Ultrastructural, metabolic and proteomic changes in leaves of upland cotton in response to cadmium stress
Present study explores physiological, biochemical and proteomic changes in leaves of upland cotton (ZMS-49) using 500 μM cadmium (Cd) along with control. Leaves' biomass and chlorophyll pigments decreased at 500 μM Cd. Cd contents in roots were higher than leaves. Levels of ROS ( [Formula: see...
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| Autor*in: |
Daud, M K [verfasserIn] |
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| Format: |
Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
2015 |
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| Rechteinformationen: |
Nutzungsrecht: Copyright © 2014 Elsevier Ltd. All rights reserved. |
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| Systematik: |
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| Übergeordnetes Werk: |
Enthalten in: Chemosphere - Kidlington, Oxford : Elsevier Science, 1972, 120(2015), Seite 309-320 |
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| Übergeordnetes Werk: |
volume:120 ; year:2015 ; pages:309-320 |
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| DOI / URN: |
10.1016/j.chemosphere.2014.07.060 |
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| 245 | 1 | 0 | |a Ultrastructural, metabolic and proteomic changes in leaves of upland cotton in response to cadmium stress |
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| 520 | |a Present study explores physiological, biochemical and proteomic changes in leaves of upland cotton (ZMS-49) using 500 μM cadmium (Cd) along with control. Leaves' biomass and chlorophyll pigments decreased at 500 μM Cd. Cd contents in roots were higher than leaves. Levels of ROS ( [Formula: see text] and H2O2) both in vivo and in vitro and MDA contents were significantly increased. Chlorophyll parameters (F0, Fm, Fm(') and Fv/Fm), total soluble protein contents and APX showed a decline at 500 μM Cd. SOD, CAT and POD and GR activities significantly enhanced. Less ultrastructural alterations in leaves under Cd stress could be observed. Scanning micrographs at 500 μM Cd possessed less number of stomata as well as near absence of closed stomata. Cd could be located in cell wall, vacuoles and intracellular spaces. Important upregulated proteins were methionine synthase, ribulose 1,5-bisphosphate carboxylase, apoplastic anionic guaiacol peroxidase, glyceraldehydes-3-phosphate dehydrogenase (chloroplastic isoform) and ATP synthase D chain, (mitochondrial). Important downregulated proteins were seed storage proteins (vicilin and legumin), molecular chaperones (hsp70, chaperonin-60 alpha subunit; putative protein disulfide isomerase), ATP-dependent Clp protease, ribulose-1,5-bisphophate carboxylase/oxygenase large subunit. Increase in the activities of ROS-scavenging enzymes, less ultrastructural modification, Cd-deposition in dead parts of cells as well as active regulation of different proteins showed Cd-resistant nature of ZMS-49. | ||
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| 650 | 4 | |a Plant Proteins - metabolism | |
| 650 | 4 | |a Soil Pollutants - toxicity | |
| 650 | 4 | |a Cadmium - toxicity | |
| 650 | 4 | |a Chlorophyll - metabolism | |
| 650 | 4 | |a Plant Leaves - drug effects | |
| 650 | 4 | |a Gossypium - drug effects | |
| 650 | 4 | |a Plant Leaves - physiology | |
| 650 | 4 | |a Gossypium - physiology | |
| 650 | 4 | |a Proteome - drug effects | |
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| 700 | 1 | |a Lei, Mei |4 oth | |
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| 700 | 1 | |a Zhu, S J |4 oth | |
