TY  - JOUR
AU  - Zarić, Božidarka L.
AU  - Petrović, Srđan
AU  - Bjekić, Milan
AU  - Rajić, Ivana
AU  - Popović, Aleksandar R.
AU  - Đorđević, Dragana S.
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1479
AB  - Analysis of volatile organic compounds (VOCs) in human breath can provide information about the current physiological state of an individual, such as clinical conditions and exposure to exogenous pollutants. The blood-borne VOCs present in exhaled breath offer the possibility of exploring physiological and pathological processes in a noninvasive way. However, the field of exhaled breath analysis is still in its infancy. We undertook this study in order to define inter-individual variation and common compounds in breath VOCs of 48 young human volunteers. Alveolar breath samples were analyzed by automated thermal desorption, gas chromatography with flame ionization detector (FID) and electron capture detector (ECD) using SUPELCO standards with 66 compounds. Predominant compounds in the alveolar breath of analyzed subjects are ethylbenzene, 1-ethyl-4-methylbenzene, 1,2,4-trimethylbenzene and 1,3,5-trimethylbenzene (over 50% of the subjects). Isopropyl alcohol, propylene, acetone, ethanol were found as well. We detected substituted compounds in exhaled breath.
PB  - Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd
T2  - Archives of biological sciences
T1  - Analysis of Human Exhaled Breath in a Population of Young Volunteers
VL  - 66
IS  - 4
SP  - 1529
EP  - 1538
DO  - 10.2298/ABS1404529Z
ER  - 

@article{
author = "Zarić, Božidarka L. and Petrović, Srđan and Bjekić, Milan and Rajić, Ivana and Popović, Aleksandar R. and Đorđević, Dragana S.",
year = "2014",
abstract = "Analysis of volatile organic compounds (VOCs) in human breath can provide information about the current physiological state of an individual, such as clinical conditions and exposure to exogenous pollutants. The blood-borne VOCs present in exhaled breath offer the possibility of exploring physiological and pathological processes in a noninvasive way. However, the field of exhaled breath analysis is still in its infancy. We undertook this study in order to define inter-individual variation and common compounds in breath VOCs of 48 young human volunteers. Alveolar breath samples were analyzed by automated thermal desorption, gas chromatography with flame ionization detector (FID) and electron capture detector (ECD) using SUPELCO standards with 66 compounds. Predominant compounds in the alveolar breath of analyzed subjects are ethylbenzene, 1-ethyl-4-methylbenzene, 1,2,4-trimethylbenzene and 1,3,5-trimethylbenzene (over 50% of the subjects). Isopropyl alcohol, propylene, acetone, ethanol were found as well. We detected substituted compounds in exhaled breath.",
publisher = "Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd",
journal = "Archives of biological sciences",
title = "Analysis of Human Exhaled Breath in a Population of Young Volunteers",
volume = "66",
number = "4",
pages = "1529-1538",
doi = "10.2298/ABS1404529Z"
}

Zarić, B. L., Petrović, S., Bjekić, M., Rajić, I., Popović, A. R.,& Đorđević, D. S.. (2014). Analysis of Human Exhaled Breath in a Population of Young Volunteers. in Archives of biological sciences
Inst Bioloska Istrazivanja Sinisa Stankovic, Beograd., 66(4), 1529-1538.
https://doi.org/10.2298/ABS1404529Z

Zarić BL, Petrović S, Bjekić M, Rajić I, Popović AR, Đorđević DS. Analysis of Human Exhaled Breath in a Population of Young Volunteers. in Archives of biological sciences. 2014;66(4):1529-1538.
doi:10.2298/ABS1404529Z .

Zarić, Božidarka L., Petrović, Srđan, Bjekić, Milan, Rajić, Ivana, Popović, Aleksandar R., Đorđević, Dragana S., "Analysis of Human Exhaled Breath in a Population of Young Volunteers" in Archives of biological sciences, 66, no. 4 (2014):1529-1538,
https://doi.org/10.2298/ABS1404529Z . .

