Developmental regulation and cellular distribution of human cytosolic malate dehydrogenase (MDH1)

Lo, Agnes S.; Liew, C. T.; Ngai, Sai-Ming; Tsui, Stephen Kwok‐Wing; Fung, Kwok‐Pui; Lee, Cheuk-Yu; Waye, Mary Miu Yee

doi:10.1002/jcb.20343

Cited by 65 publications

(44 citation statements)

References 40 publications

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“…Cytosolic oxaloacetate is then converted to malate by MDH1, and acetyl-CoA is used for fatty acid synthesis. In mammals, MDH1 is highly expressed in many tissues, and its different roles are determined by its expression levels (15)(16)(17).…”

Section: Construction Of Retroviral Vectors and Transductionmentioning

confidence: 99%

Acetylation of malate dehydrogenase 1 promotes adipogenic differentiation via activating its enzymatic activity

Kim

Kang

et al. 2012

Journal of Lipid Research

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This article is available online at http://www.jlr.org deacetylases (HDACs) and histone acetyltransferases are enzymes that catalyze deacetylation and acetylation of the -amino groups of lysine residues of proteins. Lysine acetylation was fi rst discovered to occur in histones, and histone acetylation is important in controlling the structure and function of chromatin ( 1 ). A large number of studies have further shown the existence of acetylated nonhistone proteins, including transcription factors, hormone receptors, signal transducers, and chaperones. The reversible acetylation of nonhistone proteins modulates a wide variety of key cellular processes, such as apoptosis, survival, and proliferation. Recently, several groups have reported that many metabolic enzymes are highly acetylated ( 2-5 ). Such enzymes are involved in glycolysis, fatty acid metabolism, gluconeogenesis, the TCA cycle, and the urea cycle, and the acetylation of these proteins regulates their activity so that they can respond to the metabolic demands of cells.Adipose tissue, which consists of loose connective tissue composed of adipocytes, is an important metabolic organ that functions in energy homeostasis ( 6 ). Adipocytes regulate physiologic processes, including glucose metabolism, angiogenesis, the infl ammatory response, and reproductive functions through secreted adipokines. Adipocyte differentiation can contribute to the development of obesity via a positive energy balance (energy intake > energy expenditure) ( 7 ). Obesity leads to serious health problems all over the world. The coexistence of obesity, type II diabetes, dyslipidemia, and hypertension, known as metabolic syndrome, constitutes an increased risk for the development of cardiovascular diseases ( 8 ). In adipocytes, fatty acids are stored as triglycerides, which serve as the fuel for maintaining energy balance. Acetyl-CoA is the direct precursor in the synthesis of fatty acids, and all fatty acid carbons come from the acetyl group of acetyl-CoA. In addition, it has Abstract Acetylation is one of the most crucial posttranslational modifi cations that affect protein function. Protein lysine acetylation is catalyzed by acetyltransferases, and acetyl-CoA functions as the source of the acetyl group. Additionally, acetyl-CoA plays critical roles in maintaining the balance between carbohydrate metabolism and fatty acid synthesis. Here, we sought to determine whether lysine acetylation is an important process for adipocyte differentiation. Based on an analysis of the acetylome during adipogenesis, various proteins displaying signifi cant quantitative changes were identifi ed by LC-MS/MS. Of these identifi ed proteins, we focused on malate dehydrogenase 1 (MDH1). The acetylation level of MDH1 was increased up to 6-fold at the late stage of adipogenesis. Moreover, overexpression of MDH1 in 3T3-L1 preadipocytes induced a signifi cant increase in the number of cells undergoing adipogenesis. The introduction of mutations to putative lysine acetylation sites showed a signifi cant loss ...

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Section: Construction Of Retroviral Vectors and Transductionmentioning

confidence: 99%

Acetylation of malate dehydrogenase 1 promotes adipogenic differentiation via activating its enzymatic activity

Kim

Kang

et al. 2012

Journal of Lipid Research

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“…All proteins had been previously linked to malignancies and are involved in cellular processes like cell growth (RING finger protein and protein kinase C), regulation of the biological homeostasis including haematopoiesis and immunity (G-protein-coupled receptors), apoptosis (VCP) and processes related to cell division (Malate dehydrogenase). 9,11,[33][34][35] Since quantitative 2-DE was not performed, our results only indicate that these proteins are more frequently present in the average proteome of one responder group. This does not exclude that the respective protein will not be expressed in patients belonging to the other responder group, because proteins with a low expression level, for example, might accidentally escape software recognition.…”