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10.1016/j.chemosphere.2014.07.060 doi PQ20160617 (DE-627)OLC1963058674 (DE-599)GBVOLC1963058674 (PRQ)c1333-8a8eeda27af36f3f4b64a21c634ad924ad30110ca263d549bf5240e459457af70 (KEY)0012464820150000120000000309ultrastructuralmetabolicandproteomicchangesinleave DE-627 ger DE-627 rakwb eng 333.7 DNB AR 10100 AVZ rvk 38.32 bkl 35.00 bkl Daud, M K verfasserin aut Ultrastructural, metabolic and proteomic changes in leaves of upland cotton in response to cadmium stress 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Present study explores physiological, biochemical and proteomic changes in leaves of upland cotton (ZMS-49) using 500 μM cadmium (Cd) along with control. Leaves' biomass and chlorophyll pigments decreased at 500 μM Cd. Cd contents in roots were higher than leaves. Levels of ROS ( [Formula: see text] and H2O2) both in vivo and in vitro and MDA contents were significantly increased. Chlorophyll parameters (F0, Fm, Fm(') and Fv/Fm), total soluble protein contents and APX showed a decline at 500 μM Cd. SOD, CAT and POD and GR activities significantly enhanced. Less ultrastructural alterations in leaves under Cd stress could be observed. Scanning micrographs at 500 μM Cd possessed less number of stomata as well as near absence of closed stomata. Cd could be located in cell wall, vacuoles and intracellular spaces. Important upregulated proteins were methionine synthase, ribulose 1,5-bisphosphate carboxylase, apoplastic anionic guaiacol peroxidase, glyceraldehydes-3-phosphate dehydrogenase (chloroplastic isoform) and ATP synthase D chain, (mitochondrial). Important downregulated proteins were seed storage proteins (vicilin and legumin), molecular chaperones (hsp70, chaperonin-60 alpha subunit; putative protein disulfide isomerase), ATP-dependent Clp protease, ribulose-1,5-bisphophate carboxylase/oxygenase large subunit. Increase in the activities of ROS-scavenging enzymes, less ultrastructural modification, Cd-deposition in dead parts of cells as well as active regulation of different proteins showed Cd-resistant nature of ZMS-49. Nutzungsrecht: Copyright © 2014 Elsevier Ltd. All rights reserved. Plant Proteins - metabolism Soil Pollutants - toxicity Cadmium - toxicity Chlorophyll - metabolism Plant Leaves - drug effects Gossypium - drug effects Plant Leaves - physiology Gossypium - physiology Proteome - drug effects Quiling, He oth Lei, Mei oth Ali, Basharat oth Zhu, S J oth Enthalten in Chemosphere Kidlington, Oxford : Elsevier Science, 1972 120(2015), Seite 309-320 (DE-627)129288586 (DE-600)120089-6 (DE-576)014470187 0045-6535 nnns volume:120 year:2015 pages:309-320 http://dx.doi.org/10.1016/j.chemosphere.2014.07.060 Volltext http://www.ncbi.nlm.nih.gov/pubmed/25169734 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-UMW SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-GEO SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-GGO GBV_ILN_21 GBV_ILN_70 GBV_ILN_4012 AR 10100 38.32 AVZ 35.00 AVZ AR 120 2015 309-320 |
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10.1016/j.chemosphere.2014.07.060 doi PQ20160617 (DE-627)OLC1963058674 (DE-599)GBVOLC1963058674 (PRQ)c1333-8a8eeda27af36f3f4b64a21c634ad924ad30110ca263d549bf5240e459457af70 (KEY)0012464820150000120000000309ultrastructuralmetabolicandproteomicchangesinleave DE-627 ger DE-627 rakwb eng 333.7 DNB AR 10100 AVZ rvk 38.32 bkl 35.00 bkl Daud, M K verfasserin aut Ultrastructural, metabolic and proteomic changes in leaves of upland cotton in response to cadmium stress 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Present study explores physiological, biochemical and proteomic changes in leaves of upland cotton (ZMS-49) using 500 μM cadmium (Cd) along with control. Leaves' biomass and chlorophyll