Tomić, Nenad

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  • Tomić, Nenad (3)
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Author's Bibliography

Biochemical Markers of Renal Function

Krstić, Danijela Z.; Tomić, Nenad; Radosavljević, Branimir; Avramović, Nataša; Dragutinović, Vesna; Radojević-Škodrić, Sanja; Čolović, Mirjana B.

(2016)

TY  - JOUR
AU  - Krstić, Danijela Z.
AU  - Tomić, Nenad
AU  - Radosavljević, Branimir
AU  - Avramović, Nataša
AU  - Dragutinović, Vesna
AU  - Radojević-Škodrić, Sanja
AU  - Čolović, Mirjana B.
PY  - 2016
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/1200
AB  - Kidney damage can be induced by ischemia, autoimmune diseases, hypertension, allograft rejection, metabolic or genetic disorders, infections or toxins. The influence of these factors could result in acute kidney injury (AKI) defined as an unexpected decrease in urine output or renal function, or encourage the development of chronic kidney disease (CKD). Biomarkers of renal function, measured in urine and serum, are in increasing use in order to estimate the severity and nature of kidney injury, and consequently apply appropriate therapy and improve patient management. The determined values of biomarkers can suggest the potential risk of kidney disease and the type of renal injury, predict the disease progression, as well as be helpful for assessing the response to an applied therapy. Although novel biomarkers are in practical use, serum creatinine, the indicator of glomerular filtration rate is still the most frequently used biomarker of renal function despite its known limitations. In recent decades, numerous studies resulted in discovering urinary and serum proteins that can serve as biomarkers for early and accurate detection of AKI and its development, as well as the identification of CKD. This review gives an overview of the most important renal biomarkers investigated in kidney diseases, classified in following types: functional biomarkers, up-regulated proteins, enzymes, and cycle arrest biomarkers. It describes their properties, physiological roles, and discusses the utility of these molecules in different clinical settings.
T2  - Current Medicinal Chemistry
T1  - Biochemical Markers of Renal Function
VL  - 23
IS  - 19
SP  - 2018
EP  - 2040
DO  - 10.2174/0929867323666160115130241
ER  - 
@article{
author = "Krstić, Danijela Z. and Tomić, Nenad and Radosavljević, Branimir and Avramović, Nataša and Dragutinović, Vesna and Radojević-Škodrić, Sanja and Čolović, Mirjana B.",
year = "2016",
abstract = "Kidney damage can be induced by ischemia, autoimmune diseases, hypertension, allograft rejection, metabolic or genetic disorders, infections or toxins. The influence of these factors could result in acute kidney injury (AKI) defined as an unexpected decrease in urine output or renal function, or encourage the development of chronic kidney disease (CKD). Biomarkers of renal function, measured in urine and serum, are in increasing use in order to estimate the severity and nature of kidney injury, and consequently apply appropriate therapy and improve patient management. The determined values of biomarkers can suggest the potential risk of kidney disease and the type of renal injury, predict the disease progression, as well as be helpful for assessing the response to an applied therapy. Although novel biomarkers are in practical use, serum creatinine, the indicator of glomerular filtration rate is still the most frequently used biomarker of renal function despite its known limitations. In recent decades, numerous studies resulted in discovering urinary and serum proteins that can serve as biomarkers for early and accurate detection of AKI and its development, as well as the identification of CKD. This review gives an overview of the most important renal biomarkers investigated in kidney diseases, classified in following types: functional biomarkers, up-regulated proteins, enzymes, and cycle arrest biomarkers. It describes their properties, physiological roles, and discusses the utility of these molecules in different clinical settings.",
journal = "Current Medicinal Chemistry",
title = "Biochemical Markers of Renal Function",
volume = "23",
number = "19",
pages = "2018-2040",
doi = "10.2174/0929867323666160115130241"
}
Krstić, D. Z., Tomić, N., Radosavljević, B., Avramović, N., Dragutinović, V., Radojević-Škodrić, S.,& Čolović, M. B.. (2016). Biochemical Markers of Renal Function. in Current Medicinal Chemistry, 23(19), 2018-2040.
https://doi.org/10.2174/0929867323666160115130241
Krstić DZ, Tomić N, Radosavljević B, Avramović N, Dragutinović V, Radojević-Škodrić S, Čolović MB. Biochemical Markers of Renal Function. in Current Medicinal Chemistry. 2016;23(19):2018-2040.
doi:10.2174/0929867323666160115130241 .
Krstić, Danijela Z., Tomić, Nenad, Radosavljević, Branimir, Avramović, Nataša, Dragutinović, Vesna, Radojević-Škodrić, Sanja, Čolović, Mirjana B., "Biochemical Markers of Renal Function" in Current Medicinal Chemistry, 23, no. 19 (2016):2018-2040,
https://doi.org/10.2174/0929867323666160115130241 . .
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Interaction of the [PtCl2(DMSO)(2)] Complex with L-Cysteine

Vasić, Dragana D.; Savić, Jasmina; Bugaricic, Zivadin; Krstić, Danijela Z.; Tomić, Nenad; Čolović, Mirjana B.; Petković, Marijana; Vasić, Vesna M.