TY  - CHAP
AU  - Sudar, Emina
AU  - Soskić, Sanja
AU  - Zarić, Božidarka L.
AU  - Rašić-Milutinović, Zorica
AU  - Smiljanić, Katarina
AU  - Radak, Đorđe
AU  - Mikhailidis, Dimitri
AU  - Rizzo, Manfredi
AU  - Isenović, Esma
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3919
AB  - Cardiovascular disease (CVD) is common cause of death in humans and its major underlying pathology is atherosclerosis. Atherosclerosis is a chronic inflammatory disease that predisposes to coronary artery disease (CAD), stroke and peripheral arterial disease, responsible for most of the cardiovascular morbidity and mortality. This inflammatory process, triggered by the presence of lipids in the vascular wall, and encompasses a complex interaction among inflammatory cells, vascular elements, and lipoproteins through the expression of several adhesion molecules and cytokines. Obesity is a risk factor for CVD but this association is not fully understood. Altered levels of obesity related peptides such as ghrelin may play an important role in this pathophysiology. Recent evidence indicates that ghrelin features several cardiovascular activities, including increased myocardial contractility, vasodilatation and protection from myocardial infarction. Recent data demonstrate that ghrelin can influence important key events in atherogenesis and thus they may play a role in atherosclerosis. In this review we present the latest data from recent animal and clinical studies which focus on a novel approach to ghrelin as a potential therapeutic agent in the treatment of a complex disease like atherosclerosis. Thus, ghrelin may become a new therapeutic target for the treatment of CVD. Further studies are necessary to investigate the potential mechanisms involved in the effects of ghrelin on the cardiovascular system.
PB  - Nova Science Publishers Inc, New York
T2  - Ghrelin: Production, Action Mechanisms and Physiological Effects
T1  - Ghrelin, obesity and atherosclerosis
SP  - 111
EP  - 126
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3919
ER  - 

@inbook{
author = "Sudar, Emina and Soskić, Sanja and Zarić, Božidarka L. and Rašić-Milutinović, Zorica and Smiljanić, Katarina and Radak, Đorđe and Mikhailidis, Dimitri and Rizzo, Manfredi and Isenović, Esma",
year = "2012",
abstract = "Cardiovascular disease (CVD) is common cause of death in humans and its major underlying pathology is atherosclerosis. Atherosclerosis is a chronic inflammatory disease that predisposes to coronary artery disease (CAD), stroke and peripheral arterial disease, responsible for most of the cardiovascular morbidity and mortality. This inflammatory process, triggered by the presence of lipids in the vascular wall, and encompasses a complex interaction among inflammatory cells, vascular elements, and lipoproteins through the expression of several adhesion molecules and cytokines. Obesity is a risk factor for CVD but this association is not fully understood. Altered levels of obesity related peptides such as ghrelin may play an important role in this pathophysiology. Recent evidence indicates that ghrelin features several cardiovascular activities, including increased myocardial contractility, vasodilatation and protection from myocardial infarction. Recent data demonstrate that ghrelin can influence important key events in atherogenesis and thus they may play a role in atherosclerosis. In this review we present the latest data from recent animal and clinical studies which focus on a novel approach to ghrelin as a potential therapeutic agent in the treatment of a complex disease like atherosclerosis. Thus, ghrelin may become a new therapeutic target for the treatment of CVD. Further studies are necessary to investigate the potential mechanisms involved in the effects of ghrelin on the cardiovascular system.",
publisher = "Nova Science Publishers Inc, New York",
journal = "Ghrelin: Production, Action Mechanisms and Physiological Effects",
booktitle = "Ghrelin, obesity and atherosclerosis",
pages = "111-126",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3919"
}

Sudar, E., Soskić, S., Zarić, B. L., Rašić-Milutinović, Z., Smiljanić, K., Radak, Đ., Mikhailidis, D., Rizzo, M.,& Isenović, E.. (2012). Ghrelin, obesity and atherosclerosis. in Ghrelin: Production, Action Mechanisms and Physiological Effects
Nova Science Publishers Inc, New York., 111-126.
https://hdl.handle.net/21.15107/rcub_cherry_3919

Sudar E, Soskić S, Zarić BL, Rašić-Milutinović Z, Smiljanić K, Radak Đ, Mikhailidis D, Rizzo M, Isenović E. Ghrelin, obesity and atherosclerosis. in Ghrelin: Production, Action Mechanisms and Physiological Effects. 2012;:111-126.
https://hdl.handle.net/21.15107/rcub_cherry_3919 .

Sudar, Emina, Soskić, Sanja, Zarić, Božidarka L., Rašić-Milutinović, Zorica, Smiljanić, Katarina, Radak, Đorđe, Mikhailidis, Dimitri, Rizzo, Manfredi, Isenović, Esma, "Ghrelin, obesity and atherosclerosis" in Ghrelin: Production, Action Mechanisms and Physiological Effects (2012):111-126,
https://hdl.handle.net/21.15107/rcub_cherry_3919 .

