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  1. Article ; Online: Activation of hepatic acetyl-CoA carboxylase by S-nitrosylation in response to diet.

    Venetos, Nicholas M / Stomberski, Colin T / Qian, Zhaoxia / Premont, Richard T / Stamler, Jonathan S

    Journal of lipid research

    2024  , Page(s) 100542

    Abstract: ... administration of a hypercaloric high-fat diet. This results in marked reduction in the amount of S-nitrosylation ... lipogenesis. We further show that ACC S-nitrosylation markedly increases enzymatic activity. Diminished eNOS ... expression and ACC S-nitrosylation may thus represent a physiological adaptation to caloric excess ...

    Abstract Nitric oxide (NO), produced primarily by nitric oxide synthase (NOS) enzymes, is known to influence energy metabolism by stimulating fat uptake and oxidation. The effects of NO on de novo lipogenesis, however, are less clear. Here we demonstrate that hepatic expression of eNOS is reduced following prolonged administration of a hypercaloric high-fat diet. This results in marked reduction in the amount of S-nitrosylation of liver proteins including notably Acetyl-CoA Carboxylase (ACC), the rate-limiting enzyme in de novo lipogenesis. We further show that ACC S-nitrosylation markedly increases enzymatic activity. Diminished eNOS expression and ACC S-nitrosylation may thus represent a physiological adaptation to caloric excess by constraining lipogenesis. Our findings demonstrate that S-nitrosylation of liver proteins is subject to dietary control and suggest that de novo lipogenesis is coupled to dietary and metabolic conditions through ACC S-nitrosylation.
    Language English
    Publishing date 2024-04-17
    Publishing country United States
    Document type Journal Article
    ZDB-ID 80154-9
    ISSN 1539-7262 ; 0022-2275
    ISSN (online) 1539-7262
    ISSN 0022-2275
    DOI 10.1016/j.jlr.2024.100542
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Protocol for preparing Thiopropyl Sepharose resin used for capturing S-nitrosylated proteins.

    Seth, Puneet / Hausladen, Alfred / Premont, Richard T / Stamler, Jonathan S

    STAR protocols

    2023  Volume 4, Issue 4, Page(s) 102430

    Abstract: S-nitrosothiol (SNO)-Resin Assisted Capture (SNO-RAC) relies on a Thiopropyl Sepharose resin ... to identify S-nitrosylated proteins (SNO-proteins) and sites of S-nitrosylation. Here, we present a protocol ...

    Abstract S-nitrosothiol (SNO)-Resin Assisted Capture (SNO-RAC) relies on a Thiopropyl Sepharose resin to identify S-nitrosylated proteins (SNO-proteins) and sites of S-nitrosylation. Here, we present a protocol for preparing Thiopropyl Sepharose resin with efficiency of SNO-protein capture comparable to the discontinued commercial version. We describe steps for amine coupling, disulfide reduction, and generation of thiol reactive resin. We then detail quality control procedures. This resin is also suitable for Acyl-RAC assays to capture palmitoylated proteins. For complete details on the use and execution of the SNO-RAC protocol, please refer to Forrester et al.,
    MeSH term(s) Sepharose ; Proteins/metabolism ; S-Nitrosothiols/metabolism ; Sulfhydryl Compounds
    Chemical Substances Sepharose (9012-36-6) ; Proteins ; S-Nitrosothiols ; Sulfhydryl Compounds
    Language English
    Publishing date 2023-11-04
    Publishing country United States
    Document type Journal Article
    ISSN 2666-1667
    ISSN (online) 2666-1667
    DOI 10.1016/j.xpro.2023.102430
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Essential Role of Hemoglobin βCys93 in Cardiovascular Physiology.

    Premont, Richard T / Stamler, Jonathan S

    Physiology (Bethesda, Md.)

    2020  Volume 35, Issue 4, Page(s) 234–243

    Abstract: The supply of oxygen to tissues is controlled by microcirculatory blood flow. One of the more surprising discoveries in cardiovascular physiology is the critical dependence of microcirculatory blood flow on a single conserved cysteine within the β- ... ...

