The Experts below are selected from a list of 240 Experts worldwide ranked by ideXlab platform
Rajinder S. Dhindsa - One of the best experts on this subject based on the ideXlab platform.
-
cold induced changes in freezing tolerance Protein Phosphorylation and gene expression evidence for a role of calcium
Plant Physiology, 1993Co-Authors: Antonio F. Monroy, Fathey Sarhan, Rajinder S. DhindsaAbstract:The role of Ca2+ in cold-induced changes in Protein Phosphorylation, gene expression, and development of freezing tolerance has been studied in cell-suspension cultures of a freezing-tolerant cultivar of alfalfa (Medicago sativa spp. falcata cv Anik). Chemical treatments to block Ca2+ channels, antagonize calmodulin action, or inhibit Protein kinases markedly inhibited the cellular capacity to develop cold-induced freezing tolerance but had little effect on cell viability. An analysis of phosphoProtein profile by two-dimensional polyacrylamide gel electrophoresis revealed that at low temperature the relative level of Phosphorylation of several Proteins increased, whereas that of several others decreased. When cold acclimation was carried out in the presence of N-(6-aminohexyl)-5-chloro-1-naphthalene-sulfonamide hydrochloride, an antagonist of calmodulin and Ca2+-dependent Protein kinases, or the Ca2+ channel blocker La3+, the cold-induced changes in Protein Phosphorylation were strongly inhibited, cells lost their capacity to develop freezing tolerance, and accumulation of transcripts of cold acclimation-specific genes was substantially reduced. An inhibitor of Protein kinases, 1-(5-isoquinolinesulfonyl)-2-methylpiperazine dihydrochloride, had less pronounced effects on the cold-induced Protein Phosphorylation and caused only a partial inhibition of the cold-induced development of freezing tolerance and accumulation of the transcripts. The level of Phosphorylation of one Protein, of about 15 kD, increased more than 10-fold at low temperature and showed a strong positive correlation with cold-induced freezing tolerance and gene expression even when the latter were altered with various chemical treatments. These results suggest that Ca2+ and Protein Phosphorylation, or perhaps a coupling of the two, play an important role during the acquisition of freezing tolerance during cold acclimation.
-
Cold-lnduced Changes in Freezing Tolerance, Protein Phosphorylation, and Gene Expression'
1993Co-Authors: Antonio F. Monroy, Fathey Sarhan, Rajinder S. DhindsaAbstract:lhe role of Ca’+ in cold-induced changes in Protein Phosphorylation, gene expression, and development of freezing tolerance has been studied in cell-suspension cultures of a freezing-tolerant cultivar of alfalfa (Medicago safiva spp. falcafa cv Anik). Chemical treatments to block Caz+ channels, antagonize calmodulin action, or inhibit Protein kinases markedly inhibited the cellular capacity to develop cold-induced freezing tolerance but had little effect on cell viability. An analysis of phosphoProtein profile by two-dimensional polyacrylamide gel electrophoresis revealed that at low temperature the relative level of Phosphorylation of several Proteins increased, whereas that of several others decreased. When cold acclimation was carried out in the presence of M(6-aminohexyl)-5-chloro-l-naphthalene-sulfonamide hydrochloride, an antagonist of calmodulin and ca’+-dependent Protein kinases, or the CaZ+ channel blocker La3+, the cold-induced changes in Protein Phosphorylation were strongly inhibited, cells lost their capacity to develop freezing tolerance, and accumulation of transcripts of cold acclimation-specific genes was substantially reduced. An inhibitor of Protein kinases, 1-(5-isoquinolinesulfonyl)-2-methylpiperazine dihydrochloride, had less pronounced effects on the cold-induced Protein Phosphorylation and caused only a partia1 inhibition of the cold-induced development of freezing tolerance and accumulation of the transcripts. lhe level of Phosphorylation of one Protein, of about 15 kD, increased more than 10-fold at low temperature and showed a strong positive correlation with cold-induced freezing tolerance and gene expression even when the latter were altered with various chemical treatments. lhese results suggest that CaZ+ and Protein Phosphorylation, or perhaps a coupling of the two, play an important role during the acquisition of freezing tolerance during cold acclimation.
Antonio F. Monroy - One of the best experts on this subject based on the ideXlab platform.
