LIVIVO - The Search Portal for Life Sciences

zur deutschen Oberfläche wechseln
Advanced search

Search results

Result 1 - 5 of total 5

Search options

  1. Article ; Online: Nutrient-dependent acetylation controls basic regulatory metabolic switches and cellular reprogramming.

    Dominy, J E / Gerhart-Hines, Z / Puigserver, P

    Cold Spring Harbor symposia on quantitative biology

    2012  Volume 76, Page(s) 203–209

    Abstract: Organisms must be able to selectively tailor their ability to use the macronutrients of carbohydrate, protein, and fat based on their availability. In different cell types, how the nutrient fluctuations are sensed and the mechanisms by which the pathways ...

    Abstract Organisms must be able to selectively tailor their ability to use the macronutrients of carbohydrate, protein, and fat based on their availability. In different cell types, how the nutrient fluctuations are sensed and the mechanisms by which the pathways of central metabolism are switched to favor the use of one particular nutrient type over another are topics of intense interest. Protein acetylation is one major evolutionary conserved mechanism by which nutrient fluctuations are sensed within cells and subsequently coupled with metabolic switching. In this review, we present the case of PGC-1α acetylation and how the control of PGC-1α's activity by acetylation sets into motion a wide range of metabolic adaptations that makes this protein an exemplary model for acetylation-mediated mechanisms of nutrient sensing and communication.
    MeSH term(s) Acetylation ; Animals ; Biological Evolution ; Cells/metabolism ; Food ; Humans ; Metabolic Networks and Pathways/genetics ; Signal Transduction/genetics ; Transcription Factors/metabolism
    Chemical Substances Transcription Factors ; peroxisome-proliferator-activated receptor-gamma coactivator-1
    Language English
    Publishing date 2012-02-27
    Publishing country United States
    Document type Journal Article ; Review
    ISSN 1943-4456 ; 0091-7451
    ISSN (online) 1943-4456
    ISSN 0091-7451
    DOI 10.1101/sqb.2012.76.010843
    Database MEDical Literature Analysis and Retrieval System OnLINE

    More links

    Kategorien

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  2. Article: Surprising insights that aren't so surprising in the modeling of sulfur amino acid metabolism.

    Stipanuk, M H / Dominy, J E

    Amino acids

    2006  Volume 30, Issue 3, Page(s) 251–256

    Abstract: The modeling of whole organism sulfur amino acid flux control has been aided in recent years by advancements in proteomics and mass spectroscopy-based metabolite analysis. The convergence of these two fields and their respective techniques, as ... ...

    Abstract The modeling of whole organism sulfur amino acid flux control has been aided in recent years by advancements in proteomics and mass spectroscopy-based metabolite analysis. The convergence of these two fields and their respective techniques, as demonstrated by a new study using yeast by Lafaye et al., has shown that researchers seeking to model whole cell/organism metabolism should give careful consideration to the relationships connecting enzyme concentration, enzyme activity, substrate concentration, and metabolic flux. In this paper, we outline some of the fundamental concepts for modeling sulfur amino acid metabolism and how they relate to our current understanding of mammalian sulfur amino acid metabolism.
    MeSH term(s) Amino Acids, Sulfur/metabolism ; Animals ; Humans ; Models, Biological ; Saccharomyces cerevisiae/metabolism
    Chemical Substances Amino Acids, Sulfur
    Language English
    Publishing date 2006-05
    Publishing country Austria
    Document type Journal Article ; Review
    ZDB-ID 1121341-3
    ISSN 1438-2199 ; 0939-4451
    ISSN (online) 1438-2199
    ISSN 0939-4451
    DOI 10.1007/s00726-005-0288-4
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 3490: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  3. Article: New roles for cystine and transsulfuration enzymes: production of H2S, a neuromodulator and smooth muscle relaxant

    Dominy, J.E / Stipanuk, M.H

    Nutrition reviews. 2004 Sept., v. 62, no. 9

    2004  

    Abstract: The enzymes of the transsulfuration pathway also have the capacity to catalyze the desulfhydration of cysteine. Recent studies demonstrate a role of the transsulfuration enzymes, cystathionine gamma-lyase and cystathionine beta-synthase, in catalyzing ... ...

    Abstract The enzymes of the transsulfuration pathway also have the capacity to catalyze the desulfhydration of cysteine. Recent studies demonstrate a role of the transsulfuration enzymes, cystathionine gamma-lyase and cystathionine beta-synthase, in catalyzing the desulfhydration of cysteine in brain and smooth muscle. The H2S produced from cysteine functions as a neuromodulator and smooth muscle relaxant. In glutamatergic neurons, the production of H2S by cystathionine beta-synthase enhances N-methyl-Daspartate (NMDA) receptor-mediated currents. In smooth muscle cells, H2S produced by cystathionine gamma-lyase enhances the outward flux of potassium by opening potassium channels, leading to hyperpolarization of membrane potential and smooth muscle relaxation.
    Keywords sulfur amino acids ; biochemical pathways ; enzymes ; hydrogen sulfide ; calmodulin ; cystathionine beta-synthase ; cystathionine gamma-lyase
    Language English
    Dates of publication 2004-09
    Size p. 348-353.
    Document type Article
    ZDB-ID 82067-2
    ISSN 1753-4887 ; 0029-6643
    ISSN (online) 1753-4887
    ISSN 0029-6643
    Database NAL-Catalogue (AGRICOLA)

    More links

    Kategorien

    In stock of ZB MED Bonn / Germany

    Z 2497: Show issues
    Z 4' 63/93: Show issues
    Z 2497 a: Show issues

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

    Inter-library loan at ZB MED

    Your chosen title can be delivered directly to ZB MED Cologne location if you are registered as a user at ZB MED Cologne.

