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ABSTRACT: A series of polymers system based on poly(butyl methacrylate) (PBMA) and poly (hydroxyethyl methacrylate) semi-interpenetrating polymer networks (semi-IPN) (PBMA/ PHEMA = 70/30 by weight) have been attained by a sequential polymerization method using divinylbenzene (DVB) as cross-linking agent. Oil-absorptive fibers are prepared by wet-spinning processing. Oil absorbencies, swollen diameter variation, tensile strength, percentage elongation at break of the oil-absorptive fibers are reported. Crystalline structures have been estimated using wide angle X-ray diffraction (WXRD). Thermogravimetric analyzer (TGA), derivative thermogravimetry (DTG) and differential scanning calorimetry (DSC) are used to investigate thermal properties of oil-absorptive fibers. The results show that the cross-linking agent has a full impact on the properties of the oil-absorptive fiber. With an increase in DVB, oil absorbency can be improved, and the fiber shows many special phenomena including perfect cross-linking structure, excellent entanglement behaviors, good thermal stability and mediated crystalline temperature. However, glass transition temperature increases, and crystallization behavior becomes poor as increasing the cross-linking agent of DVB.
Polymer-Plastics Technology and Engineering 05/2011; 50(8):818-824. · 1.28 Impact Factor
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ABSTRACT: Axon degeneration is supposed to be a therapeutic target for treating neurodegenerative diseases. Mauthner cells (M-cells) are ideal for studying axons in vivo because of their limited numbers, large size, and long axons. In this study, we labeled M-cells by single-cell electroporation with plasmids expressing DsRed2 or EGFP. Injury-induced axon degeneration in labeled M-cell was imaged under a confocal microscope, and we found that the Mauthner axons started to degenerate about 24 hr after lesion. The Wld(S) protein containing full-length Nmnat1 is well-known for its axon-protective function in many systems. Overexpression of Wld(S) in M-cells also greatly delayed axon degeneration in live zebrafish. Nmnat2 is the only Nmnat highly expressed in brain. Here we demonstrated that overexpression of Nmnat2 in M-cells significantly delayed axon degeneration in vivo, and disruption of the NAD synthesis activity of Nmnat2 markedly attenuated its axon-protective function. All these data show that injury-induced axon degeneration of M-cell has a mechanism similar to that in mammalians and would be a valuable model for studying axon degeneration in vivo.
Journal of Neuroscience Research 11/2010; 88(15):3319-27. · 2.74 Impact Factor
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ABSTRACT: A chimeric protein called Wallerian degeneration slow (Wld(S)) was first discovered in a spontaneous mutant strain of mice that exhibited delayed Wallerian degeneration. This provides a useful tool in elucidating the mechanisms of axon degeneration. Over-expression of Wld(S) attenuates the axon degeneration that is associated with several neurodegenerative disease models, suggesting a new logic for developing a potential protective strategy. At molecular level, although Wld(S) is a fusion protein, the nicotinamide mononucleotide adenylyl transferase 1 (Nmnat1) is required and sufficient for the protective effects of Wld(S), indicating a critical role of NAD biosynthesis and perhaps energy metabolism in axon degeneration. These findings challenge the proposed model in which axon degeneration is operated by an active programmed process and thus may have important implication in understanding the mechanisms of neurodegeneration. In this review, we will summarize these recent findings and discuss their relevance to the mechanisms of axon degeneration.
Protein & Cell 03/2010; 1(3):237-45.
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ABSTRACT: Axon degeneration has been proposed to be a new therapeutic target for neurodegenerative diseases, because it usually occurs earlier than neuronal cell body death with a distinct active program from apoptosis and necrosis. Overexpression of Wld(S) or Nmnats (nicotinamide mononucleotide adenylytransferase, EC2.7.7.1) has been demonstrated to delay axon degeneration initiated by various insults. NAD synthesis activity of Wld(S) and Nmnats was shown to be responsible for their axon-protective function. The mitochondrial Nmnat3 and cytoplasm-localized mutants of Wld(S) and Nmnat1 have similar or even stronger effect than Wld(S) to delay axon degeneration, which suggest that increased mitochondrial or local NAD synthesis might contribute to the protective function of Wld(S) and Nmnats. Further studies show NAD synthesis pathway and ubiquitin proteasome system play important roles in delaying axon degeneration. Wld(S) mice are resistant to a variety of neurodegenerative diseases, but the role of Nmnats in neurodegenerative diseases are largely unknown. NAD plays key roles in energy metabolism, mitochondrial functions and aging, and is suggested to be involved in neuron degenerative diseases. Future studies to identify the upstream factors inducing NAD depletion and the downstream NAD effectors responsible for the axon-protective function will provide more meaningful insights into the molecular mechanisms of axon degeneration in neurodegenerative diseases.