-
cold induced changes in freezing tolerance Protein Phosphorylation and gene expression evidence for a role of calcium
Plant Physiology, 1993Co-Authors: Antonio F. Monroy, Fathey Sarhan, Rajinder S. DhindsaAbstract:The role of Ca2+ in cold-induced changes in Protein Phosphorylation, gene expression, and development of freezing tolerance has been studied in cell-suspension cultures of a freezing-tolerant cultivar of alfalfa (Medicago sativa spp. falcata cv Anik). Chemical treatments to block Ca2+ channels, antagonize calmodulin action, or inhibit Protein kinases markedly inhibited the cellular capacity to develop cold-induced freezing tolerance but had little effect on cell viability. An analysis of phosphoProtein profile by two-dimensional polyacrylamide gel electrophoresis revealed that at low temperature the relative level of Phosphorylation of several Proteins increased, whereas that of several others decreased. When cold acclimation was carried out in the presence of N-(6-aminohexyl)-5-chloro-1-naphthalene-sulfonamide hydrochloride, an antagonist of calmodulin and Ca2+-dependent Protein kinases, or the Ca2+ channel blocker La3+, the cold-induced changes in Protein Phosphorylation were strongly inhibited, cells lost their capacity to develop freezing tolerance, and accumulation of transcripts of cold acclimation-specific genes was substantially reduced. An inhibitor of Protein kinases, 1-(5-isoquinolinesulfonyl)-2-methylpiperazine dihydrochloride, had less pronounced effects on the cold-induced Protein Phosphorylation and caused only a partial inhibition of the cold-induced development of freezing tolerance and accumulation of the transcripts. The level of Phosphorylation of one Protein, of about 15 kD, increased more than 10-fold at low temperature and showed a strong positive correlation with cold-induced freezing tolerance and gene expression even when the latter were altered with various chemical treatments. These results suggest that Ca2+ and Protein Phosphorylation, or perhaps a coupling of the two, play an important role during the acquisition of freezing tolerance during cold acclimation.
-
Cold-lnduced Changes in Freezing Tolerance, Protein Phosphorylation, and Gene Expression'
1993Co-Authors: Antonio F. Monroy, Fathey Sarhan, Rajinder S. DhindsaAbstract:lhe role of Ca’+ in cold-induced changes in Protein Phosphorylation, gene expression, and development of freezing tolerance has been studied in cell-suspension cultures of a freezing-tolerant cultivar of alfalfa (Medicago safiva spp. falcafa cv Anik). Chemical treatments to block Caz+ channels, antagonize calmodulin action, or inhibit Protein kinases markedly inhibited the cellular capacity to develop cold-induced freezing tolerance but had little effect on cell viability. An analysis of phosphoProtein profile by two-dimensional polyacrylamide gel electrophoresis revealed that at low temperature the relative level of Phosphorylation of several Proteins increased, whereas that of several others decreased. When cold acclimation was carried out in the presence of M(6-aminohexyl)-5-chloro-l-naphthalene-sulfonamide hydrochloride, an antagonist of calmodulin and ca’+-dependent Protein kinases, or the CaZ+ channel blocker La3+, the cold-induced changes in Protein Phosphorylation were strongly inhibited, cells lost their capacity to develop freezing tolerance, and accumulation of transcripts of cold acclimation-specific genes was substantially reduced. An inhibitor of Protein kinases, 1-(5-isoquinolinesulfonyl)-2-methylpiperazine dihydrochloride, had less pronounced effects on the cold-induced Protein Phosphorylation and caused only a partia1 inhibition of the cold-induced development of freezing tolerance and accumulation of the transcripts. lhe level of Phosphorylation of one Protein, of about 15 kD, increased more than 10-fold at low temperature and showed a strong positive correlation with cold-induced freezing tolerance and gene expression even when the latter were altered with various chemical treatments. lhese results suggest that CaZ+ and Protein Phosphorylation, or perhaps a coupling of the two, play an important role during the acquisition of freezing tolerance during cold acclimation.
Matthias Mann - One of the best experts on this subject based on the ideXlab platform.
-
Protein Phosphorylation a major switch mechanism for metabolic regulation
Trends in Endocrinology and Metabolism, 2015Co-Authors: Sean J Humphrey, David E James, Matthias MannAbstract:Metabolism research is undergoing a renaissance because many diseases are increasingly recognized as being characterized by perturbations in intracellular metabolic regulation. Metabolic changes can be conferred through changes to the expression of metabolic enzymes, the concentrations of substrates or products that govern reaction kinetics, or post-translational modification (PTM) of the Proteins that facilitate these reactions. On the 60th anniversary since its discovery, reversible Protein Phosphorylation is widely appreciated as an essential PTM regulating metabolism. With the ability to quantitatively measure dynamic changes in Protein Phosphorylation on a global scale – hereafter referred to as phosphoproteomics – we are now entering a new era in metabolism research, with mass spectrometry (MS)-based proteomics at the helm.
-
analysis of Protein Phosphorylation using mass spectrometry deciphering the phosphoproteome
Trends in Biotechnology, 2002Co-Authors: Matthias Mann, Ole Nørregaard Jensen, Mads Gronborg, Hanno Steen, Akhilesh PandeyAbstract:In signal transduction in eukaryotes, Protein Phosphorylation is a key event. To understand signaling processes, we must first acquire an inventory of phosphoProteins and their Phosphorylation sites under different conditions. Because Phosphorylation is a dynamic process, elucidation of signaling networks also requires quantitation of these Phosphorylation events. In this article, we outline several methods for enrichment of phosphorylated Proteins and peptides and discuss various options for their identification and quantitation with special emphasis on mass spectrometry-based techniques.