TY  - CHAP
AU  - Sudar, Emina
AU  - Soskić, Sanja
AU  - Zarić, Božidarka L.
AU  - Rašić-Milutinović, Zorica
AU  - Smiljanić, Katarina
AU  - Radak, Đorđe
AU  - Mikhailidis, Dimitri
AU  - Rizzo, Manfredi
AU  - Isenović, Esma
PY  - 2012
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3920
AB  - Cardiovascular disease (CVD) is common cause of death in humans and its major underlying pathology is atherosclerosis. Atherosclerosis is a chronic inflammatory disease that predisposes to coronary artery disease (CAD), stroke and peripheral arterial disease, responsible for most of the cardiovascular morbidity and mortality. This inflammatory process, triggered by the presence of lipids in the vascular wall, and encompasses a complex interaction among inflammatory cells, vascular elements, and lipoproteins through the expression of several adhesion molecules and cytokines. Obesity is a risk factor for CVD but this association is not fully understood. Altered levels of obesity related peptides such as ghrelin may play an important role in this pathophysiology. Recent evidence indicates that ghrelin features several cardiovascular activities, including increased myocardial contractility, vasodilatation and protection from myocardial infarction. Recent data demonstrate that ghrelin can influence important key events in atherogenesis and thus they may play a role in atherosclerosis. In this review we present the latest data from recent animal and clinical studies which focus on a novel approach to ghrelin as a potential therapeutic agent in the treatment of a complex disease like atherosclerosis. Thus, ghrelin may become a new therapeutic target for the treatment of CVD. Further studies are necessary to investigate the potential mechanisms involved in the effects of ghrelin on the cardiovascular system.
PB  - Nova Science Publishers Inc, New York
T2  - Ghrelin: Production, Action Mechanisms and Physiological Effects
T1  - Ghrelin, obesity and atherosclerosis
SP  - 111
EP  - 126
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3920
ER  - 

@inbook{
author = "Sudar, Emina and Soskić, Sanja and Zarić, Božidarka L. and Rašić-Milutinović, Zorica and Smiljanić, Katarina and Radak, Đorđe and Mikhailidis, Dimitri and Rizzo, Manfredi and Isenović, Esma",
year = "2012",
abstract = "Cardiovascular disease (CVD) is common cause of death in humans and its major underlying pathology is atherosclerosis. Atherosclerosis is a chronic inflammatory disease that predisposes to coronary artery disease (CAD), stroke and peripheral arterial disease, responsible for most of the cardiovascular morbidity and mortality. This inflammatory process, triggered by the presence of lipids in the vascular wall, and encompasses a complex interaction among inflammatory cells, vascular elements, and lipoproteins through the expression of several adhesion molecules and cytokines. Obesity is a risk factor for CVD but this association is not fully understood. Altered levels of obesity related peptides such as ghrelin may play an important role in this pathophysiology. Recent evidence indicates that ghrelin features several cardiovascular activities, including increased myocardial contractility, vasodilatation and protection from myocardial infarction. Recent data demonstrate that ghrelin can influence important key events in atherogenesis and thus they may play a role in atherosclerosis. In this review we present the latest data from recent animal and clinical studies which focus on a novel approach to ghrelin as a potential therapeutic agent in the treatment of a complex disease like atherosclerosis. Thus, ghrelin may become a new therapeutic target for the treatment of CVD. Further studies are necessary to investigate the potential mechanisms involved in the effects of ghrelin on the cardiovascular system.",
publisher = "Nova Science Publishers Inc, New York",
journal = "Ghrelin: Production, Action Mechanisms and Physiological Effects",
booktitle = "Ghrelin, obesity and atherosclerosis",
pages = "111-126",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3920"
}

Sudar, E., Soskić, S., Zarić, B. L., Rašić-Milutinović, Z., Smiljanić, K., Radak, Đ., Mikhailidis, D., Rizzo, M.,& Isenović, E.. (2012). Ghrelin, obesity and atherosclerosis. in Ghrelin: Production, Action Mechanisms and Physiological Effects
Nova Science Publishers Inc, New York., 111-126.
https://hdl.handle.net/21.15107/rcub_cherry_3920

Sudar E, Soskić S, Zarić BL, Rašić-Milutinović Z, Smiljanić K, Radak Đ, Mikhailidis D, Rizzo M, Isenović E. Ghrelin, obesity and atherosclerosis. in Ghrelin: Production, Action Mechanisms and Physiological Effects. 2012;:111-126.
https://hdl.handle.net/21.15107/rcub_cherry_3920 .