pigments decreased at 500 μM Cd. Cd contents in roots were higher than leaves. Levels of ROS ( [Formula: see text] and H2O2) both in vivo and in vitro and MDA contents were significantly increased. Chlorophyll parameters (F0, Fm, Fm(') and Fv/Fm), total soluble protein contents and APX showed a decline at 500 μM Cd. SOD, CAT and POD and GR activities significantly enhanced. Less ultrastructural alterations in leaves under Cd stress could be observed. Scanning micrographs at 500 μM Cd possessed less number of stomata as well as near absence of closed stomata. Cd could be located in cell wall, vacuoles and intracellular spaces. Important upregulated proteins were methionine synthase, ribulose 1,5-bisphosphate carboxylase, apoplastic anionic guaiacol peroxidase, glyceraldehydes-3-phosphate dehydrogenase (chloroplastic isoform) and ATP synthase D chain, (mitochondrial). Important downregulated proteins were seed storage proteins (vicilin and legumin), molecular chaperones (hsp70, chaperonin-60 alpha subunit; putative protein disulfide isomerase), ATP-dependent Clp protease, ribulose-1,5-bisphophate carboxylase/oxygenase large subunit. Increase in the activities of ROS-scavenging enzymes, less ultrastructural modification, Cd-deposition in dead parts of cells as well as active regulation of different proteins showed Cd-resistant nature of ZMS-49. Nutzungsrecht: Copyright © 2014 Elsevier Ltd. All rights reserved. Plant Proteins - metabolism Soil Pollutants - toxicity Cadmium - toxicity Chlorophyll - metabolism Plant Leaves - drug effects Gossypium - drug effects Plant Leaves - physiology Gossypium - physiology Proteome - drug effects Quiling, He oth Lei, Mei oth Ali, Basharat oth Zhu, S J oth Enthalten in Chemosphere Kidlington, Oxford : Elsevier Science, 1972 120(2015), Seite 309-320 (DE-627)129288586 (DE-600)120089-6 (DE-576)014470187 0045-6535 nnns volume:120 year:2015 pages:309-320 http://dx.doi.org/10.1016/j.chemosphere.2014.07.060 Volltext http://www.ncbi.nlm.nih.gov/pubmed/25169734 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-UMW SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-GEO SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-GGO GBV_ILN_21 GBV_ILN_70 GBV_ILN_4012 AR 10100 38.32 AVZ 35.00 AVZ AR 120 2015 309-320 |
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10.1016/j.chemosphere.2014.07.060 doi PQ20160617 (DE-627)OLC1963058674 (DE-599)GBVOLC1963058674 (PRQ)c1333-8a8eeda27af36f3f4b64a21c634ad924ad30110ca263d549bf5240e459457af70 (KEY)0012464820150000120000000309ultrastructuralmetabolicandproteomicchangesinleave DE-627 ger DE-627 rakwb eng 333.7 DNB AR 10100 AVZ rvk 38.32 bkl 35.00 bkl Daud, M K verfasserin aut Ultrastructural, metabolic and proteomic changes in leaves of upland cotton in response to cadmium stress 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Present study explores physiological, biochemical and proteomic changes in leaves of upland cotton (ZMS-49) using 500 μM cadmium (Cd) along with control. Leaves' biomass and chlorophyll pigments decreased at 500 μM Cd. Cd contents in roots were higher than leaves. Levels of ROS ( [Formula: see text] and H2O2) both in vivo and in vitro and MDA contents were significantly increased. Chlorophyll parameters (F0, Fm, Fm(') and Fv/Fm), total soluble protein contents and APX showed a decline at 500 μM Cd. SOD, CAT and POD and GR activities significantly enhanced. Less ultrastructural alterations in leaves under Cd stress could be observed. Scanning micrographs at 500 μM Cd possessed less number of stomata as well as near absence of closed stomata. Cd could be located in cell wall, vacuoles and intracellular spaces. Important upregulated proteins were methionine