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1

Badanie szpiku u królika

100%
Mackiewicz U.
Acta Physiologica Polonica
|
1957
|
tom 08
|
nr 4
2
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Content available

Badania nad odczynem bazofilów szpiku kostnego i krwi krążącej u królika po dożylnym wstrzyknięciu heparyny

63%
Labendzinski F., Mackiewicz U.
Acta Physiologica Polonica
|
1958
|
tom 09
|
nr 6
3

Calcium in excitation-contraction coupling of cardiac myocytes: physiology, hypertrophy, heart failure

63%
Lewartowski B., Mackiewicz U.
Acta Biochimica Polonica
|
2003
|
tom 50
|
nr Supplement 1
4
Content available remote

The non-neuronal heart's acetylcholine in health and disease

63%
Lewartowski B., Mackiewicz U.
Journal of Physiology and Pharmacology
|
2015
|
tom 66
|
nr 6
5
Content available remote

The effect of sarcoplasmic reticulum Ca2+ leak on contractile activity of guinea pig heart myocytes depends on activity of sarcoplasmic reticulum Ca2+-ATPase and Na+/Ca2+ exchanger

63%
Mackiewicz U., Lewartowski B.
Journal of Physiology and Pharmacology
|
2008
|
tom 59
|
nr 2
Decreased expression of sarcoplasmic reticulum (SR) Ca2+-ATPase (SERCA), overexpression of Na+/Ca2+ exchanger (NCX) and diastolic SR Ca2+ leak from the ryanodine receptors (RyRs) are believed to contribute to the decrease of myocyte contraction in failing heart. In this work we induced Ca2+ leak through RyRs in isolated myocytes of guinea pig hearts by 20µM FK-506. The SR Ca2+ leak resulted in (1) decreased amplitude of cell shortening and of Ca2+ transients, (2) decreased rate of Ca2+ transients decay (3) enhanced diastolic Ca2+ loss. The effect of FK-506 on amplitude of cell shortening was reversed and that on diastolic Ca2+ loss blocked by partial inhibition of NCX due to lowering Na+ concentration in superfusion solution from 144 mM to 100 mM. The amplitude of cell shortening and Ca2+ transients decreased by FK-506 was significantly increased by 10-7 M thapsigargin. In conclusion, the effect of SR Ca2+ leak induced by FK-506 on myocyte contraction is strictly dependent on activity of SERCA and NCX.
6
Content available remote

Temperature dependent contribution of Ca2+ transporters to relaxation in cardiac myocytes: important role of sarcolemmal Ca2+ -ATPase

63%
Mackiewicz U., Lewartowski B.
Journal of Physiology and Pharmacology
|
2006
|
tom 57
|
nr 1
Activities of Ca2+-ATPase of sarcoplasmic reticulum (SERCA) and Na+/Ca2+ exchanger (NCX) involved in cellular Ca2+ turnover greatly change in hypertrophied and failing hearts. Unfortunately, contribution of these proteins as well as of the sarcolemmal Ca2+-ATPase (PMCA) to cellular Ca2+ turnover has been investigated almost exclusively at room temperature. PMCA is of particular interest since it may affect activity of calcineurin and nNOS. Therefore the objective of this study was to reinvestigate contribution of SERCA, NCX and PMCA to cell relaxation and the effect of PMCA on cell contraction at 37°C. Myocytes isolated from the ventricles of guinea pig and rat hearts and incubated with Indo-1 were field stimulated at the rate of 60/min. Contribution of SERCA, NCX and PMCA was calculated from the rate constants of the decaying components of electrically stimulated Ca2+ transients or of the transients initiated by caffeine dissolved in normal Tyrode or in 0Na, 0Ca Tyrode. Increase in temperature from 24 to 37°C increased the relative contribution of NCX from 6.1% to 7.5% in rat and from 21.3 to 51.9 % in guinea pig at the expense of SERCA. The contribution of the PMCA to relaxation in both species increased upon rise in temperature from 24 % to 37°C from negligible values to 3.7 %. In both species amplitude of Ca2+ transients was at 24°C nearly twice as high as at 37°C. It was nearly doubled by carboxyeosine (CE), a PMCA blocker at 37°C but was hardly affected at 24°C. The effects of CE were concentration-dependent and conformed with the degree of inhibition of activity of PMCA. Conclusions: PMCA plays an important role in regulation of myocardial contraction despite its small contribution to relaxation. In guinea pig but not in rat relative contribution of SERCA and NCX to relaxation is highly temperature dependent.
7
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Aktywność enzymów oddechowych szeregu oksydazy bursztynowej w niedokrwistości doświadczalnej z niedoboru żelaza

51%
Mackiewicz U., Kasprzak L., Obuchowicz L., Michejda J.
Acta Physiologica Polonica
|
1961
|
tom 12
|
nr 2
8
Content available remote