Neurochemistry International 03/2010; 56(4):529-34. · 2.86 Impact Factor
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ABSTRACT: Axon degeneration is a common hallmark of many neurodegenerative diseases, and the underlying mechanism remains largely unknown. Lysosomes are involved in some neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease. Whether lysosomes are involved in axon degeneration is yet to be elucidated. In this study, we found only about 10% lysosomes remained in axons of cultured superior cervical ganglia (SCGs) after transection for 4h when stained with LysoTracker. Furthermore, we found that lysosomal disruption occurred earlier than morphological changes and loss of mitochondrial membrane potential. In addition, the well-known axon-protective protein Wld(S) delayed injury-induced axon degeneration from both morphological changes and lysosomal disruption. Lysosomal inhibitors including chloroquine and ammonium chloride induced axon degeneration in cultured SCGs, and Wld(S) also slowed down the axon degeneration induced by lysosomal inhibitors. All these data suggest that lysosomal disruption is an early marker of axon degeneration, and inhibition of lysosome induces axon degeneration in a Wld(S)-protectable way. Thus, maintenance of normal lysosomal function might be an important approach to delay axon degeneration in neurodegenerative diseases.
Neurochemistry International 02/2010; 56(3):516-21. · 2.86 Impact Factor
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ABSTRACT: Axon degeneration is an active program of self-destruction observed in many physiological and pathological settings. There are three Nicotinamide mononucleotide adenylyl transferase (Nmnat, EC2.7.7.1) in mammals. Overexpression of Nmnat1 or Nmnat3 can delay axon degeneration, while the role of Nmnat2 in axon degeneration remains largely unknown. Here we found that Nmnat2 was specifically and highly expressed in brain compared with Nmnat1 and Nmnat3. Furthermore, we found brain Nmnat2 was correlated with Alzheimer's disease in APPswe/PS1dE9 transgenic mice. Nmnat2 delayed Wallerian degeneration in cultured superior cervical ganglia (SCGs) from morphological changes, microtubule destruction and neurofilament degradation, mutation of the conserved enzyme activity site in Nmnat2 disrupted its enzyme activity as well as the axon-protective function. Our results demonstrate that the brain-specific Nmnat2 delays injury-induced axon degeneration dependent on its NAD synthesis activity. These findings provide new clues to further study the molecular mechanisms of axon degeneration and the related neurodegenerative diseases.
Neurochemistry International 09/2009; 56(1):101-6. · 2.86 Impact Factor
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ABSTRACT: The chimeric Wld(s) protein consisting of the N-terminal 70 amino acids of Ufd2 and the complete sequence of nicotinamide mononucleotide adenylyltransferase1 (Nmnat1), delays Wallerian degeneration in Wld(s) mice. Although Nmnat1 enzyme activity was showed to be critical for the function of Wld(s) protein, the expected phenotype was not observed in Nmnat1 transgenic mice. To further check whether Nmnat1 enzyme activity is involved, we aligned sequences of eukaryotic Nmnats, and found that Phe in helix A is highly conserved not only in various species, but also in different homologues. The Phe is a residue located near to the highly conserved GXFXPX(T/H)XXH motif and resides in the same helix as the last His of this conserved motif. To investigate the role of the conserved Phe in Nmnat activity, we made the point mutation of Phe. The Phe28 mutation of mouse Nmnat1 in Wld(s) completely abolished its Nmnat enzyme activity. To study the role of mutant Wld(s) in axon degeneration, herpes viruses were packaged to infect cultured SCGs. We found that the mutant Wld(s) failed to protect axon degeneration from morphological changes, microtubule integration and neurofilament degradation. Therefore, we have identified a Phe residue that critical for both enzyme activity of Nmnat and the axon-protective function of Wld(s), and further confirmed that Nmnat1 enzyme activity is required in Wld(s) function.
Neuroscience Letters 03/2007; 413(1):46-51. · 2.11 Impact Factor
