3,336 cal/mol (for carbamylated BLA) and 3,430 cal/mol for Ca-depleted BLA suggested reduced conformational stability upon modification of amino groups of BLA or depletion of calcium. Since both succinylation and carbamylation reactions abolish the positive charge on amino groups (both α- and ε- amino), the decrease in conformational stability can be ascribed to the disruption of salt bridges present in the protein which might have released the intrinsic calcium from its binding site.
Źródło:
Acta Biochimica Polonica; 2011, 58, 3; 405-412
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Is MLC phosphorylation essential for the recovery from ROCK inhibition in glioma C6 cells?
Autorzy:
Korczyński, Jarosław
Sobierajska, Katarzyna
Krzemiński, Patryk
Wasik, Anna
Wypych, Dorota
Pomorski, Paweł
Kłopocka, Wanda
Powiązania:
https://bibliotekanauki.pl/articles/1039964.pdf
Data publikacji:
2011
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
RhoA
myosin II
calcium signaling
actin
MLC phosphorylation
Opis:
Inhibition of Rho-associated protein kinase (ROCK) activity in glioma C6 cells induces changes in actin cytoskeleton organization and cell morphology similar to those observed in other types of cells with inhibited RhoA/ROCK signaling pathway. We show that phosphorylation of myosin light chains (MLC) induced by P2Y2 receptor stimulation in cells with blocked ROCK correlates in time with actin cytoskeleton reorganization, F-actin redistribution and stress fibers assembly followed by recovery of normal cell morphology. Presented results indicate that myosin light-chain kinase (MLCK) is responsible for the observed phosphorylation of MLC. We also found that the changes induced by P2Y2 stimulation in actin cytoskeleton dynamics and morphology of cells with inhibited ROCK, but not in the level of phosphorylated MLC, depend on the presence of calcium in the cell environment.
Źródło:
Acta Biochimica Polonica; 2011, 58, 1; 125-130
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Environmental parameters conditioning microbially induced mineralization under the experimental model conditions
Autorzy:
Otlewska, Anna
Gutarowska, Beata
Powiązania:
https://bibliotekanauki.pl/articles/1038825.pdf
Data publikacji:
2016
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
microbially induced mineralization
calcium carbonate
abiotic factors
urease
Opis:
Microbially induced calcium carbonate precipitation is one of the biomineralization types closely dependent on the parameters of the microenvironment. Minerals are precipitated as a product of environmental and bacterial cell interactions, however, this system has very little control via microorganisms. The aim of research was to determine the influence of abiotic factors (pH, temperature, agitation speed of bacterial culture and calcium ion source) on the mineralization induced by Arthrobacter sulfureus, Bacillus muralis and B. atrophaeus strains under the standard laboratory conditions. Because of the key role of urease in biomineralization, processes occurring in environments with and without the urea were compared. For this purpose, cultivation of bacteria (A. sulfureus, B. muralis and B. atrophaeus) was carried out in B4 liquid medium for 5 days with various environmental parameters (pH 6-9; temperature 25-44°C; speed of agitation 0-180 rpm, different calcium sources). It was noticed that the pH and the speed of agitation clearly affect the amount of the calcium carbonate that formed. Our observations suggest that the highest precipitation rate takes place in alkaline pH between 8-9, with shaking at 180 rpms. Among studied sources of calcium ions (calcium acetate, calcium chloride and calcium nitrate), calcium acetate demonstrated the strongest potential in the biomineralization process. Moreover, work presented here demonstrates that the correlation between cultivation temperature and biomineralization process cannot be clearly evaluated. The morphology and size of calcium carbonate minerals was strain-specific, although affected by the presence of urea in the surrounding solution.
Źródło:
Acta Biochimica Polonica; 2016, 63, 2; 343-351
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Effect of Rho-associated kinase inhibition on actin cytoskeleton structure and calcium response in glioma C6 cells
Autorzy:
Targos, Berenika
Pomorski, Paweł
Krzemiński, Patryk
Barańska, Jolanta
Rędowicz, Maria
Kłopocka, Wanda
Powiązania:
https://bibliotekanauki.pl/articles/1041182.pdf
Data publikacji:
2006
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
glioma C6
actin cytoskeleton
RhoA
ROCK
calcium transients
Opis:
The role of actin cytoskeleton functional state in glioma C6 cell morphology and calcium signaling was investigated through modification of myosin II activity by blocking Rho-associated kinase with the specific inhibitor Y-27632. Treatment of glioma C6 cells with ROCK inhibitor resulted in actin cytoskeleton reorganization and also in the changed shape and distribution of mitochondria. Changes in the distribution of ER, the main calcium store in glioma C6 cells, were not visible. The inhibition of myosin II activity influences the first phase of calcium signaling evoked by agonist, and both phases of thapsigargin-evoked calcium response. We suggest that the observed increase in Ca2+ release from intracellular stores induced by IP3 formation as well as inhibition of SERCA ATPase is at least in part related to severely affected mitochondria. Enhancement of capacitative calcium entry evoked by thapsigargin is probably associated with the reorganization of the acto-myosin II system. ATP-induced calcium response presents no changes in the second phase. We observed that ATP stimulation of Y-27632 pretreated cells leads to immediate morphological rearrangement of glioma C6 cells. It is a consequence of actin cytoskeleton reorganization: formation of stress fibers and relocation of phosphorylated myosin II to actin filaments. It seems that the agonist-evoked strong calcium signal may be sufficient for myosin II activation and the stress fiber organization. This is the first work showing the dependence between the functional state of the acto-myosin II system and calcium signaling stressing the reversible character of this relationship.