  4. Article: Cysteine dioxygenase: a robust system for regulation of cellular cysteine levels

    Stipanuk, M. H / Ueki, I / Dominy, J. E. Jr / Simmons, C. R / Hirschberger, L. L

    Amino acids. 2009 May, v. 37, no. 1

    2009  

    Abstract: Cysteine catabolism in mammals is dependent upon cysteine dioxygenase (CDO), an enzyme that adds molecular oxygen to the sulfur of cysteine, converting the thiol to a sulfinic acid known as cysteinesulfinic acid (3-sulfinoalanine). CDO is one of the most ...

    Abstract Cysteine catabolism in mammals is dependent upon cysteine dioxygenase (CDO), an enzyme that adds molecular oxygen to the sulfur of cysteine, converting the thiol to a sulfinic acid known as cysteinesulfinic acid (3-sulfinoalanine). CDO is one of the most highly regulated metabolic enzymes responding to diet that is known. It undergoes up to 45-fold changes in concentration and up to 10-fold changes in catalytic efficiency. This provides a remarkable responsiveness of the cell to changes in sulfur amino acid availability: the ability to decrease CDO activity and conserve cysteine when cysteine is scarce and to rapidly increase CDO activity and catabolize cysteine to prevent cytotoxicity when cysteine supply is abundant. CDO in both liver and adipose tissues responds to changes in dietary intakes of protein and/or sulfur amino acids over a range that encompasses the requirement level, suggesting that cysteine homeostasis is very important to the living organism.
    Language English
    Dates of publication 2009-05
    Size p. 55-63.
    Publisher Springer Vienna
    Publishing place Vienna
    Document type Article
    ZDB-ID 1121341-3
    ISSN 1438-2199 ; 0939-4451
    ISSN (online) 1438-2199
    ISSN 0939-4451
    DOI 10.1007/s00726-008-0202-y
    Database NAL-Catalogue (AGRICOLA)

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 3490: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

  5. Article ; Online: Cysteine dioxygenase: a robust system for regulation of cellular cysteine levels.

    Stipanuk, M H / Ueki, I / Dominy, J E / Simmons, C R / Hirschberger, L L

    Amino acids

    2008  Volume 37, Issue 1, Page(s) 55–63

    Abstract: Cysteine catabolism in mammals is dependent upon cysteine dioxygenase (CDO), an enzyme that adds molecular oxygen to the sulfur of cysteine, converting the thiol to a sulfinic acid known as cysteinesulfinic acid (3-sulfinoalanine). CDO is one of the most ...

    Abstract Cysteine catabolism in mammals is dependent upon cysteine dioxygenase (CDO), an enzyme that adds molecular oxygen to the sulfur of cysteine, converting the thiol to a sulfinic acid known as cysteinesulfinic acid (3-sulfinoalanine). CDO is one of the most highly regulated metabolic enzymes responding to diet that is known. It undergoes up to 45-fold changes in concentration and up to 10-fold changes in catalytic efficiency. This provides a remarkable responsiveness of the cell to changes in sulfur amino acid availability: the ability to decrease CDO activity and conserve cysteine when cysteine is scarce and to rapidly increase CDO activity and catabolize cysteine to prevent cytotoxicity when cysteine supply is abundant. CDO in both liver and adipose tissues responds to changes in dietary intakes of protein and/or sulfur amino acids over a range that encompasses the requirement level, suggesting that cysteine homeostasis is very important to the living organism.
    MeSH term(s) Adipose Tissue/cytology ; Adipose Tissue/enzymology ; Adipose Tissue/metabolism ; Animals ; Cysteine/metabolism ; Cysteine Dioxygenase/metabolism ; Duodenum/cytology ; Duodenum/enzymology ; Duodenum/metabolism ; Homeostasis/physiology ; Kidney/cytology ; Kidney/enzymology ; Kidney/metabolism ; Liver/cytology ; Liver/enzymology ; Liver/metabolism ; Pancreas/cytology ; Pancreas/enzymology ; Pancreas/metabolism
    Chemical Substances Cysteine Dioxygenase (EC 1.13.11.20) ; Cysteine (K848JZ4886)
    Language English
    Publishing date 2008-11-15
    Publishing country Austria
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 1121341-3
    ISSN 1438-2199 ; 0939-4451
    ISSN (online) 1438-2199
    ISSN 0939-4451
    DOI 10.1007/s00726-008-0202-y
    Database MEDical Literature Analysis and Retrieval System OnLINE

    Full text online

    More links

    Kategorien

    In stock of ZB MED Cologne/Königswinter

    Zs.A 3490: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

    Order via subito

    This service is chargeable due to the Delivery terms set by subito. Orders including an article and supplementary material will be classified as separate orders. In these cases, fees will be demanded for each order.

To top