synthase, ribulose 1,5-bisphosphate carboxylase, apoplastic anionic guaiacol peroxidase, glyceraldehydes-3-phosphate dehydrogenase (chloroplastic isoform) and ATP synthase D chain, (mitochondrial). Important downregulated proteins were seed storage proteins (vicilin and legumin), molecular chaperones (hsp70, chaperonin-60 alpha subunit; putative protein disulfide isomerase), ATP-dependent Clp protease, ribulose-1,5-bisphophate carboxylase/oxygenase large subunit. Increase in the activities of ROS-scavenging enzymes, less ultrastructural modification, Cd-deposition in dead parts of cells as well as active regulation of different proteins showed Cd-resistant nature of ZMS-49. Nutzungsrecht: Copyright © 2014 Elsevier Ltd. All rights reserved. Plant Proteins - metabolism Soil Pollutants - toxicity Cadmium - toxicity Chlorophyll - metabolism Plant Leaves - drug effects Gossypium - drug effects Plant Leaves - physiology Gossypium - physiology Proteome - drug effects Quiling, He oth Lei, Mei oth Ali, Basharat oth Zhu, S J oth Enthalten in Chemosphere Kidlington, Oxford : Elsevier Science, 1972 120(2015), Seite 309-320 (DE-627)129288586 (DE-600)120089-6 (DE-576)014470187 0045-6535 nnns volume:120 year:2015 pages:309-320 http://dx.doi.org/10.1016/j.chemosphere.2014.07.060 Volltext http://www.ncbi.nlm.nih.gov/pubmed/25169734 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-UMW SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-GEO SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-GGO GBV_ILN_21 GBV_ILN_70 GBV_ILN_4012 AR 10100 38.32 AVZ 35.00 AVZ AR 120 2015 309-320 |
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10.1016/j.chemosphere.2014.07.060 doi PQ20160617 (DE-627)OLC1963058674 (DE-599)GBVOLC1963058674 (PRQ)c1333-8a8eeda27af36f3f4b64a21c634ad924ad30110ca263d549bf5240e459457af70 (KEY)0012464820150000120000000309ultrastructuralmetabolicandproteomicchangesinleave DE-627 ger DE-627 rakwb eng 333.7 DNB AR 10100 AVZ rvk 38.32 bkl 35.00 bkl Daud, M K verfasserin aut Ultrastructural, metabolic and proteomic changes in leaves of upland cotton in response to cadmium stress 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Present study explores physiological, biochemical and proteomic changes in leaves of upland cotton (ZMS-49) using 500 μM cadmium (Cd) along with control. Leaves' biomass and chlorophyll pigments decreased at 500 μM Cd. Cd contents in roots were higher than leaves. Levels of ROS ( [Formula: see text] and H2O2) both in vivo and in vitro and MDA contents were significantly increased. Chlorophyll parameters (F0, Fm, Fm(') and Fv/Fm), total soluble protein contents and APX showed a decline at 500 μM Cd. SOD, CAT and POD and GR activities significantly enhanced. Less ultrastructural alterations in leaves under Cd stress could be observed. Scanning micrographs at 500 μM Cd possessed less number of stomata as well as near absence of closed stomata. Cd could be located in cell wall, vacuoles and intracellular spaces. Important upregulated proteins were methionine synthase, ribulose 1,5-bisphosphate carboxylase, apoplastic anionic guaiacol peroxidase, glyceraldehydes-3-phosphate dehydrogenase (chloroplastic isoform) and ATP synthase D chain, (mitochondrial). Important downregulated proteins were seed storage proteins (vicilin and legumin), molecular chaperones (hsp70, chaperonin-60 alpha subunit; putative protein disulfide isomerase), ATP-dependent Clp protease, ribulose-1,5-bisphophate carboxylase/oxygenase large subunit. Increase in the activities of ROS-scavenging enzymes, less ultrastructural modification, Cd-deposition in dead parts of cells as well as active regulation of different proteins showed Cd-resistant nature of ZMS-49. Nutzungsrecht: