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Vanadium Compounds as Pro-Inflammatory Agents: Effects on Cyclooxygenases.

Korbecki J, Baranowska-Bosiacka I, Gutowska I, Chlubek D - Int J Mol Sci (2015)

Bottom Line: We refer mainly to the effects of vanadate (orthovanadate), vanadyl and pervanadate ions; the main focus is placed on their impact on intracellular signaling.We describe the exact mechanism of the effect of vanadium compounds on protein tyrosine phosphatases (PTP), epidermal growth factor receptor (EGFR), PLCγ, Src, mitogen-activated protein kinase (MAPK) cascades, transcription factor NF-κB, the effect on the proteolysis of COX-2 and the activity of cPLA2.For a better understanding of these processes, a lot of space is devoted to the transformation of vanadium compounds within the cell and the molecular influence on the direct targets of the discussed vanadium compounds.

View Article: PubMed Central - PubMed

Affiliation: Department of Biochemistry and Medical Chemistry, Pomeranian Medical University, Powstańców Wlkp. 72 Av., 70-111 Szczecin, Poland. jan.korbecki@onet.eu.

ABSTRACT
This paper discusses how the activity and expression of cyclooxygenases are influenced by vanadium compounds at anticancer concentrations and recorded in inorganic vanadium poisonings. We refer mainly to the effects of vanadate (orthovanadate), vanadyl and pervanadate ions; the main focus is placed on their impact on intracellular signaling. We describe the exact mechanism of the effect of vanadium compounds on protein tyrosine phosphatases (PTP), epidermal growth factor receptor (EGFR), PLCγ, Src, mitogen-activated protein kinase (MAPK) cascades, transcription factor NF-κB, the effect on the proteolysis of COX-2 and the activity of cPLA2. For a better understanding of these processes, a lot of space is devoted to the transformation of vanadium compounds within the cell and the molecular influence on the direct targets of the discussed vanadium compounds.

No MeSH data available.


Related in: MedlinePlus

Activation of cPLA2 by vanadium compounds. Vanadium compounds at low concentrations activates MAPK cascades that phosphorylates cPLA2. At higher concentrations of vanadium compounds activate Src, which phosphorylates PLCγ1. This process causes the release into the cytoplasm of IP3, which causes the activation of Ca2+ channels and the ion influx into the cytoplasm. This PLCγ1 also activates MAPK cascades. By increasing the concentration of Ca2+ and the activation of the MAPK cascades is activated cPLA2.
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ijms-16-12648-f006: Activation of cPLA2 by vanadium compounds. Vanadium compounds at low concentrations activates MAPK cascades that phosphorylates cPLA2. At higher concentrations of vanadium compounds activate Src, which phosphorylates PLCγ1. This process causes the release into the cytoplasm of IP3, which causes the activation of Ca2+ channels and the ion influx into the cytoplasm. This PLCγ1 also activates MAPK cascades. By increasing the concentration of Ca2+ and the activation of the MAPK cascades is activated cPLA2.

Mentions: The influx of Ca2+ induced by vanadium compounds may be due to PLCγ activation which results in the release of IP3 into the cytoplasm (Figure 6) [79,103,106,107,110]. Another pathway activated by PLCγ via DAG are ERK and p38 MAPK cascades, which are also involved in the activation of cPLA2 [104]; this route of MAPK cascade activation by vanadium compounds is tissue-specific [72,79]. IP3 activates ion channels that are responsible for the influx of Ca2+. The activation of PLCγ1 may depend on Src. Although this family of kinases may also activate PLCγ2, the influence of pervanadate via this pathway is yet to be confirmed [111].


Vanadium Compounds as Pro-Inflammatory Agents: Effects on Cyclooxygenases.

Korbecki J, Baranowska-Bosiacka I, Gutowska I, Chlubek D - Int J Mol Sci (2015)

Activation of cPLA2 by vanadium compounds. Vanadium compounds at low concentrations activates MAPK cascades that phosphorylates cPLA2. At higher concentrations of vanadium compounds activate Src, which phosphorylates PLCγ1. This process causes the release into the cytoplasm of IP3, which causes the activation of Ca2+ channels and the ion influx into the cytoplasm. This PLCγ1 also activates MAPK cascades. By increasing the concentration of Ca2+ and the activation of the MAPK cascades is activated cPLA2.
© Copyright Policy
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4490466&req=5

ijms-16-12648-f006: Activation of cPLA2 by vanadium compounds. Vanadium compounds at low concentrations activates MAPK cascades that phosphorylates cPLA2. At higher concentrations of vanadium compounds activate Src, which phosphorylates PLCγ1. This process causes the release into the cytoplasm of IP3, which causes the activation of Ca2+ channels and the ion influx into the cytoplasm. This PLCγ1 also activates MAPK cascades. By increasing the concentration of Ca2+ and the activation of the MAPK cascades is activated cPLA2.
Mentions: The influx of Ca2+ induced by vanadium compounds may be due to PLCγ activation which results in the release of IP3 into the cytoplasm (Figure 6) [79,103,106,107,110]. Another pathway activated by PLCγ via DAG are ERK and p38 MAPK cascades, which are also involved in the activation of cPLA2 [104]; this route of MAPK cascade activation by vanadium compounds is tissue-specific [72,79]. IP3 activates ion channels that are responsible for the influx of Ca2+. The activation of PLCγ1 may depend on Src. Although this family of kinases may also activate PLCγ2, the influence of pervanadate via this pathway is yet to be confirmed [111].

Bottom Line: We refer mainly to the effects of vanadate (orthovanadate), vanadyl and pervanadate ions; the main focus is placed on their impact on intracellular signaling.We describe the exact mechanism of the effect of vanadium compounds on protein tyrosine phosphatases (PTP), epidermal growth factor receptor (EGFR), PLCγ, Src, mitogen-activated protein kinase (MAPK) cascades, transcription factor NF-κB, the effect on the proteolysis of COX-2 and the activity of cPLA2.For a better understanding of these processes, a lot of space is devoted to the transformation of vanadium compounds within the cell and the molecular influence on the direct targets of the discussed vanadium compounds.

View Article: PubMed Central - PubMed

Affiliation: Department of Biochemistry and Medical Chemistry, Pomeranian Medical University, Powstańców Wlkp. 72 Av., 70-111 Szczecin, Poland. jan.korbecki@onet.eu.

ABSTRACT
This paper discusses how the activity and expression of cyclooxygenases are influenced by vanadium compounds at anticancer concentrations and recorded in inorganic vanadium poisonings. We refer mainly to the effects of vanadate (orthovanadate), vanadyl and pervanadate ions; the main focus is placed on their impact on intracellular signaling. We describe the exact mechanism of the effect of vanadium compounds on protein tyrosine phosphatases (PTP), epidermal growth factor receptor (EGFR), PLCγ, Src, mitogen-activated protein kinase (MAPK) cascades, transcription factor NF-κB, the effect on the proteolysis of COX-2 and the activity of cPLA2. For a better understanding of these processes, a lot of space is devoted to the transformation of vanadium compounds within the cell and the molecular influence on the direct targets of the discussed vanadium compounds.

No MeSH data available.


Related in: MedlinePlus