    Abstract The supply of oxygen to tissues is controlled by microcirculatory blood flow. One of the more surprising discoveries in cardiovascular physiology is the critical dependence of microcirculatory blood flow on a single conserved cysteine within the β-subunit (βCys93) of hemoglobin (Hb). βCys93 is the primary site of Hb
    MeSH term(s) Animals ; Cardiovascular Physiological Phenomena ; Hemodynamics ; Hemoglobins/chemistry ; Hemoglobins/metabolism ; Humans ; Hypoxia/metabolism ; Hypoxia/microbiology ; Hypoxia/pathology ; Microcirculation ; Nitric Oxide/metabolism ; Oxygen/metabolism ; Vasodilation
    Chemical Substances Hemoglobins ; Nitric Oxide (31C4KY9ESH) ; Oxygen (S88TT14065)
    Language English
    Publishing date 2020-08-26
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 2158667-6
    ISSN 1548-9221 ; 1548-9213
    ISSN (online) 1548-9221
    ISSN 1548-9213
    DOI 10.1152/physiol.00040.2019
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Protocol for preparing Thiopropyl Sepharose resin used for capturing S-nitrosylated proteins

    Puneet Seth / Alfred Hausladen / Richard T. Premont / Jonathan S. Stamler

    STAR Protocols, Vol 4, Iss 4, Pp 102430- (2023)

    2023  

    Abstract: Summary: S-nitrosothiol (SNO)-Resin Assisted Capture (SNO-RAC) relies on a Thiopropyl Sepharose ... resin to identify S-nitrosylated proteins (SNO-proteins) and sites of S-nitrosylation. Here, we present ... RAC protocol, please refer to Forrester et al.,1 Fonseca et al.,2 and Seth et al.3 : Publisher’s note ...

    Abstract Summary: S-nitrosothiol (SNO)-Resin Assisted Capture (SNO-RAC) relies on a Thiopropyl Sepharose resin to identify S-nitrosylated proteins (SNO-proteins) and sites of S-nitrosylation. Here, we present a protocol for preparing Thiopropyl Sepharose resin with efficiency of SNO-protein capture comparable to the discontinued commercial version. We describe steps for amine coupling, disulfide reduction, and generation of thiol reactive resin. We then detail quality control procedures. This resin is also suitable for Acyl-RAC assays to capture palmitoylated proteins.For complete details on the use and execution of the SNO-RAC protocol, please refer to Forrester et al.,1 Fonseca et al.,2 and Seth et al.3 : Publisher’s note: Undertaking any experimental protocol requires adherence to local institutional guidelines for laboratory safety and ethics.
    Keywords Signal Transduction ; Protein Biochemistry ; Chemistry ; Science (General) ; Q1-390
    Language English
    Publishing date 2023-12-01T00:00:00Z
    Publisher Elsevier
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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  5. Article ; Online: An optimized protocol for isolation of S-nitrosylated proteins from

    Seth, Puneet / Premont, Richard T / Stamler, Jonathan S

    STAR protocols

    2021  Volume 2, Issue 2, Page(s) 100547

    Abstract: Post-translational modification by S-nitrosylation regulates numerous cellular functions and ... impacts most proteins across phylogeny. We describe a protocol for isolating S-nitrosylated proteins (SNO ...

    Abstract Post-translational modification by S-nitrosylation regulates numerous cellular functions and impacts most proteins across phylogeny. We describe a protocol for isolating S-nitrosylated proteins (SNO-proteins) from
    MeSH term(s) Animals ; Caenorhabditis elegans/chemistry ; Caenorhabditis elegans Proteins/analysis ; Caenorhabditis elegans Proteins/chemistry ; Caenorhabditis elegans Proteins/isolation & purification ; Nitrosation ; Proteome/analysis ; Proteome/chemistry ; Proteome/isolation & purification ; Proteomics/methods ; S-Nitrosothiols
    Chemical Substances Caenorhabditis elegans Proteins ; Proteome ; S-Nitrosothiols
    Language English
    Publishing date 2021-05-19
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ISSN 2666-1667
    ISSN (online) 2666-1667
    DOI 10.1016/j.xpro.2021.100547
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: The manifold roles of protein S-nitrosylation in the life of insulin.

