scholarly journals Manganese influx and expression of ZIP8 is essential in primary myoblasts and contributes to activation of SOD2

Metallomics ◽  
2019 ◽  
Vol 11 (6) ◽  
pp. 1140-1153 ◽  
Author(s):  
Shellaina J. V. Gordon ◽  
Daniel E. Fenker ◽  
Katherine E. Vest ◽  
Teresita Padilla-Benavides
Keyword(s):  
Trace Elements ◽  
Cell Signaling ◽  
Second Messengers ◽  
Primary Myoblasts ◽  
Enzyme Cofactors

Trace elements such as copper (Cu), zinc (Zn), iron (Fe), and manganese (Mn) function as enzyme cofactors and second messengers in cell signaling.

scholarly journals Manganese influx and expression of ZIP8 is essential in primary myoblasts and contributes to activation of SOD2

2018 ◽  
Author(s):  
Shellaina J. V. Gordon ◽  
Daniel E. Fenker ◽  
Katherine E. Vest ◽  
Teresita Padilla-Benavides
Keyword(s):  
Skeletal Muscle ◽  
Trace Elements ◽  
Second Messengers ◽  
Muscle Cells ◽  
Skeletal Muscle Cells ◽  
Metal Transporters ◽  
Primary Myoblasts ◽  
Zip Family ◽  
Enzyme Cofactors ◽  
Functional Relevance

ABSTRACTTrace elements such as copper (Cu), zinc (Zn), iron (Fe), and manganese (Mn) are enzyme cofactors and second messengers in cell signaling. Trace elements are emerging as key regulators of differentiation and development of mammalian tissues including blood, brain, and skeletal muscle. We previously reported an influx of Cu and dynamic expression of various metal transporters during differentiation of skeletal muscle cells. Here, we demonstrate that during differentiation of skeletal myoblasts an increase of additional trace elements such as Mn, Fe and Zn occurs. Interestingly the Mn increase is concomitant with increased Mn-dependent SOD2 levels. To better understand the Mn import pathway in skeletal muscle cells, we probed the functional relevance of the closely related proteins ZIP8 and ZIP14, which are implicated in Zn, Mn, and Fe transport. Partial depletion of ZIP8 severely impaired growth of myoblasts and led to cell death under differentiation conditions, indicating that ZIP8-mediated metal transport is essential in skeletal muscle cells. Moreover, knockdown of Zip8 impaired activity of the Mn-dependent SOD2. Growth defects were partially rescued by Mn supplementation to the medium, suggesting additional functions for ZIP8 in the skeletal muscle lineage. Knockdown of Zip14, on the other hand, had only a mild effect on myotube size, consistent with a role for ZIP14 in muscle hypertrophy. This is the first report on the functional relevance of two members of the ZIP family of metal transporters in the skeletal muscle lineage, and further supports the paradigm that trace metal transporters are critical modulators of mammalian tissue development.

scholarly journals Conceptual Evolution of Cell Signaling

2019 ◽  
Vol 20 (13) ◽  
pp. 3292 ◽  
Author(s):  
Arathi Nair ◽  
Prashant Chauhan ◽  
Bhaskar Saha ◽  
Katharina F. Kubatzky
Keyword(s):  
Cell Signaling ◽  
Intracellular Signaling ◽  
Protein Targeting ◽  
Second Messengers ◽  
Common Mechanism ◽  
Physiological Processes ◽  
Intracellular Messengers ◽  
Response Profiles ◽  
Conceptual Evolution

During the last 100 years, cell signaling has evolved into a common mechanism for most physiological processes across systems. Although the majority of cell signaling principles were initially derived from hormonal studies, its exponential growth has been supported by interdisciplinary inputs, e.g., from physics, chemistry, mathematics, statistics, and computational fields. As a result, cell signaling has grown out of scope for any general review. Here, we review how the messages are transferred from the first messenger (the ligand) to the receptor, and then decoded with the help of cascades of second messengers (kinases, phosphatases, GTPases, ions, and small molecules such as cAMP, cGMP, diacylglycerol, etc.). The message is thus relayed from the membrane to the nucleus where gene expression ns, subsequent translations, and protein targeting to the cell membrane and other organelles are triggered. Although there are limited numbers of intracellular messengers, the specificity of the response profiles to the ligands is generated by the involvement of a combination of selected intracellular signaling intermediates. Other crucial parameters in cell signaling are its directionality and distribution of signaling strengths in different pathways that may crosstalk to adjust the amplitude and quality of the final effector output. Finally, we have reflected upon its possible developments during the coming years.

