Molecular cloning and characterization of neutral ceramidase homologue from the red flour beetle, Tribolium castaneum

Zhou, Ying; Lin, Xianwen; Yang, Qiong; Zhang, Yanru; Yuan, Jingqun; Lin, Xinhua; Xu, Ruijuan; Cheng, Jiaan; Mao, Cungui; Zhu, Zhiliang

doi:10.1016/j.biochi.2011.03.009

Cited by 8 publications

(17 citation statements)

References 17 publications

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“…LsnCer has an alkaline optimum pH at pH 8.0, whereas nCDases from D. melanogaster , mouse, rat and humans have a neutral optimum pH (El Bawab et al ., ; Yoshimura et al ., , ). LsnCer is also distinct in terms of its optimum pH from the nCDase of T. castaneum , which shows a broad optimum pH range for its activity (Zhou et al ., ). Similar to the nCDase from T. castaneum , LsnCer has an optimum temperature of 37 °C for its in vitro enzymatic activity.…”

Section: Discussionmentioning

confidence: 82%

“…Confocal microscopy revealed that LsnCer was mainly located in the PM. We have previously shown that the nCDase of T. castaneum is also localized in the PM (Zhou et al ., ). These results suggest that the cellular location of nCDase is conserved among different insects.…”

Section: Discussionmentioning

confidence: 98%

“…The nCDase gene is necessary for maintaining photoreceptor homeostasis by regulating rhodopsin endocytosis (Acharya et al ., ). In our previous study, we demonstrated that nCDase is highly expressed in Tribolium castaneum reproductive organs (Zhou et al, ), indicating that nCDase may be important in insect reproduction. Our group found that daCER regulates the antioxidant ability and the lifespan of the Drosophila (Yang et al ., ).…”

Section: Introductionmentioning

confidence: 99%

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Identification and biochemical characterization of Laodelphax striatellus neutral ceramidase

Zhou

Lin

Zhang

et al. 2013

Insect Molecular Biology

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Ceramidases are a group of enzymes that catalyze hydrolysis of ceramides to generate fatty acid and sphingosine. In this study, we report the cloning and characterization of the rice small brown planthopper Laodelphax striatellus neutral ceramidase (nCDase), LsnCer. LsnCer was identified by sequencing the transcriptome of Laodelphax striatellus. LsnCer is a protein of 717 amino acids with a predicted molecular weight of 79.3 kDa. Similar to other known nCDases, LsnCer has a pH optimum at 8.0 and a temperature optimum at 37 °C for its in vitro activity. LsnCer activity is inhibited by Zn2+ significantly and Fe2+ slightly. LsnCer has broad substrate specificity with preference for ceramides with a medium acyl-chain or a mono unsaturated long acyl-chain. Infection with the rice strip virus (RSV) or treatment with insecticides significantly increased LsnCer mRNA expression and its enzymatic activity in L. striatellus. These results suggest that LsnCer is a bona fide nCDase that may have a role in adaption of L. striatellus to environmental stresses.

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Section: Discussionmentioning

confidence: 82%

Section: Discussionmentioning

confidence: 98%

Section: Introductionmentioning

confidence: 99%

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Identification and biochemical characterization of Laodelphax striatellus neutral ceramidase

Zhou

Lin

Zhang

et al. 2013

Insect Molecular Biology

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“…The microsome was prepared and western blotting was analysed according to our previous study (Zhou et al ., ).…”

Section: Methodsmentioning

confidence: 97%

Identification and characterization of Laodelphax striatellus (Insecta: Hemiptera: Delphacidae) neutral sphingomyelinase

Zhou

Lin

Begum

et al. 2017

Insect Molecular Biology

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The neutral sphingomyelinase (nSMase) 1 homologue gene LsSMase was cloned from Laodelphax striatellus, a direct sap-sucker and virus vector of gramineous plants, and expressed via a Bac to Bac baculovirus expression system. The LsSMase-enhanced green fluorescent protein fusion protein was located in the endoplasmic reticulum in a similar manner to mammalian nSMase 1. The biochemical properties of LsSMase were determined in detail. The optimal pH and temperature for recombinant LsSMase were 8 and 37 °C, respectively. LsSMase was an Mg or Mn dependent enzyme, but different concentration of each were needed. The activity of LsSMase was significantly stimulated by Ethylene glycol bis(2-aminoethyl ether)tetraacetic acid (EGTA), whereas it was inhibited by ethylenediaminetetraacetic acid. Millimolar concentrations of Zn completely inhibited LsSMase. The reducing agents dithiothreitol and β-mercaptoethanol varied in their effects on activity. Phospholipids were not found to stimulate LsSMase.

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“…Acidic ceramidases are located in lysosomes, and they efficiently hydrolyze ceramides with medium chain fatty acid components [96]. Neutral ceramidases are located in the plasma membrane and use long-chain to very-long-chain fatty acid components (C 16 to >C 24 ) as substrates [97, 98]. Alkaline ceramidases 1 and 2 (ACER1 and ACER2) are localized in the ER and Golgi, and they also utilize very-long-chain acyl groups as substrates.…”

Section: Ceramides- Reviewedmentioning

confidence: 99%

Triangulated Mal-Signaling in Alzheimer's Disease: Roles of Neurotoxic Ceramides, ER Stress, and Insulin Resistance Reviewed

Monte

2012

JAD

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Ceramides are lipid signaling molecules that cause cytotoxicity and cell death mediated by insulin resistance, inflammation, and endoplasmic reticulum (ER) stress. However, insulin resistance dysregulates lipid metabolism, which promotes ceramide accumulation with attendant inflammation and ER stress. Herein, we discuss two major pathways, extrinsic and intrinsic, that converge and often overlap in propagating AD-type neurodegeneration via a triangulated mal-signaling network. First, we review evidence that systemic insulin resistance diseases linked to obesity, type 2 diabetes, and non-alcoholic steatohepatitis promote neurodegeneration. Mechanistically, we propose that toxic ceramides generated in extra-CNS tissues (e.g., liver) get released into peripheral blood, and subsequently transit across the blood-brain barrier into the brain where they induce brain insulin resistance, inflammation, and cell death (extrinsic pathway). Then we discuss the role of the intrinsic pathway of neurodegeneration which is mediated by endogenous or primary brain insulin/IGF resistance, and impairs neuronal and oligodendrocyte survival, energy metabolism, membrane integrity, cytoskeletal function, and AβPP-Aβ secretion. The end result is increased ER stress and ceramide generation, which exacerbate brain insulin resistance, cell death, myelin degeneration, and neuroinflammation. Altogether, the data suggest that the triangulated mal-signaling network mediated by toxic ceramides, ER stress, and insulin resistance should be targeted to disrupt positive feedback loops that drive the AD neurodegeneration cascade.

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Molecular cloning and characterization of neutral ceramidase homologue from the red flour beetle, Tribolium castaneum

Cited by 8 publications

References 17 publications

Identification and biochemical characterization of Laodelphax striatellus neutral ceramidase

Identification and biochemical characterization of Laodelphax striatellus neutral ceramidase

Identification and characterization of Laodelphax striatellus (Insecta: Hemiptera: Delphacidae) neutral sphingomyelinase

Triangulated Mal-Signaling in Alzheimer's Disease: Roles of Neurotoxic Ceramides, ER Stress, and Insulin Resistance Reviewed

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