<scp>d</scp>‐Glyceraldehyde‐3‐phosphate dehydrogenase purified from rabbit muscle contains phosphotyrosine

Sergienko, Edward A.; Kharitonenkov, A.I.; Bulargina, T. V.; Muronetz, Vladimir; Nagradova, N.K.

doi:10.1016/0014-5793(92)80580-a

Cited by 21 publications

(15 citation statements)

References 17 publications

(4 reference statements)

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“…The exact GAPDH amino acid modified by these kinases is unknown; however, preliminary studies suggest a Tyr as the site of phosphorylation [13, 98]. Furthermore, studies have shown that mammalian, tetrameric GAPDH was auto-phosphorylated in the presence of ATP and Mg 2+ in a concentration-dependent manner and dephosphorylated in the presence of NAD + , NADH, and/or G3P [9, 14, 15].…”

Section: 0 Gapdh Functional Diversitymentioning

confidence: 99%

“…A second way GAPDH is involved in apoptosis is through post-translational modification and small molecule/protein interactions, including Ap4A binding [5, 124], VDAC-1 binding [99], phosphorylation [8–15, 98], S -glutathionylation (Section 5.1.1), p53 binding (Section 5.1.2), S -nitrosylation (Section 5.1.3), and AβPP binding (Section 5.4). Ap4A is a part of the diadenosine oligophosphate (ApnA) signal-transduction family of molecules, which play a role in DNA replication and repair through binding cell membranes and the DNA polymerase-α complex [5, 95, 124].…”

Section: 0 Gapdh and Alzheimer Diseasementioning

confidence: 99%

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Oxidatively Modified Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) and Alzheimer's Disease: Many Pathways to Neurodegeneration

Butterfield

Hardas

Lange

2010

JAD

235

185

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Recently, the oxidoreductase, glyceraldehyde-3-phosphate dehydrogenase (GAPDH), has become a subject of interest as more and more studies reveal a surfeit of diverse GAPDH functions, extending beyond traditional aerobic metabolism of glucose. As a result of multiple isoforms and cellular locales, GAPDH is able to come in contact with a variety of small molecules, proteins, membranes, etc., that play important roles in normal and pathologic cell function. Specifically, GAPDH has been shown to interact with neurodegenerative disease-associated proteins, including the amyloid-beta protein precursor (AbetaPP). Studies from our laboratory have shown significant inhibition of GAPDH dehydrogenase activity in Alzheimer's disease (AD) brain due to oxidative modification. Although oxidative stress and damage is a common phenomenon in the AD brain, it would seem that inhibition of glycolytic enzyme activity is merely one avenue in which AD pathology affects neuronal cell development and survival, as oxidative modification can also impart a toxic gain-of-function to many proteins, including GAPDH. In this review, we examine the many functions of GAPDH with respect to AD brain; in particular, the apparent role(s) of GAPDH in AD-related apoptotic cell death is emphasized.

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Section: 0 Gapdh Functional Diversitymentioning

confidence: 99%

Section: 0 Gapdh and Alzheimer Diseasementioning

confidence: 99%

Oxidatively Modified Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) and Alzheimer's Disease: Many Pathways to Neurodegeneration

Butterfield

Hardas

Lange

2010

JAD

235

185

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“…For Western blotting for GLUT1, GLUT4, or PPARg, cells were treated for 72 h with FGF-21 (50 nM), rosiglitazone (1 mM), or both. Cell lysates were immunoblotted with anti-GLUT1 against the 29 C-terminal amino acids of the human sequence, anti-GLUT4 (Slieker et al, 1992), anti-PPARg (Santa Cruz) or anti-GAPDH (Sergienko et al, 1992). PPARg protein bands were quantitated from film using a Molecular Dynamics Personal Densitometer SI with ImageQuant TM software (GE Healthcare, Piscataway, NJ).…”

Section: Cell Culturementioning

confidence: 99%

Molecular determinants of FGF‐21 activity—synergy and cross‐talk with PPARγ signaling

Moyers

Shiyanova

Mehrbod

et al. 2006

Journal Cellular Physiology

170

130

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Fibroblast growth factor (FGF)-21 is a novel regulator of insulin-independent glucose transport in 3T3-L1 adipocytes and has glucose and triglyceride lowering effects in rodent models of diabetes. The precise mechanisms whereby FGF-21 regulates metabolism remain to be determined. Here we describe the early signaling events triggered by FGF-21 treatment of 3T3-L1 adipocytes and reveal a functional interplay between FGF-21 and peroxisome proliferator-activated receptor gamma (PPARg) pathways that leads to a marked stimulation of glucose transport. While the early actions of FGF-21 on 3T3-L1 adipocytes involve rapid accumulation of intracellular calcium and phosphorylation of Akt, GSK-3, p70 S6K , SHP-2, MEK1/2, and Stat3, continuous treatment for 72 h induces an increase in PPARg protein expression. Moreover, chronic activation of the PPARg pathway in 3T3-L1 adipocytes with the PPARg agonist and anti-diabetic agent, rosiglitazone (BRL 49653), enhances FGF-21 action to induce tyrosine phosphorylation of FGF receptor-2. Strikingly, treatment of cells with FGF-21 and rosiglitazone in combination leads to a pronounced increase in expression of the GLUT1 glucose transporter and a marked synergy in stimulation of glucose transport. Together these results reveal a novel synergy between two regulators of glucose homeostasis, FGF-21 and PPARg, and further define FGF-21 mechanism of action.

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“…These include its role in nuclear RNA transport (42), modulation of cytoskeletal structure (43), DNA repair (44), and apoptosis (45). We observed, in this study, that an increase in GAPDH protein levels in PLC-γ l-transformed cells was significantly correlated with ATP production and anchorage-independent growth ( Figure 6).…”

Section: Discussionmentioning

confidence: 47%

Prolonged Protein Turnover of Glyceraldehyde-3-Phosphate Dehydrogenase by Phospholipase C-gamma 1 is Critical for Anchorage-Independent Growth and ATP Synthesis in Transformed Cells

Yun

Kim

2011

Cancer Investigation

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Overexpression of phospholipase C-γl (PLC-γl) in rat 3Y1 fibroblasts leads to the formation of tumors in nude mice. However, the molecular mechanism for PLC-γl-mediated cellular transformation has not been studied in detail. In this study, we found that glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a glycolytic enzyme, protein levels were increased substantially in cells overexpressing PLC-γl, and that PLC-γl upregulation of GAPDH was due to a decrease in ubiquitination, followed by sustained protein turnover and subsequent accumulation. These observations suggest that regulation of the turnover rate of GAPDH is critical for anchorage-independent growth and ATP synthesis of transformed cells.

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d‐Glyceraldehyde‐3‐phosphate dehydrogenase purified from rabbit muscle contains phosphotyrosine

Cited by 21 publications

References 17 publications

Oxidatively Modified Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) and Alzheimer's Disease: Many Pathways to Neurodegeneration

Oxidatively Modified Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH) and Alzheimer's Disease: Many Pathways to Neurodegeneration

Molecular determinants of FGF‐21 activity—synergy and cross‐talk with PPARγ signaling

Prolonged Protein Turnover of Glyceraldehyde-3-Phosphate Dehydrogenase by Phospholipase C-gamma 1 is Critical for Anchorage-Independent Growth and ATP Synthesis in Transformed Cells

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