    Zhou, Hua-Lin / Premont, Richard T / Stamler, Jonathan S

    Nature reviews. Endocrinology

    2021  Volume 18, Issue 2, Page(s) 111–128

    Abstract: ... coupled to protein S-nitrosylation, in which nitric oxide groups are conjugated to cysteine thiols to form ... S-nitrosothiols, within effectors of insulin action. We discuss the role of S-nitrosylation ... degradation in target tissues. Finally, we consider how aberrant S-nitrosylation contributes ...

    Abstract Insulin, which is released by pancreatic islet β-cells in response to elevated levels of glucose in the blood, is a critical regulator of metabolism. Insulin triggers the uptake of glucose and fatty acids into the liver, adipose tissue and muscle, and promotes the storage of these nutrients in the form of glycogen and lipids. Dysregulation of insulin synthesis, secretion, transport, degradation or signal transduction all cause failure to take up and store nutrients, resulting in type 1 diabetes mellitus, type 2 diabetes mellitus and metabolic dysfunction. In this Review, we make the case that insulin signalling is intimately coupled to protein S-nitrosylation, in which nitric oxide groups are conjugated to cysteine thiols to form S-nitrosothiols, within effectors of insulin action. We discuss the role of S-nitrosylation in the life cycle of insulin, from its synthesis and secretion in pancreatic β-cells, to its signalling and degradation in target tissues. Finally, we consider how aberrant S-nitrosylation contributes to metabolic diseases, including the roles of human genetic mutations and cellular events that alter S-nitrosylation of insulin-regulating proteins. Given the growing influence of S-nitrosylation in cellular metabolism, the field of metabolic signalling could benefit from renewed focus on S-nitrosylation in type 2 diabetes mellitus and insulin-related disorders.
    MeSH term(s) Diabetes Mellitus, Type 2/metabolism ; Humans ; Insulin/metabolism ; Insulin Resistance/physiology ; Insulin-Secreting Cells/metabolism ; Nitric Oxide ; Sulfhydryl Compounds
    Chemical Substances Insulin ; Sulfhydryl Compounds ; Nitric Oxide (31C4KY9ESH)
    Language English
    Publishing date 2021-11-17
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Review
    ZDB-ID 2489381-X
    ISSN 1759-5037 ; 1759-5029
    ISSN (online) 1759-5037
    ISSN 1759-5029
    DOI 10.1038/s41574-021-00583-1
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: The enzymatic function of the honorary enzyme: S-nitrosylation of hemoglobin in physiology and medicine.

    Premont, Richard T / Singel, David J / Stamler, Jonathan S

    Molecular aspects of medicine

    2021  Volume 84, Page(s) 101056

    Abstract: ... nitric oxide (NO) in the form of S-nitrosothiol (SNO) at β-globin Cys93 (βCys93), and that formation and export ...

    Abstract The allosteric transition within tetrameric hemoglobin (Hb) that allows both full binding to four oxygen molecules in the lung and full release of four oxygens in hypoxic tissues would earn Hb the moniker of 'honorary enzyme'. However, the allosteric model for oxygen binding in hemoglobin overlooked the essential role of blood flow in tissue oxygenation that is essential for life (aka autoregulation of blood flow). That is, blood flow, not oxygen content of blood, is the principal determinant of oxygen delivery under most conditions. With the discovery that hemoglobin carries a third biologic gas, nitric oxide (NO) in the form of S-nitrosothiol (SNO) at β-globin Cys93 (βCys93), and that formation and export of SNO to dilate blood vessels are linked to hemoglobin allostery through enzymatic activity, this title is honorary no more. This chapter reviews evidence that hemoglobin formation and release of SNO is a critical mediator of hypoxic autoregulation of blood flow in tissues leading to oxygen delivery, considers the physiological implications of a 3-gas respiratory cycle (O
    MeSH term(s) Erythrocytes/metabolism ; Hemoglobins/metabolism ; Humans ; Hypoxia/metabolism ; Oxygen ; S-Nitrosothiols/metabolism ; Vasodilation/physiology
    Chemical Substances Hemoglobins ; S-Nitrosothiols ; Oxygen (S88TT14065)
    Language English
    Publishing date 2021-11-28
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Review
    ZDB-ID 197640-0
    ISSN 1872-9452 ; 0098-2997
    ISSN (online) 1872-9452
    ISSN 0098-2997
    DOI 10.1016/j.mam.2021.101056
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: GSNOR regulates cardiomyocyte differentiation and maturation through protein S-nitrosylation.