Clinically Accessible Cell Signaling: Second Messengers in Sepsis and Trauma

1996 ◽  
Vol 60 (1) ◽  
pp. 270-277 ◽  
Author(s):  
Thomas F. Rehring ◽  
Elizabeth C. Brew ◽  
Randall S. Friese ◽  
Anirban Banerjee ◽  
Alden H. Harken
Keyword(s):  
Cell Signaling ◽  
Second Messengers

PTP1B and TC-PTP: novel roles in immune-cell signalingThis paper is one of a selection of papers published in this Special issue, entitled Second Messengers and Phosphoproteins—12th International Conference.

2006 ◽  
Vol 84 (7) ◽  
pp. 667-675 ◽  
Author(s):  
Paul D. Simoncic ◽  
C. Jane McGlade ◽  
Michel L. Tremblay
Keyword(s):  
Immune Response ◽  
Cell Signaling ◽  
Protein Tyrosine Phosphatase ◽  
Immune Cell ◽  
Second Messengers ◽  
Tyrosine Phosphatase ◽  
Special Issue ◽  
Substrate Specificities ◽  
Myeloid Development ◽  
Selection Of

It has recently been demonstrated that the protein tyrosine phosphatase (PTP) PTP1B and the T-cell PTP (TC-PTP) target several substrates involved in immune cell signaling. Recent data have furthered the view of these 2 PTP members as key regulators of the immune response. This review will focus on the substrate specificities of PTP1B and TC-PTP and their roles in immune cell signaling, and will discuss some new data implicating PTP1B and TC-PTP in myeloid development.

New insights into pancreatic β-cell metabolic signaling in insulin secretion

1996 ◽  
Vol 134 (3) ◽  
pp. 272-286 ◽  
Author(s):  
Marc Prentki
Keyword(s):  
Insulin Secretion ◽  
Cell Signaling ◽  
Insulin Release ◽  
Cell Activation ◽  
Cell Metabolism ◽  
Second Messengers ◽  
Acid Oxidation ◽  
Pancreatic Β Cell ◽  
Β Cell ◽  
Metabolic Signaling

Prentki M. New insights into pancreatic β-cell metabolic signaling in insulin secretion. Eur J Endocrinol 1996;134:272–86. ISSN 0804–4643 In recent years, it has become apparent that second messengers and factors other than ATP, metabolically sensitive KATP+ channels and Ca2+ play essential roles in nutrient-induced insulin release. This paper reviews the evidence in support of several new concepts and hypotheses in the field of β-cell signaling. These include in particular that: a rise in cytosolic Ca2+ is not sufficient to explain the kinetics and extent of secretion induced by glucose: variations in ADP, rather than ATP, regulate β-cell metabolism and the KATP+ channel; anaplerosis (the replenishment of the citric acid cycle with intermediates) is essential for β-cell activation; a shift from fatty acid oxidation to esterification is an important event in β-cell signaling; malonyl-CoA and long chain acyl-CoA esters may act as metabolic coupling factors; glycolytic oscillations underlie, in part, oscillations in electrical activity, cytosolic Ca2+ and insulin release. A metabolic model of fuel sensing that integrates the mode of action of all classes of nutrient secretagogues is proposed. Marc Prentki, Department of Nutrition, University of Montreal, CP6128, Succ, Centre-Ville, Montreal, PQ H3C3J7, Canada

scholarly journals Cell signaling promoting protein carbonylation does not cause sulfhydryl oxidation: Implications to the mechanism of redox signaling

F1000Research ◽  
2017 ◽  
Vol 6 ◽  
pp. 455
Author(s):  
Yuichiro J. Suzuki ◽  
Faisal Almansour ◽  
Camilla Cucinotta ◽  
Vladyslava Rybka ◽  
Lucia Marcocci
Keyword(s):  
Cell Signaling ◽  
Second Messengers ◽  
Protein Carbonylation ◽  
Cysteine Residues ◽  
State Monitoring ◽  
High Concentration ◽  
Sulfhydryl Oxidation ◽  
Pdgf Stimulation ◽  
Human Pulmonary Artery ◽  
Cysteine Thiols