Section: Discussionmentioning

confidence: 80%

Unsupervised proteome analysis of human leukaemia cells identifies the Valosin-containing protein as a putative marker for glucocorticoid resistance

et al. 2006

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The response to initial glucocorticoid therapy in childhood acute lymphoblastic leukaemia (ALL) reliably predicts the response to multiagent chemotherapy. Patients resistant to glucocorticoids (prednisone poor responders (PPR)) have a poorer event-free survival compared to glucocorticoid-sensitive patients (prednisone good responders (PGR)). A casecontrol study was performed to investigate differential protein expression in leukaemic blasts from PGR and PPR childhood ALL patients. Two-dimensional gel electrophoresis (2-DE) was used for an unsupervised screening and surface enhanced laser desorption/ionisation-time of flight mass spectrometry (SELDI-TOF MS) for the characterisation of protein spots. In difference maps of average gels for the proteomes of each responder group, differentially expressed proteins were identified after tryptic digestion and spotting onto H4-SELDI-TOF-MS chips. Proteins overexpressed in PPR were Catalase, RING finger protein 22 alpha, Valosin-containing protein (VCP) and a G-protein-coupled receptor. Proteins overexpressed in PGR were protein kinase C and malate dehydrogenase. Valosincontaining protein was chosen for validation and quantification by Western blot analysis in a second case-control group of ALL patients. In this second independent cohort, median VCP expression (P 25 -P 75 ) was 0.15 (0.11-0.28) in PGR and 0.34 (0.14-0.99) in PPR patients (P ¼ 0.04). We conclude that high VCP expression is associated with poor prednisone response in childhood ALL patients.

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“…Both MDH1 and MDH2 expression levels in lung and spleen are low compared to liver. The lowest level of MDH1 expression was observed in human lung and bone marrow (Lo et al, 2005).…”

Section: Discussionmentioning

confidence: 91%

“…In humans, MDH1 mRNA is expressed at relatively high levels in heart, skeletal muscle and brain (Lo et al, 2005). Similarly, Mori et al (2009) reported that MDH1 mRNA is highly expressed in skeletal muscle in cats.…”

Section: Discussionmentioning

confidence: 92%

Molecular analysis of cytosolic and mitochondrial malate dehydrogenases isolated from domestic cats (Felis catus)

Sasaki¹,

Nakamura²,

Soeta³

2014

Genet. Mol. Res.

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ABSTRACT. Malate dehydrogenase (MDH) plays crucial roles in energy and cellular metabolism. In this study, we describe the identification and characterization of cytosolic MDH (MDH1) and mitochondrial MDH (MDH2) in liver of domestic cat (Felis catus). To clone the feline full-length MDH genes, we performed rapid amplification of cDNA ends. The MDH1 gene encoded a protein of 334 amino acids and the MDH2 gene encoded a protein of 338 amino acids, containing a 24-amino acid mitochondrial target sequence. The feline MDH1 and MDH2 proteins shared, respectively, 98.8-93.7 and 96.7-94.4% homology with dog, giant panda, horse, cow, pig, human, mouse, and rat. The feline MDHs had a highly conserved active motif, which contained important residues for catalysis and coenzyme binding. The putatively acetylated lysine residues that regulate MDH activity were also conserved at K118, K121, and K298 in MDH1, and K185, K301, K307, and K314 in MDH2. Both MDH1 and MDH2 mRNAs were ubiquitously expressed, but these expression levels varied in a tissue-specific manner. Both MDH genes were expressed at considerably high levels in heart and skeletal muscle, but at low levels in lung and spleen.

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Developmental regulation and cellular distribution of human cytosolic malate dehydrogenase (MDH1)

Cited by 65 publications

References 40 publications

Acetylation of malate dehydrogenase 1 promotes adipogenic differentiation via activating its enzymatic activity

Acetylation of malate dehydrogenase 1 promotes adipogenic differentiation via activating its enzymatic activity

Unsupervised proteome analysis of human leukaemia cells identifies the Valosin-containing protein as a putative marker for glucocorticoid resistance

Molecular analysis of cytosolic and mitochondrial malate dehydrogenases isolated from domestic cats (Felis catus)

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