Sudar, Emina, Soskić, Sanja, Zarić, Božidarka L., Rašić-Milutinović, Zorica, Smiljanić, Katarina, Radak, Đorđe, Mikhailidis, Dimitri, Rizzo, Manfredi, Isenović, Esma, "Ghrelin, obesity and atherosclerosis" in Ghrelin: Production, Action Mechanisms and Physiological Effects (2012):111-126,
https://hdl.handle.net/21.15107/rcub_cherry_3920 .

TY  - JOUR
AU  - Zarić, Božidarka L.
AU  - Jovanović, Vesna B.
AU  - Stojanović, Srđan Đ.
PY  - 2011
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1140
AB  - The distinguishing property of Sm protein associations is their high stability. In order to understand this property, we analyzed the interface non-covalent interactions and compared the properties of the Sm protein interfaces with those of a test set, Binding Interface Database (BID). The comparison revealed that the main differences between interfaces of Sm proteins and those of the BID set are the content of charged residues, hydrogen bonds, salt bridges, and conservation scores of interface residues. In Sm proteins, the interfaces have more hydrophobic and fewer charged residues than the surface, which is also the case for the BID test set and other proteins. However, in the interfaces, the content of charged residues in Sm proteins (26%) is substantially larger than that in the BID set (22%). Both interfaces of Sm proteins and of test set have a similar number of hydrophobic interactions per 100 angstrom(2). The interfaces of Sm proteins have substantially more hydrogen bonds than the interfaces in test set. The results show clearly that the interfaces of Sm proteins form more salt bridges compared with test set. On average, there are about 16 salt bridges per interface. The high conservation score of amino acids that are involved in non-covalent interactions in protein interfaces is an additional strong argument for their importance. The overriding conclusion from this study is that the non-covalent interactions in Sm protein interfaces considerably contribute to stability of higher order structures. (C) 2010 Elsevier Ltd. All rights reserved.
PB  - Academic Press Ltd- Elsevier Science Ltd, London
T2  - Journal of Theoretical Biology
T1  - Non-covalent interactions across subunit interfaces in Sm proteins
VL  - 271
IS  - 1
SP  - 18
EP  - 26
DO  - 10.1016/j.jtbi.2010.11.025
ER  - 

@article{
author = "Zarić, Božidarka L. and Jovanović, Vesna B. and Stojanović, Srđan Đ.",
year = "2011",
abstract = "The distinguishing property of Sm protein associations is their high stability. In order to understand this property, we analyzed the interface non-covalent interactions and compared the properties of the Sm protein interfaces with those of a test set, Binding Interface Database (BID). The comparison revealed that the main differences between interfaces of Sm proteins and those of the BID set are the content of charged residues, hydrogen bonds, salt bridges, and conservation scores of interface residues. In Sm proteins, the interfaces have more hydrophobic and fewer charged residues than the surface, which is also the case for the BID test set and other proteins. However, in the interfaces, the content of charged residues in Sm proteins (26%) is substantially larger than that in the BID set (22%). Both interfaces of Sm proteins and of test set have a similar number of hydrophobic interactions per 100 angstrom(2). The interfaces of Sm proteins have substantially more hydrogen bonds than the interfaces in test set. The results show clearly that the interfaces of Sm proteins form more salt bridges compared with test set. On average, there are about 16 salt bridges per interface. The high conservation score of amino acids that are involved in non-covalent interactions in protein interfaces is an additional strong argument for their importance. The overriding conclusion from this study is that the non-covalent interactions in Sm protein interfaces considerably contribute to stability of higher order structures. (C) 2010 Elsevier Ltd. All rights reserved.",
publisher = "Academic Press Ltd- Elsevier Science Ltd, London",
journal = "Journal of Theoretical Biology",
title = "Non-covalent interactions across subunit interfaces in Sm proteins",
volume = "271",
number = "1",
pages = "18-26",
doi = "10.1016/j.jtbi.2010.11.025"
}

Zarić, B. L., Jovanović, V. B.,& Stojanović, S. Đ.. (2011). Non-covalent interactions across subunit interfaces in Sm proteins. in Journal of Theoretical Biology
Academic Press Ltd- Elsevier Science Ltd, London., 271(1), 18-26.
https://doi.org/10.1016/j.jtbi.2010.11.025

Zarić BL, Jovanović VB, Stojanović SĐ. Non-covalent interactions across subunit interfaces in Sm proteins. in Journal of Theoretical Biology. 2011;271(1):18-26.
doi:10.1016/j.jtbi.2010.11.025 .