(2009)

TY  - JOUR
AU  - Vasić, Dragana D.
AU  - Savić, Jasmina
AU  - Bugaricic, Zivadin
AU  - Krstić, Danijela Z.
AU  - Tomić, Nenad
AU  - Čolović, Mirjana B.
AU  - Petković, Marijana
AU  - Vasić, Vesna M.
PY  - 2009
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3657
AB  - The reaction between [PtCl,(DMSO)(2)] and L-cysteine (L-Cys) has been investigated in the presence of micelles of sodium dodecyl sulfate (SDS) - as a model for biological membranes. Additionally, the inhibitory effect of [PtCl2(DMSO)(2)] on the Na+,K+-ATPise activity and its partial prevention with 10 mM L-Cys were demonstrated. The interaction of L-Cys with [Ptcl(2)(DMSO)(2)] resulted in the formation of a [Pt(DMSO)(2)L-Cys)(2)](2+) (DMSO)(2)] Complex, which most probably occurs through stepwise replacement of Cl- with L-Cys. It has also been demonstrated that neither the pH value nor SDS affects the composition of the new complex. On the other hand, the pH value and SDS do affect the reaction rate, most probably due to electrostatic interactions with reactants. In Summary, this study can be used as a simple model approach for the investigation of reaction mechanisms between platinum complexes and various biomolecules, and for the determination of potential toxicity and/or side effects of antitumour platinum drugs.
T2  - Zeitschrift fur Naturforschung. Section C: Journal of Biosciences
T1  - Interaction of the [PtCl2(DMSO)(2)] Complex with L-Cysteine
VL  - 64
IS  - 1-2
SP  - 103
EP  - 108
DO  - 10.1515/znc-2009-1-217
UR  - https://hdl.handle.net/21.15107/rcub_vinar_3657
ER  - 
@article{
author = "Vasić, Dragana D. and Savić, Jasmina and Bugaricic, Zivadin and Krstić, Danijela Z. and Tomić, Nenad and Čolović, Mirjana B. and Petković, Marijana and Vasić, Vesna M.",
year = "2009",
abstract = "The reaction between [PtCl,(DMSO)(2)] and L-cysteine (L-Cys) has been investigated in the presence of micelles of sodium dodecyl sulfate (SDS) - as a model for biological membranes. Additionally, the inhibitory effect of [PtCl2(DMSO)(2)] on the Na+,K+-ATPise activity and its partial prevention with 10 mM L-Cys were demonstrated. The interaction of L-Cys with [Ptcl(2)(DMSO)(2)] resulted in the formation of a [Pt(DMSO)(2)L-Cys)(2)](2+) (DMSO)(2)] Complex, which most probably occurs through stepwise replacement of Cl- with L-Cys. It has also been demonstrated that neither the pH value nor SDS affects the composition of the new complex. On the other hand, the pH value and SDS do affect the reaction rate, most probably due to electrostatic interactions with reactants. In Summary, this study can be used as a simple model approach for the investigation of reaction mechanisms between platinum complexes and various biomolecules, and for the determination of potential toxicity and/or side effects of antitumour platinum drugs.",
journal = "Zeitschrift fur Naturforschung. Section C: Journal of Biosciences",
title = "Interaction of the [PtCl2(DMSO)(2)] Complex with L-Cysteine",
volume = "64",
number = "1-2",
pages = "103-108",
doi = "10.1515/znc-2009-1-217",
url = "https://hdl.handle.net/21.15107/rcub_vinar_3657"
}
Vasić, D. D., Savić, J., Bugaricic, Z., Krstić, D. Z., Tomić, N., Čolović, M. B., Petković, M.,& Vasić, V. M.. (2009). Interaction of the [PtCl2(DMSO)(2)] Complex with L-Cysteine. in Zeitschrift fur Naturforschung. Section C: Journal of Biosciences, 64(1-2), 103-108.
https://doi.org/10.1515/znc-2009-1-217
https://hdl.handle.net/21.15107/rcub_vinar_3657
Vasić DD, Savić J, Bugaricic Z, Krstić DZ, Tomić N, Čolović MB, Petković M, Vasić VM. Interaction of the [PtCl2(DMSO)(2)] Complex with L-Cysteine. in Zeitschrift fur Naturforschung. Section C: Journal of Biosciences. 2009;64(1-2):103-108.
doi:10.1515/znc-2009-1-217
https://hdl.handle.net/21.15107/rcub_vinar_3657 .
Vasić, Dragana D., Savić, Jasmina, Bugaricic, Zivadin, Krstić, Danijela Z., Tomić, Nenad, Čolović, Mirjana B., Petković, Marijana, Vasić, Vesna M., "Interaction of the [PtCl2(DMSO)(2)] Complex with L-Cysteine" in Zeitschrift fur Naturforschung. Section C: Journal of Biosciences, 64, no. 1-2 (2009):103-108,
https://doi.org/10.1515/znc-2009-1-217 .,
https://hdl.handle.net/21.15107/rcub_vinar_3657 .
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The influence of potassium ion (K+) on digoxin-induced inhibition of porcine cerebral cortex Na+/K+-ATPase

Krstić, Danijela Z.; Tomić, Nenad; Krinulović, Katarina; Vasić, Vesna M.