    Grimmett, Zachary W / Venetos, Nicholas M / Premont, Richard T / Stamler, Jonathan S

    The journal of cardiovascular aging

    2021  Volume 1

    Abstract: S-nitrosoglutathione reductase (GSNOR) is a denitrosylase enzyme responsible for reverting protein ... S-nitrosylation (SNO). In this issue, Salerno ...

    Abstract S-nitrosoglutathione reductase (GSNOR) is a denitrosylase enzyme responsible for reverting protein S-nitrosylation (SNO). In this issue, Salerno
    Language English
    Publishing date 2021-10-13
    Publishing country United States
    Document type Journal Article
    ISSN 2768-5993
    ISSN (online) 2768-5993
    DOI 10.20517/jca.2021.25
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Comparison of the Nitric Oxide Synthase Interactomes and S-Nitroso-Proteomes: Furthering the Case for Enzymatic S-Nitrosylation.

    Seth, Divya / Stomberski, Colin T / McLaughlin, Precious J / Premont, Richard T / Lundberg, Kathleen / Stamler, Jonathan S

    Antioxidants & redox signaling

    2023  Volume 39, Issue 10-12, Page(s) 621–634

    Abstract: Aims: ...

    Abstract Aims:
    MeSH term(s) Humans ; Proteome/metabolism ; Nitric Oxide Synthase/metabolism ; Oxidation-Reduction ; Signal Transduction ; Nitric Oxide/metabolism ; Protein Isoforms/metabolism
    Chemical Substances Proteome ; Nitric Oxide Synthase (EC 1.14.13.39) ; Nitric Oxide (31C4KY9ESH) ; Protein Isoforms
    Language English
    Publishing date 2023-06-01
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 1483836-9
    ISSN 1557-7716 ; 1523-0864
    ISSN (online) 1557-7716
    ISSN 1523-0864
    DOI 10.1089/ars.2022.0199
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: Optimized S-nitrosohemoglobin Synthesis in Red Blood Cells to Preserve Hypoxic Vasodilation Via

    Hausladen, Alfred / Qian, Zhaoxia / Zhang, Rongli / Premont, Richard T / Stamler, Jonathan S

    The Journal of pharmacology and experimental therapeutics

    2022  Volume 382, Issue 1, Page(s) 1–10

    Abstract: ... the mediator of microvascular blood flow through its ability to release vasodilatory S-nitrosothiol (SNO ...

    Abstract Classic physiology links tissue hypoxia to oxygen delivery through control of microvascular blood flow (autoregulation of blood flow). Hemoglobin (Hb) serves both as the source of oxygen and the mediator of microvascular blood flow through its ability to release vasodilatory S-nitrosothiol (SNO) in proportion to degree of hypoxia.
    MeSH term(s) Animals ; Erythrocytes ; Hemoglobins ; Hypoxia ; Mice ; Microcirculation ; Nitric Oxide ; Oxygen ; S-Nitrosothiols ; Vasodilation/physiology ; beta-Globins/genetics
    Chemical Substances Hemoglobins ; S-Nitrosothiols ; S-nitrosohemoglobin ; beta-Globins ; Nitric Oxide (31C4KY9ESH) ; Oxygen (S88TT14065)
    Language English
    Publishing date 2022-05-05
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
    ZDB-ID 3106-9
    ISSN 1521-0103 ; 0022-3565
    ISSN (online) 1521-0103
    ISSN 0022-3565
    DOI 10.1124/jpet.122.001194
    Database MEDical Literature Analysis and Retrieval System OnLINE

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