Copyright © 2014 Elsevier Ltd. All rights reserved. Plant Proteins - metabolism Soil Pollutants - toxicity Cadmium - toxicity Chlorophyll - metabolism Plant Leaves - drug effects Gossypium - drug effects Plant Leaves - physiology Gossypium - physiology Proteome - drug effects Quiling, He oth Lei, Mei oth Ali, Basharat oth Zhu, S J oth Enthalten in Chemosphere Kidlington, Oxford : Elsevier Science, 1972 120(2015), Seite 309-320 (DE-627)129288586 (DE-600)120089-6 (DE-576)014470187 0045-6535 nnns volume:120 year:2015 pages:309-320 http://dx.doi.org/10.1016/j.chemosphere.2014.07.060 Volltext http://www.ncbi.nlm.nih.gov/pubmed/25169734 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-UMW SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-GEO SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-GGO GBV_ILN_21 GBV_ILN_70 GBV_ILN_4012 AR 10100 38.32 AVZ 35.00 AVZ AR 120 2015 309-320 |
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10.1016/j.chemosphere.2014.07.060 doi PQ20160617 (DE-627)OLC1963058674 (DE-599)GBVOLC1963058674 (PRQ)c1333-8a8eeda27af36f3f4b64a21c634ad924ad30110ca263d549bf5240e459457af70 (KEY)0012464820150000120000000309ultrastructuralmetabolicandproteomicchangesinleave DE-627 ger DE-627 rakwb eng 333.7 DNB AR 10100 AVZ rvk 38.32 bkl 35.00 bkl Daud, M K verfasserin aut Ultrastructural, metabolic and proteomic changes in leaves of upland cotton in response to cadmium stress 2015 Text txt rdacontent ohne Hilfsmittel zu benutzen n rdamedia Band nc rdacarrier Present study explores physiological, biochemical and proteomic changes in leaves of upland cotton (ZMS-49) using 500 μM cadmium (Cd) along with control. Leaves' biomass and chlorophyll pigments decreased at 500 μM Cd. Cd contents in roots were higher than leaves. Levels of ROS ( [Formula: see text] and H2O2) both in vivo and in vitro and MDA contents were significantly increased. Chlorophyll parameters (F0, Fm, Fm(') and Fv/Fm), total soluble protein contents and APX showed a decline at 500 μM Cd. SOD, CAT and POD and GR activities significantly enhanced. Less ultrastructural alterations in leaves under Cd stress could be observed. Scanning micrographs at 500 μM Cd possessed less number of stomata as well as near absence of closed stomata. Cd could be located in cell wall, vacuoles and intracellular spaces. Important upregulated proteins were methionine synthase, ribulose 1,5-bisphosphate carboxylase, apoplastic anionic guaiacol peroxidase, glyceraldehydes-3-phosphate dehydrogenase (chloroplastic isoform) and ATP synthase D chain, (mitochondrial). Important downregulated proteins were seed storage proteins (vicilin and legumin), molecular chaperones (hsp70, chaperonin-60 alpha subunit; putative protein disulfide isomerase), ATP-dependent Clp protease, ribulose-1,5-bisphophate carboxylase/oxygenase large subunit. Increase in the activities of ROS-scavenging enzymes, less ultrastructural modification, Cd-deposition in dead parts of cells as well as active regulation of different proteins showed Cd-resistant nature of ZMS-49. Nutzungsrecht: Copyright © 2014 Elsevier Ltd. All rights reserved. Plant Proteins - metabolism Soil Pollutants - toxicity Cadmium - toxicity Chlorophyll - metabolism Plant Leaves - drug effects Gossypium - drug effects Plant Leaves - physiology Gossypium - physiology Proteome - drug effects Quiling, He oth Lei, Mei oth Ali, Basharat oth Zhu, S J oth Enthalten in Chemosphere Kidlington, Oxford : Elsevier Science, 1972 120(2015), Seite 309-320 (DE-627)129288586 (DE-600)120089-6 (DE-576)014470187 0045-6535 nnns volume:120 year:2015 pages:309-320 http://dx.doi.org/10.1016/j.chemosphere.2014.07.060 Volltext http://www.ncbi.nlm.nih.gov/pubmed/25169734 GBV_USEFLAG_A SYSFLAG_A GBV_OLC SSG-OLC-UMW SSG-OLC-TEC SSG-OLC-CHE SSG-OLC-GEO SSG-OLC-PHA SSG-OLC-DE-84 SSG-OPC-GGO GBV_ILN_21 GBV_ILN_70 GBV_ILN_4012 AR 10100 38.32 AVZ 35.00 AVZ AR 120 2015 309-320 |