Zarić, Božidarka L., Jovanović, Vesna B., Stojanović, Srđan Đ., "Non-covalent interactions across subunit interfaces in Sm proteins" in Journal of Theoretical Biology, 271, no. 1 (2011):18-26,
https://doi.org/10.1016/j.jtbi.2010.11.025 . .

TY  - JOUR
AU  - Stojanović, Srđan Đ.
AU  - Zarić, Božidarka L.
AU  - Zarić, Snežana D.
PY  - 2010
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1123
AB  - The distinguishing property of Sm protein associations is very high stability. In order to understand this property, we analyzed the interfaces and compared the properties of Sm protein interfaces with those of a test set, the Binding Interface Database (BID). The comparison revealed that the main differences between the interfaces of Sm proteins and those of the BID set are the content of charged residues, the coordination numbers of the residues, knowledge-based pair potentials, and the conservation scores of hot spots. In Sm proteins, the interfaces have more hydrophobic and fewer charged residues than the surfaces, which is also the case for the BID test set and other proteins. However, in the interfaces, the content of charged residues in Sm proteins (26%) is substantially larger than that in the BID set (22%). Hot spots are residues that make up a small fraction of the interfaces, but they contribute most of the binding energy. These residues are critical to protein-protein interactions. Analyses of knowledge-based pair potentials of hot spot and non-hot spot residues in Sm proteins show that they are significantly different; their mean values are 31.5 and 11.3, respectively. In the BID set, this difference is smaller; in this case, the mean values for hot spot and non-hot spot residues are 20.7 and 12.4, respectively. Hence, the pair potentials of hot spots differ significantly for the Sm and BID data sets. In the interfaces of Sm proteins, the amino acids are tightly packed, and the coordination numbers are larger in Sm proteins than in the BID set for both hot spots and non-hot spots. At the same time, the coordination numbers are higher for hot spots; the average coordination number of the hot spot residues in Sm proteins is 7.7, while it is 6.1 for the non-hot spot residues. The difference in the calculated average conservation score for hot spots and non-hot spots in Sm proteins is significantly larger than it is in the BID set. In Sm proteins, the average conservation score for the hot spots is 7.4. Hot spots are surrounded by residues that are moderately conserved (5.9). The average conservation score for the other interface residues is 5.6. The conservation scores in the BID set do not show a significant distinction between hot and non-hot spots: the mean values for hot and non-hot spot residues are 5.5 and 5.2, respectively. These data show that structurally conserved residues and hot spots are significantly correlated in Sm proteins.
PB  - Springer, New York
T2  - Journal of Molecular Modeling
T1  - Protein subunit interfaces: a statistical analysis of hot spots in Sm proteins
VL  - 16
IS  - 11
SP  - 1743
EP  - 1751
DO  - 10.1007/s00894-010-0787-4
ER  - 

