Proteomics and phosphoproteomics study of LCMT1 overexpression and oxidative stress: overexpression of LCMT1 arrests H2O2-induced lose of cells viability. (1st January 2019)
- Record Type:
- Journal Article
- Title:
- Proteomics and phosphoproteomics study of LCMT1 overexpression and oxidative stress: overexpression of LCMT1 arrests H2O2-induced lose of cells viability. (1st January 2019)
- Main Title:
- Proteomics and phosphoproteomics study of LCMT1 overexpression and oxidative stress: overexpression of LCMT1 arrests H2O2-induced lose of cells viability
- Authors:
- Wang, Xinhang
Tang, Shen
Qin, Fu
Liu, Yuyang
Liang, Ziwei
Cai, Haiqing
Mo, Laiming
Xiao, Deqiang
Guo, Songcao
Ouyang, Yiqiang
Sun, Bin
Lu, Cailing
Li, Xiyi - Abstract:
- ABSTRACT: Objectives: Protein phosphatase 2A (PP2A), a major serine/threonine phosphatase, is also known to be a target of ROS. The methylation of PP2A can be catalyzed by leucine carboxyl methyltransferase-1 (LCMT1), which regulates PP2A activity and substrate specificity. Methods: In the previous study, we have showed that LCMT1-dependent PP2Ac methylation arrests H2 O2 -induced cell oxidative stress damage. To explore the possible protective mechanism, we performed iTRAQ-based comparative quantitative proteomics and phosphoproteomics studies of H2 O2 -treated vector control and LCMT1-overexpressing cells. Results: A total of 4480 non-redundant proteins and 3801 unique phosphopeptides were identified by this means. By comparing the H2 O2 -regulated proteins in LCMT1-overexpressing and vector control cells, we found that these differences were mainly related to protein phosphorylation, gene expression, protein maturation, the cytoskeleton and cell division. Further investigation of LCMT1 overexpression-specific regulated proteins under H2 O2 treatment supported the idea that LCMT1 overexpression induced ageneral dephosphorylation of proteins and indicated increased expression of non-erythrocytic hemoglobin, inactivation of MAPK3 and regulation of proteins related to Rho signal transduction, which were known to be linked to the regulation of the cytoskeleton. Discussion: These data provide proteomics and phosphoproteomics insights into the association of LCMT1-dependentABSTRACT: Objectives: Protein phosphatase 2A (PP2A), a major serine/threonine phosphatase, is also known to be a target of ROS. The methylation of PP2A can be catalyzed by leucine carboxyl methyltransferase-1 (LCMT1), which regulates PP2A activity and substrate specificity. Methods: In the previous study, we have showed that LCMT1-dependent PP2Ac methylation arrests H2 O2 -induced cell oxidative stress damage. To explore the possible protective mechanism, we performed iTRAQ-based comparative quantitative proteomics and phosphoproteomics studies of H2 O2 -treated vector control and LCMT1-overexpressing cells. Results: A total of 4480 non-redundant proteins and 3801 unique phosphopeptides were identified by this means. By comparing the H2 O2 -regulated proteins in LCMT1-overexpressing and vector control cells, we found that these differences were mainly related to protein phosphorylation, gene expression, protein maturation, the cytoskeleton and cell division. Further investigation of LCMT1 overexpression-specific regulated proteins under H2 O2 treatment supported the idea that LCMT1 overexpression induced ageneral dephosphorylation of proteins and indicated increased expression of non-erythrocytic hemoglobin, inactivation of MAPK3 and regulation of proteins related to Rho signal transduction, which were known to be linked to the regulation of the cytoskeleton. Discussion: These data provide proteomics and phosphoproteomics insights into the association of LCMT1-dependent PP2Ac methylation and oxidative stress and indirectly indicate that the methylation of PP2A plays an important role against oxidative stress. … (more)
- Is Part Of:
- Redox report. Volume 24:Number 1(2019)
- Journal:
- Redox report
- Issue:
- Volume 24:Number 1(2019)
- Issue Display:
- Volume 24, Issue 1 (2019)
- Year:
- 2019
- Volume:
- 24
- Issue:
- 1
- Issue Sort Value:
- 2019-0024-0001-0000
- Page Start:
- 1
- Page End:
- 9
- Publication Date:
- 2019-01-01
- Subjects:
- LCMT1 -- oxidative stress -- proteomics -- hemoglobin -- MAPK3 -- Rho signal transduction
Free radicals (Chemistry) -- Pathophysiology -- Periodicals
Oxidation, Physiological -- Periodicals
541.224 - Journal URLs:
- http://www.ingentaconnect.com/content/maney/rer ↗
http://maneypublishing.com/ ↗ - DOI:
- 10.1080/13510002.2019.1595332 ↗
- Languages:
- English
- ISSNs:
- 1351-0002
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 16952.xml