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333.7 DNB AR 10100 AVZ rvk 38.32 bkl 35.00 bkl Ultrastructural, metabolic and proteomic changes in leaves of upland cotton in response to cadmium stress Plant Proteins - metabolism Soil Pollutants - toxicity Cadmium - toxicity Chlorophyll - metabolism Plant Leaves - drug effects Gossypium - drug effects Plant Leaves - physiology Gossypium - physiology Proteome - drug effects |
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ultrastructural, metabolic and proteomic changes in leaves of upland cotton in response to cadmium stress |
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Ultrastructural, metabolic and proteomic changes in leaves of upland cotton in response to cadmium stress |
| abstract |
Present study explores physiological, biochemical and proteomic changes in leaves of upland cotton (ZMS-49) using 500 μM cadmium (Cd) along with control. Leaves' biomass and chlorophyll pigments decreased at 500 μM Cd. Cd contents in roots were higher than leaves. Levels of ROS ( [Formula: see text] and H2O2) both in vivo and in vitro and MDA contents were significantly increased. Chlorophyll parameters (F0, Fm, Fm(') and Fv/Fm), total soluble protein contents and APX showed a decline at 500 μM Cd. SOD, CAT and POD and GR activities significantly enhanced. Less ultrastructural alterations in leaves under Cd stress could be observed. Scanning micrographs at 500 μM Cd possessed less number of stomata as well as near absence of closed stomata. Cd could be located in cell wall, vacuoles and intracellular spaces. Important upregulated proteins were methionine synthase, ribulose 1,5-bisphosphate carboxylase, apoplastic anionic guaiacol peroxidase, glyceraldehydes-3-phosphate dehydrogenase (chloroplastic isoform) and ATP synthase D chain, (mitochondrial). Important downregulated proteins were seed storage proteins (vicilin and legumin), molecular chaperones (hsp70, chaperonin-60 alpha subunit; putative protein disulfide isomerase), ATP-dependent Clp protease, ribulose-1,5-bisphophate carboxylase/oxygenase large subunit. Increase in the activities of ROS-scavenging enzymes, less ultrastructural modification, Cd-deposition in dead parts of cells as well as active regulation of different proteins showed Cd-resistant nature of ZMS-49. |
| abstractGer |
Present study explores physiological, biochemical and proteomic changes in leaves of upland cotton (ZMS-49) using 500 μM cadmium (Cd) along with control. Leaves' biomass and chlorophyll pigments decreased at 500 μM Cd. Cd contents in roots were higher than leaves. Levels of ROS ( [Formula: see text] and H2O2) both in vivo and in vitro and MDA contents were significantly increased. Chlorophyll parameters (F0, Fm, Fm(') and Fv/Fm), total soluble protein contents and APX showed a decline at 500 μM Cd. SOD, CAT and POD and GR activities significantly enhanced. Less ultrastructural alterations in leaves under Cd stress could be observed. Scanning micrographs at 500 μM Cd possessed less number of stomata as well as near absence of closed stomata. Cd could be located in cell wall, vacuoles and intracellular spaces. Important upregulated proteins were methionine synthase, ribulose 1,5-bisphosphate carboxylase, apoplastic anionic guaiacol peroxidase, glyceraldehydes-3-phosphate dehydrogenase (chloroplastic isoform) and ATP synthase D chain, (mitochondrial). Important downregulated proteins were seed storage proteins (vicilin and legumin), molecular chaperones (hsp70, chaperonin-60 alpha subunit; putative protein disulfide isomerase), ATP-dependent Clp protease, ribulose-1,5-bisphophate carboxylase/oxygenase large subunit. Increase in the activities of ROS-scavenging enzymes, less ultrastructural modification, Cd-deposition in dead parts of cells as well as active regulation of different proteins showed Cd-resistant nature of ZMS-49. |