@article{
author = "Stojanović, Srđan Đ. and Zarić, Božidarka L. and Zarić, Snežana D.",
year = "2010",
abstract = "The distinguishing property of Sm protein associations is very high stability. In order to understand this property, we analyzed the interfaces and compared the properties of Sm protein interfaces with those of a test set, the Binding Interface Database (BID). The comparison revealed that the main differences between the interfaces of Sm proteins and those of the BID set are the content of charged residues, the coordination numbers of the residues, knowledge-based pair potentials, and the conservation scores of hot spots. In Sm proteins, the interfaces have more hydrophobic and fewer charged residues than the surfaces, which is also the case for the BID test set and other proteins. However, in the interfaces, the content of charged residues in Sm proteins (26%) is substantially larger than that in the BID set (22%). Hot spots are residues that make up a small fraction of the interfaces, but they contribute most of the binding energy. These residues are critical to protein-protein interactions. Analyses of knowledge-based pair potentials of hot spot and non-hot spot residues in Sm proteins show that they are significantly different; their mean values are 31.5 and 11.3, respectively. In the BID set, this difference is smaller; in this case, the mean values for hot spot and non-hot spot residues are 20.7 and 12.4, respectively. Hence, the pair potentials of hot spots differ significantly for the Sm and BID data sets. In the interfaces of Sm proteins, the amino acids are tightly packed, and the coordination numbers are larger in Sm proteins than in the BID set for both hot spots and non-hot spots. At the same time, the coordination numbers are higher for hot spots; the average coordination number of the hot spot residues in Sm proteins is 7.7, while it is 6.1 for the non-hot spot residues. The difference in the calculated average conservation score for hot spots and non-hot spots in Sm proteins is significantly larger than it is in the BID set. In Sm proteins, the average conservation score for the hot spots is 7.4. Hot spots are surrounded by residues that are moderately conserved (5.9). The average conservation score for the other interface residues is 5.6. The conservation scores in the BID set do not show a significant distinction between hot and non-hot spots: the mean values for hot and non-hot spot residues are 5.5 and 5.2, respectively. These data show that structurally conserved residues and hot spots are significantly correlated in Sm proteins.",
publisher = "Springer, New York",
journal = "Journal of Molecular Modeling",
title = "Protein subunit interfaces: a statistical analysis of hot spots in Sm proteins",
volume = "16",
number = "11",
pages = "1743-1751",
doi = "10.1007/s00894-010-0787-4"
}

Stojanović, S. Đ., Zarić, B. L.,& Zarić, S. D.. (2010). Protein subunit interfaces: a statistical analysis of hot spots in Sm proteins. in Journal of Molecular Modeling
Springer, New York., 16(11), 1743-1751.
https://doi.org/10.1007/s00894-010-0787-4

Stojanović SĐ, Zarić BL, Zarić SD. Protein subunit interfaces: a statistical analysis of hot spots in Sm proteins. in Journal of Molecular Modeling. 2010;16(11):1743-1751.
doi:10.1007/s00894-010-0787-4 .

Stojanović, Srđan Đ., Zarić, Božidarka L., Zarić, Snežana D., "Protein subunit interfaces: a statistical analysis of hot spots in Sm proteins" in Journal of Molecular Modeling, 16, no. 11 (2010):1743-1751,
https://doi.org/10.1007/s00894-010-0787-4 . .

TY  - JOUR
AU  - Isenovic, Esma R.
AU  - Fretaud, Maxence
AU  - Dobutović, Branislava
AU  - Sudar, Emina
AU  - Smiljanić, Katarina
AU  - Zarić, Božidarka L.
AU  - Trpkovic, Andreja
AU  - Marche, Pierre
PY  - 2009
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/612
AB  - Insulin (INS) via INS receptor acts as a mitogen in vascular smooth muscle cells (VSMCs) through stimulation of multiple signaling mechanisms, including p42/44 mitogen-activated protein kinase (ERK1/2) and phosphatidyl inositol-3 kinase (PI3K). In addition, cytosolic phospholipase 2 (cPLA(2)) is linked to VSMCs proliferation. However, the upstream mechanisms responsible for activation of cPLA(2) are not well defined. Therefore, this investigation used primary cultured rat VSMCs to examine the role of PI3K and ERK1/2 in the INS-dependent phosphorylation of cPLA(2) and proliferation induced by INS. Exposure of VSMCs to INS (100 nM) for 10 min increased the phosphorylation of cPLA(2) by 1.5-fold (p  lt  0.01), which was blocked by the cPLA(2) inhibitor MAFP (10 mu M; 15 min). Similarly, the PI3K inhibitor LY294002 (10 mu M; 15 min) and ERK1/2 inhibitor PD98059 (20 mu M; 15 min) abolished the INS-mediated increase in cPLA(2) phosphorylation by 59% (p  lt  0.001), and by 75% (p  lt  0.001), respectively. Further, inhibition of cPLA2 with cPLA2 inhibitor MAFP abolished the INS-stimulated ERK1/2 phosphorylation by 65% (p  lt  0.01). Incubation of rat VSMCs with INS resulted in an increase of VSMCs proliferation by 85% (p  lt  0.001). The effect of INS on VSMCs proliferation was significantly (p  lt  0.01) reduced by pretreatment with MAFP. Thus, we hypothesized that INS stimulates VSMCs proliferation via a mechanism involving the PI3K-dependent activation of cPLA(2) and release of arachidonic acid (AA), which activates ERK1/2 and further amplifies cPLA(2) activity. (C) 2009 International Federation for Cell Biology. Published by Elsevier Ltd. All rights reserved.
PB  - Academic Press Ltd- Elsevier Science Ltd, London
T2  - Cell Biology International
T1  - A novel hypothesis regarding the possible involvement of cytosolic phospholipase 2 in insulin-stimulated proliferation of vascular smooth muscle cells
VL  - 33
IS  - 3
SP  - 386
EP  - 392
DO  - 10.1016/j.cellbi.2009.01.010
ER  - 