(2006)

TY  - JOUR
AU  - Krstić, Danijela Z.
AU  - Tomić, Nenad
AU  - Krinulović, Katarina
AU  - Vasić, Vesna M.
PY  - 2006
UR  - https://vinar.vin.bg.ac.rs/handle/123456789/3081
AB  - The in vitro influence of potassium ion modulations, in the concentration range 2mM - 500mM, on digoxin-induced inhibition of porcine cerebral cortex Na+/K+-ATPase activity was studied. The response of enzymatic activity in the presence of various K+ concentrations to digoxin was biphasic, thereby, indicating the existence of two Na+/K+-ATPase isoforms, differing in the affinity towards the tested drug. Both isoforms showed higher sensitivity to digoxin in the presence of K+ ions below 20mM in the medium assay. The IC50 values for high/low isoforms 2.77 x 10(-6) M/8.56 x 10(-5) Mand 7.06 x 10(-7) M/1.87 x 10(-5) Mwere obtained in the presence of optimal (20mM) and 2mMK(+), respectively. However, preincubation in the presence of elevated K+ concentration (50 - 500mM) in the medium assay prior to Na+/K+-ATPase exposure to digoxin did not prevent the inhibition, i.e. IC50 values for both isoforms was the same as in the presence of the optimal K+ concentration. On the contrary, addition of 200mMK(+) into the medium assay after 10 minutes exposure of Na+/K+-ATPase to digoxin, showed a time-dependent recovery effect on the inhibited enzymatic activity. Kinetic analysis showed that digoxin inhibited Na+/K+-ATPase by reducing maximum enzymatic velocity (V-max) and K-m, implying an uncompetitive mode of interaction.
T2  - Journal of Enzyme Inhibition and Medicinal Chemistry
T1  - The influence of potassium ion (K+) on digoxin-induced inhibition of porcine cerebral cortex Na+/K+-ATPase
VL  - 21
IS  - 4
SP  - 471
EP  - 475
DO  - 10.1080/14756360600642230
ER  - 
@article{
author = "Krstić, Danijela Z. and Tomić, Nenad and Krinulović, Katarina and Vasić, Vesna M.",
year = "2006",
abstract = "The in vitro influence of potassium ion modulations, in the concentration range 2mM - 500mM, on digoxin-induced inhibition of porcine cerebral cortex Na+/K+-ATPase activity was studied. The response of enzymatic activity in the presence of various K+ concentrations to digoxin was biphasic, thereby, indicating the existence of two Na+/K+-ATPase isoforms, differing in the affinity towards the tested drug. Both isoforms showed higher sensitivity to digoxin in the presence of K+ ions below 20mM in the medium assay. The IC50 values for high/low isoforms 2.77 x 10(-6) M/8.56 x 10(-5) Mand 7.06 x 10(-7) M/1.87 x 10(-5) Mwere obtained in the presence of optimal (20mM) and 2mMK(+), respectively. However, preincubation in the presence of elevated K+ concentration (50 - 500mM) in the medium assay prior to Na+/K+-ATPase exposure to digoxin did not prevent the inhibition, i.e. IC50 values for both isoforms was the same as in the presence of the optimal K+ concentration. On the contrary, addition of 200mMK(+) into the medium assay after 10 minutes exposure of Na+/K+-ATPase to digoxin, showed a time-dependent recovery effect on the inhibited enzymatic activity. Kinetic analysis showed that digoxin inhibited Na+/K+-ATPase by reducing maximum enzymatic velocity (V-max) and K-m, implying an uncompetitive mode of interaction.",
journal = "Journal of Enzyme Inhibition and Medicinal Chemistry",
title = "The influence of potassium ion (K+) on digoxin-induced inhibition of porcine cerebral cortex Na+/K+-ATPase",
volume = "21",
number = "4",
pages = "471-475",
doi = "10.1080/14756360600642230"
}
Krstić, D. Z., Tomić, N., Krinulović, K.,& Vasić, V. M.. (2006). The influence of potassium ion (K+) on digoxin-induced inhibition of porcine cerebral cortex Na+/K+-ATPase. in Journal of Enzyme Inhibition and Medicinal Chemistry, 21(4), 471-475.
https://doi.org/10.1080/14756360600642230
Krstić DZ, Tomić N, Krinulović K, Vasić VM. The influence of potassium ion (K+) on digoxin-induced inhibition of porcine cerebral cortex Na+/K+-ATPase. in Journal of Enzyme Inhibition and Medicinal Chemistry. 2006;21(4):471-475.
doi:10.1080/14756360600642230 .
Krstić, Danijela Z., Tomić, Nenad, Krinulović, Katarina, Vasić, Vesna M., "The influence of potassium ion (K+) on digoxin-induced inhibition of porcine cerebral cortex Na+/K+-ATPase" in Journal of Enzyme Inhibition and Medicinal Chemistry, 21, no. 4 (2006):471-475,
https://doi.org/10.1080/14756360600642230 . .
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