Fathey Sarhan - One of the best experts on this subject based on the ideXlab platform.
-
cold induced changes in freezing tolerance Protein Phosphorylation and gene expression evidence for a role of calcium
Plant Physiology, 1993Co-Authors: Antonio F. Monroy, Fathey Sarhan, Rajinder S. DhindsaAbstract:The role of Ca2+ in cold-induced changes in Protein Phosphorylation, gene expression, and development of freezing tolerance has been studied in cell-suspension cultures of a freezing-tolerant cultivar of alfalfa (Medicago sativa spp. falcata cv Anik). Chemical treatments to block Ca2+ channels, antagonize calmodulin action, or inhibit Protein kinases markedly inhibited the cellular capacity to develop cold-induced freezing tolerance but had little effect on cell viability. An analysis of phosphoProtein profile by two-dimensional polyacrylamide gel electrophoresis revealed that at low temperature the relative level of Phosphorylation of several Proteins increased, whereas that of several others decreased. When cold acclimation was carried out in the presence of N-(6-aminohexyl)-5-chloro-1-naphthalene-sulfonamide hydrochloride, an antagonist of calmodulin and Ca2+-dependent Protein kinases, or the Ca2+ channel blocker La3+, the cold-induced changes in Protein Phosphorylation were strongly inhibited, cells lost their capacity to develop freezing tolerance, and accumulation of transcripts of cold acclimation-specific genes was substantially reduced. An inhibitor of Protein kinases, 1-(5-isoquinolinesulfonyl)-2-methylpiperazine dihydrochloride, had less pronounced effects on the cold-induced Protein Phosphorylation and caused only a partial inhibition of the cold-induced development of freezing tolerance and accumulation of the transcripts. The level of Phosphorylation of one Protein, of about 15 kD, increased more than 10-fold at low temperature and showed a strong positive correlation with cold-induced freezing tolerance and gene expression even when the latter were altered with various chemical treatments. These results suggest that Ca2+ and Protein Phosphorylation, or perhaps a coupling of the two, play an important role during the acquisition of freezing tolerance during cold acclimation.
-
Cold-lnduced Changes in Freezing Tolerance, Protein Phosphorylation, and Gene Expression'
1993Co-Authors: Antonio F. Monroy, Fathey Sarhan, Rajinder S. DhindsaAbstract:lhe role of Ca’+ in cold-induced changes in Protein Phosphorylation, gene expression, and development of freezing tolerance has been studied in cell-suspension cultures of a freezing-tolerant cultivar of alfalfa (Medicago safiva spp. falcafa cv Anik). Chemical treatments to block Caz+ channels, antagonize calmodulin action, or inhibit Protein kinases markedly inhibited the cellular capacity to develop cold-induced freezing tolerance but had little effect on cell viability. An analysis of phosphoProtein profile by two-dimensional polyacrylamide gel electrophoresis revealed that at low temperature the relative level of Phosphorylation of several Proteins increased, whereas that of several others decreased. When cold acclimation was carried out in the presence of M(6-aminohexyl)-5-chloro-l-naphthalene-sulfonamide hydrochloride, an antagonist of calmodulin and ca’+-dependent Protein kinases, or the CaZ+ channel blocker La3+, the cold-induced changes in Protein Phosphorylation were strongly inhibited, cells lost their capacity to develop freezing tolerance, and accumulation of transcripts of cold acclimation-specific genes was substantially reduced. An inhibitor of Protein kinases, 1-(5-isoquinolinesulfonyl)-2-methylpiperazine dihydrochloride, had less pronounced effects on the cold-induced Protein Phosphorylation and caused only a partia1 inhibition of the cold-induced development of freezing tolerance and accumulation of the transcripts. lhe level of Phosphorylation of one Protein, of about 15 kD, increased more than 10-fold at low temperature and showed a strong positive correlation with cold-induced freezing tolerance and gene expression even when the latter were altered with various chemical treatments. lhese results suggest that CaZ+ and Protein Phosphorylation, or perhaps a coupling of the two, play an important role during the acquisition of freezing tolerance during cold acclimation.
Akhilesh Pandey - One of the best experts on this subject based on the ideXlab platform.
-
analysis of Protein Phosphorylation using mass spectrometry deciphering the phosphoproteome
Trends in Biotechnology, 2002Co-Authors: Matthias Mann, Ole Nørregaard Jensen, Mads Gronborg, Hanno Steen, Akhilesh PandeyAbstract:In signal transduction in eukaryotes, Protein Phosphorylation is a key event. To understand signaling processes, we must first acquire an inventory of phosphoProteins and their Phosphorylation sites under different conditions. Because Phosphorylation is a dynamic process, elucidation of signaling networks also requires quantitation of these Phosphorylation events. In this article, we outline several methods for enrichment of phosphorylated Proteins and peptides and discuss various options for their identification and quantitation with special emphasis on mass spectrometry-based techniques.