Źródło:
Acta Biochimica Polonica; 2006, 53, 4; 825-831
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Regulation of subcellular localization of muscle FBPase in cardiomyocytes. The decisive role of calcium ions
Autorzy:
Majkowski, Michal
Wypych, Dorota
Pomorski, Pawel
Dzugaj, Andrzej
Powiązania:
https://bibliotekanauki.pl/articles/1042732.pdf
Data publikacji:
2010
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
cardiomyocytes
Z-line
insulin
calcium
intercalated disc
muscle FBPase
Opis:
Glyconeogenesis, the synthesis of glycogen from carbohydrate precursors like lactate, seems to be an important pathway participating in replenishing glycogen in cardiomyocytes. Fructose-1,6-bisphosphatase (FBPase), an indispensible enzyme of glyconeogenesis, has been found in cardiomyocytes on the Z-line, in the nuclei and in the intercalated discs. Glyconeogenesis may proceed only when FBPase accumulates on the Z-line. Searching for the mechanism of a FBPase regulation we investigated the effects of the calcium ionophore A23187, a muscle relaxant dantrolene, glucagon, insulin and medium without glucose on the subcellular localization of this enzyme in primary culture of neonatal rat cardiomyocytes. Immunofluorescence was used for protein localization and the intracellular calcium concentration was measured with Fura. We found that the concentration of calcium ions was the decisive factor determining the localization of muscle FBPase on the Z-line. Calcium ions had no effect on the localization of the enzyme in the intercalated discs or in the nuclei, but accumulation of FBPase in the nuclei was induced by insulin.
Źródło:
Acta Biochimica Polonica; 2010, 57, 4; 597-605
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Ca2+differently affects hydrophobic properties of guanylyl cyclase-activating proteins (GCAPs) and recoverin.
Autorzy:
Gorczyca, Wojciech
Kobiałka, Marcin
Kuropatwa, Marianna
Kurowska, Ewa
Powiązania:
https://bibliotekanauki.pl/articles/1043612.pdf
Data publikacji:
2003
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
fluorescence
calcium-binding proteins
recoverin
guanylyl cyclase-activating proteins
Opis:
Guanylyl cyclase-activating proteins (GCAPs) and recoverin are retina-specific Ca2+-binding proteins involved in phototransduction. We provide here evidence that in spite of structural similarities GCAPs and recoverin differently change their overall hydrophobic properties in response to Ca2+. Using native bovine GCAP1, GCAP2 and recoverin we show that: i) the Ca2+-dependent binding of recoverin to Phenyl-Sepharose is distinct from such interactions of GCAPs; ii) fluorescence intensity of 1-anilinonaphthalene-8-sulfonate (ANS) is markedly higher at high [Ca2+]gfree (10 μM) than at low [Ca2+]free (10 nM) in the presence of recoverin, while an opposing effect is observed in the presence of GCAPs; iii) fluorescence resonance energy transfer from tryptophane residues to ANS is more efficient at high [Ca2+]free in recoverin and at low [Ca2+]free in GCAP2. Such different changes of hydrophobicity evoked by Ca2+ appear to be the precondition for possible mechanisms by which GCAPs and recoverin control the activities of their target enzymes.
Źródło:
Acta Biochimica Polonica; 2003, 50, 2; 367-376
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Plasma membrane Ca2+ -ATPase in excitable and nonexcitable cells.
Autorzy:
Żylińska, Ludmiła
Soszyński, Mirosław
Powiązania:
https://bibliotekanauki.pl/articles/1044284.pdf
Data publikacji:
2000
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
calcium homeostasis
brain
erythrocytes
plasma membrane Ca2+ -ATPase
Opis:
There is a significant number of data confirming that the maintenance of calcium homeostasis in a living cell is a complex, multiregulated process. Calcium efflux from excitable cells (i.e., neurons) occurs through two main systems - an electrochemically driven Na+/Ca2+ exchanger with a low Ca2+ affinity (K0.5 = 10-15 μM), and a plasmalemmal, specific Ca2+-ATPase, with a high Ca2+ affinity (K0.5 < 0.5-1 μM), whereas in nonexcitable cells (i.e., erythrocytes) the calcium pump is the sole system responsible for the extrusion of calcium ions. The plasma membrane Ca2+-ATPase (PMCA) is a ubiquitously expressed protein, and more than 26 transcripts of four PMCA genes are distributed in a tissue specific manner. Differences in the structure and localization of PMCA variants are thought to correlate with specific regulatory properties and may have consequences for proper cellular Ca2+ signaling. The regulatory mechanisms of calcium pump activity have been studied extensively, resulting in a new view of the functioning of this important molecule in the membranes.
Źródło:
Acta Biochimica Polonica; 2000, 47, 3; 529-539
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Wyświetlanie 1-15 z 27

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