| abstract_unstemmed |
Present study explores physiological, biochemical and proteomic changes in leaves of upland cotton (ZMS-49) using 500 μM cadmium (Cd) along with control. Leaves' biomass and chlorophyll pigments decreased at 500 μM Cd. Cd contents in roots were higher than leaves. Levels of ROS ( [Formula: see text] and H2O2) both in vivo and in vitro and MDA contents were significantly increased. Chlorophyll parameters (F0, Fm, Fm(') and Fv/Fm), total soluble protein contents and APX showed a decline at 500 μM Cd. SOD, CAT and POD and GR activities significantly enhanced. Less ultrastructural alterations in leaves under Cd stress could be observed. Scanning micrographs at 500 μM Cd possessed less number of stomata as well as near absence of closed stomata. Cd could be located in cell wall, vacuoles and intracellular spaces. Important upregulated proteins were methionine synthase, ribulose 1,5-bisphosphate carboxylase, apoplastic anionic guaiacol peroxidase, glyceraldehydes-3-phosphate dehydrogenase (chloroplastic isoform) and ATP synthase D chain, (mitochondrial). Important downregulated proteins were seed storage proteins (vicilin and legumin), molecular chaperones (hsp70, chaperonin-60 alpha subunit; putative protein disulfide isomerase), ATP-dependent Clp protease, ribulose-1,5-bisphophate carboxylase/oxygenase large subunit. Increase in the activities of ROS-scavenging enzymes, less ultrastructural modification, Cd-deposition in dead parts of cells as well as active regulation of different proteins showed Cd-resistant nature of ZMS-49. |
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| title_short |
Ultrastructural, metabolic and proteomic changes in leaves of upland cotton in response to cadmium stress |
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Leaves' biomass and chlorophyll pigments decreased at 500 μM Cd. Cd contents in roots were higher than leaves. Levels of ROS ( [Formula: see text] and H2O2) both in vivo and in vitro and MDA contents were significantly increased. Chlorophyll parameters (F0, Fm, Fm(') and Fv/Fm), total soluble protein contents and APX showed a decline at 500 μM Cd. SOD, CAT and POD and GR activities significantly enhanced. Less ultrastructural alterations in leaves under Cd stress could be observed. Scanning micrographs at 500 μM Cd possessed less number of stomata as well as near absence of closed stomata. Cd could be located in cell wall, vacuoles and intracellular spaces. Important upregulated proteins were methionine synthase, ribulose 1,5-bisphosphate carboxylase, apoplastic anionic guaiacol peroxidase, glyceraldehydes-3-phosphate dehydrogenase (chloroplastic isoform) and ATP synthase D chain, (mitochondrial). Important downregulated proteins were seed storage proteins (vicilin and legumin), molecular chaperones (hsp70, chaperonin-60 alpha subunit; putative protein disulfide isomerase), ATP-dependent Clp protease, ribulose-1,5-bisphophate carboxylase/oxygenase large subunit. Increase in the activities of ROS-scavenging enzymes, less ultrastructural modification, Cd-deposition in dead parts of cells as well as active regulation of different proteins showed Cd-resistant nature of ZMS-49.</subfield></datafield><datafield tag="540" ind1=" " ind2=" "><subfield code="a">Nutzungsrecht: Copyright © 2014 Elsevier Ltd. 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