Reactive oxygen species (ROS) have been recognized as second messengers, however, targeting mechanisms for ROS in cell signaling have not been defined. While ROS oxidizing protein cysteine thiols has been the most popular proposed mechanism, our laboratory proposed that ligand/receptor-mediated cell signaling involves protein carbonylation. Peroxiredoxin-6 (Prx6) is one protein that is carbonylated at 10 min after the platelet-derived growth factor (PDGF) stimulation of human pulmonary artery smooth muscle cells. In the present study, the SulfoBiotics Protein Redox State Monitoring Kit Plus (Dojindo Molecular Technologies) was used to test if cysteine residues of Prx6 are oxidized in response to the PDGF stimulation. Human Prx6 has a molecular weight of 25 kDa and contains two cysteine residues. The Dojindo system adds the 15 kDa Protein-SHifter if these cysteine residues are reduced in the cells. Results showed that, in untreated cells, the Prx6 molecule predominantly exhibited the 55 kDa band, indicating that both cysteine residues are reduced in the cells. Treatment of cells with 1 mM H2O2 caused the disappearance of the 55 kDa band and the appearance of a 40 kDa band, suggesting that the high concentration of H2O2 oxidized one of the two cysteine residues in the Prx6 molecule. By contrast, PDGF stimulation had no effects on the thiol status of the Prx6 molecule. We concluded that protein carbonylation is a more sensitive target of ROS during ligand/receptor-mediated cell signaling than sulfhydryl oxidation.

Lipid second messengers and cell signaling in vascular wall

2007 ◽  
Vol 72 (8) ◽  
pp. 797-808 ◽  
Author(s):  
N. V. Prokazova ◽  
N. N. Samovilova ◽  
N. K. Golovanova ◽  
E. V. Gracheva ◽  
A. A. Korotaeva ◽  
...  
Keyword(s):  
Cell Signaling ◽  
Second Messengers ◽  
Vascular Wall

l-O-Hexadecyl-2-O-methyl-sn-glycero-3-phosphocholine inhibits diacylglycerol kinase in WEHI-3B cells

1993 ◽  
Vol 71 (1-2) ◽  
pp. 36-42 ◽  
Author(s):  
Hassan Salari ◽  
Mervin Low ◽  
Sandra Howard ◽  
Glenn Edin ◽  
Robert Bittman
Keyword(s):  
Phosphatidic Acid ◽  
Cell Signaling ◽  
Cytotoxic Activity ◽  
Second Messengers ◽  
Diacylglycerol Kinase ◽  
Ether Lipids ◽  
Enzyme Preparations

The effects of 1-O-hexadecyl-2-O-methyl-sn-glycero-3-phosphocholine (ET-16-OCH3-GPC) and its metabolite 1-O-hexadecyl-2-O-methyl-sn-glycerol (AMG) on the activity of diacylglycerol kinase (DGK) in WEHI-3B cells were investigated. Treatment of WEHI-3B cells with 200 nM 12-O-tetradecanoylphorbol-13-acetate (TPA) for 5 min leads to the activation of cytosolic DGK without significant effect on microsomal DGK. When these cells were first exposed to 50 μM ET-16-OCH3-GPC for 30 min prior to activation with TPA, the activity of DGK was inhibited by about 70%, as measured by the ability of enzyme to form [32P]phosphatidic acid ([32P]PA). Addition of either ET-16-OCH3-GPC or AMG to the preparation of enzyme in vitro also inhibited 1,2-dioleoyl-sn-glycerol (DG) phosphorylation in the presence of [γ-32P]ATP. The IC50 value for inhibition of cytosolic DGK by ET-16-OCH3-GPC and AMG were about 8.5 and 15 μM, respectively. ET-16-OCH3-GPC also inhibited the ability of guanosine 5′-O-(3-thiophosphate) (GTP-7S) to activate DGK in vitro. The potency of ET-16-OCH3-GPC at 10 μM in inhibiting DGK was greater than that of sphingosine at 50 μM, but less than that of R59022 (a specific DGK inhibitor) at 10 μM. The abilities of ET-16-OCH3-GPC and AMG to inhibit cytosolic DGK in intact WEHI-3B cells and enzyme preparations in vitro suggest that the cytotoxic activity of ether lipids may in part result from interference with this vital enzyme involved in the synthesis of phospholipids from DG and in cell-signaling systems.Key words: diacylglycerol, kinases, second messengers, ether lipids, cancer, WEHI-3B cells.

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