@article{
author = "Isenovic, Esma R. and Fretaud, Maxence and Dobutović, Branislava and Sudar, Emina and Smiljanić, Katarina and Zarić, Božidarka L. and Trpkovic, Andreja and Marche, Pierre",
year = "2009",
abstract = "Insulin (INS) via INS receptor acts as a mitogen in vascular smooth muscle cells (VSMCs) through stimulation of multiple signaling mechanisms, including p42/44 mitogen-activated protein kinase (ERK1/2) and phosphatidyl inositol-3 kinase (PI3K). In addition, cytosolic phospholipase 2 (cPLA(2)) is linked to VSMCs proliferation. However, the upstream mechanisms responsible for activation of cPLA(2) are not well defined. Therefore, this investigation used primary cultured rat VSMCs to examine the role of PI3K and ERK1/2 in the INS-dependent phosphorylation of cPLA(2) and proliferation induced by INS. Exposure of VSMCs to INS (100 nM) for 10 min increased the phosphorylation of cPLA(2) by 1.5-fold (p  lt  0.01), which was blocked by the cPLA(2) inhibitor MAFP (10 mu M; 15 min). Similarly, the PI3K inhibitor LY294002 (10 mu M; 15 min) and ERK1/2 inhibitor PD98059 (20 mu M; 15 min) abolished the INS-mediated increase in cPLA(2) phosphorylation by 59% (p  lt  0.001), and by 75% (p  lt  0.001), respectively. Further, inhibition of cPLA2 with cPLA2 inhibitor MAFP abolished the INS-stimulated ERK1/2 phosphorylation by 65% (p  lt  0.01). Incubation of rat VSMCs with INS resulted in an increase of VSMCs proliferation by 85% (p  lt  0.001). The effect of INS on VSMCs proliferation was significantly (p  lt  0.01) reduced by pretreatment with MAFP. Thus, we hypothesized that INS stimulates VSMCs proliferation via a mechanism involving the PI3K-dependent activation of cPLA(2) and release of arachidonic acid (AA), which activates ERK1/2 and further amplifies cPLA(2) activity. (C) 2009 International Federation for Cell Biology. Published by Elsevier Ltd. All rights reserved.",
publisher = "Academic Press Ltd- Elsevier Science Ltd, London",
journal = "Cell Biology International",
title = "A novel hypothesis regarding the possible involvement of cytosolic phospholipase 2 in insulin-stimulated proliferation of vascular smooth muscle cells",
volume = "33",
number = "3",
pages = "386-392",
doi = "10.1016/j.cellbi.2009.01.010"
}

Isenovic, E. R., Fretaud, M., Dobutović, B., Sudar, E., Smiljanić, K., Zarić, B. L., Trpkovic, A.,& Marche, P.. (2009). A novel hypothesis regarding the possible involvement of cytosolic phospholipase 2 in insulin-stimulated proliferation of vascular smooth muscle cells. in Cell Biology International
Academic Press Ltd- Elsevier Science Ltd, London., 33(3), 386-392.
https://doi.org/10.1016/j.cellbi.2009.01.010

Isenovic ER, Fretaud M, Dobutović B, Sudar E, Smiljanić K, Zarić BL, Trpkovic A, Marche P. A novel hypothesis regarding the possible involvement of cytosolic phospholipase 2 in insulin-stimulated proliferation of vascular smooth muscle cells. in Cell Biology International. 2009;33(3):386-392.
doi:10.1016/j.cellbi.2009.01.010 .

Isenovic, Esma R., Fretaud, Maxence, Dobutović, Branislava, Sudar, Emina, Smiljanić, Katarina, Zarić, Božidarka L., Trpkovic, Andreja, Marche, Pierre, "A novel hypothesis regarding the possible involvement of cytosolic phospholipase 2 in insulin-stimulated proliferation of vascular smooth muscle cells" in Cell Biology International, 33, no. 3 (2009):386-392,
https://doi.org/10.1016/j.cellbi.2009.01.010 . .