Voltage dependent activation of tonic contraction in cardiac myocytes

51%
Mackiewicz U., Emanuel K., Lewartowski B.
Journal of Physiology and Pharmacology
|
2003
|
tom 54
|
nr 3
Contractions of isolated single myocytes of guinea pig heart stimulated by rectangular depolarizing pulses consist of a phasic component and a voltage dependent tonic component. In this study we analyzed the mechanism of activation of the graded, sustained contractions elicited by slow ramp depolarization and their relation to the components of contractions elicited by rectangular depolarizing pulses. Experiments were performed at 37°C in ventricular myocytes of guinea pig heart. Voltage-clamped myocytes were stimulated by the pulses from the holding potential of -40 to +5 mV or by ramp depolarization shifting voltage within this range within 6 s. [Ca2+]i was monitored as fluorescence of Indo 1-AM and contractions were recorded with the TV edge-tracking system. Myocytes responded to the ramp depolarization between -25 and -6 mV by the slow, sustained increase in [Ca2+]i and shortening, the maximal amplitude of which was in each cell similar to that of the tonic component of Ca2+ transient and contraction. The contractile responses to ramp depolarization were blocked by 200 µM ryanodine and Ca2+-free solution, but were not blocked by 20 µM nifedipine or 100 - 200 µM Cd2+ and potentiated by 5 mM Ni2+. The responses to ramp depolarization were with this respect similar to the tonic but not to the phasic component of contraction: both components were blocked by 200 µM ryanodine, and were not blocked by Cd2+ or Ni2+ despite complete inhibition of the phasic Ca2+ current. However, the phasic component but not the tonic component of contraction in cells superfused with Ni2+ was inhibited by nifedipine. Both components of contraction were inhibited by Ca2+-free solution superfused 15 s prior to stimulation. Conclusions: In myocytes of guinea pig heart the contractile response to ramp depolarization is equivalent to the tonic component of contraction. It is activated by Ca2+ released from the sarcoplasmic reticulum by the ryanodine receptors. Their activation and inactivation is voltage dependent and it does not depend on the Ca2+ influx by the Ca2+ channels or reverse mode Na+/Ca2+ exchange, however, it may depend on Ca2+ influx by some other, not yet defined route.
9
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Properties of ventricular myocytes isolated from the hypertrophied and failing hearts of spontaneously hypertensive rats

51%
Emanuel K., Mackiewicz U., Pytkowski B., Lewartowski B.
Journal of Physiology and Pharmacology
|
1999
|
tom 50
|
nr 2
10
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Agonist of dihydropyridine receptors, BayK8644 depresses excitation-contraction coupling in myocytes of guinea pig heart

51%
Mackiewicz U., Emanuel K., Lewartowski B.
Journal of Physiology and Pharmacology
|
2001
|
tom 52
|
nr 3
11
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Effects of mibefradil, a blocker of T-type Ca2plus channels, in single myocytes and intact muscle of guinea-pig heart

51%
Emanuel K., Mackiewicz U., Pytkowski B., Lewartowski B.
Journal of Physiology and Pharmacology
|
1998
|
tom 49
|
nr 4
12
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Dihydropyridine receptors functioning as voltage sensors in cardiac myocytes

51%
Mackiewicz U., Emanuel K., Lewartowski B.
Journal of Physiology and Pharmacology
|
2000
|
tom 51
|
nr 4,2
13

Effect of thyroid hormone on the myosin heavy chain isoforms in slow and fast muscles of the rat

45%
Jakubiec-Puka A., Ciechomska I., Mackiewicz U., Langford J., Chomontowska H.
Acta Biochimica Polonica
|
1999
|
tom 46
|
nr 3
The myosin heavy chain (MHC) was studied by biochemical methods in the slow-twitch (soleus) and two fast-twitch leg muscles of the triiodothyronine treated (hyperthyroid), thyreoidectomized (hypothyroid) and euthyroid (control) rats. The changes in the contents of individual MHC isoforms (MHC-1, MHC-2A, MHC-2B and MHC-2X) were evaluated in relation to the muscle mass and the total MHC content. The MHC-1 content decreased in hyperthyreosis, while it increased in hypothyreosis in the soleus and in the fast muscles. The MHC-2A content increased in hyperthyreosis and it decreased in hypothyreosis in the soleus muscle. In the fast muscles hyperthyreosis did not affect the MHC-2A content, whereas hypothyreosis caused an increase in this MHC isoform content. The MHC-2X, present only in traces or undetected in the control soleus muscle, was synthesised in considerable amount in hyperthyreosis; in hypothyreosis the MHC-2X was not detected in the soleus. In the fast muscles the content of MHC-2X was not affected by any changes in the thyroid hormone level. The MHC-2B seemed to be not influenced by hyperthyreosis in the fast muscles, whereas the hypothyreosis caused a decrease of its content. In the soleus muscle the MHC-2B was not detected in any groups of rats. The results suggest that the amount of each of the four MHC isoforms expressed in the mature rat leg muscles is influenced by the thyroid hormone in a different way. The MHC-2A and the MHC-2X are differently regulated in the soleus and in the fast muscles; thyroid hormone seems to be necessary for expression of those isoforms in the soleus muscle.
14
Content available remote

Total and high molecular weight adiponectin levels in the rat model of post-myocardial infarction heart failure

33%
Kalisz M., Baranowska B., Wolinska-Witort E., Maczewski M., Mackiewicz U., Tulacz D., Gora M., Martynska L., Bik W.
Journal of Physiology and Pharmacology
|
2015
|
tom 66
|
nr 5
15
Content available remote

Human skeletal muscle-derived stem/progenitor cells modified with connexin-43 prevent arrhythmia in rat post-infarction hearts and influence gene expression in the myocardium

27%
Rugowska A., Wiernicki B., Maczewski M., Mackiewicz U., Chojnacka K., Bednarek-Rajewska K., Kluk A., Majewski P., Kolanowski T., Malcher A., Rozwadowska N., Kurpisz M.
Journal of Physiology and Pharmacology
|
2019
|
tom 70
|
nr 6
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