Citation: Isabel Saez, David Vilchez. Protein clearance mechanisms and their demise in age-related neurodegenerative diseases[J]. AIMS Molecular Science, 2015, 1(1): 1-21. doi: 10.3934/molsci.2015.1.1
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Titanium dioxide has been extensively investigated for applications ranging from water splitting, dye-sensitized solar cells, degradation of pollutants, and destruction of bacteria to bio-medical applications [1,2,3,4,5]. Titania has been widely used because it is inexpensive to synthesize, benign, and photostable. A porous structured titanium dioxide can improve photocatalytic activity due to improved mass transport properties. In this regard, mesoporous materials offer promise. In recent years, several methods have been attempted to prepare porous TiO2 nanomaterials [6,7,8]. These include supercritical, hydrothermal, hard templating, and Evaporation-Induced Self-Assembly (EISA) methods. The high temperature supercritical method minimizes the collapse of pores, but requires expensive instrumentation, is energy intensive, and has challenges in scaling up due to the requirements of relatively high pressures and temperatures [8]. Hydrothermal method requires the use of autoclaves and relatively high pressures and temperatures [9]. The hard templating method is laborious, requires multiple steps of impregnation and long processing times [10,11]. In comparison to the above methods, EISA seems to be a facile and simple method, and it has the added benefit that the materials can be prepared and processed at mild conditions [12,13]. Another main advantage of the EISA method is that the material can be recovered as a powder or as a film. Several parameters such as pH, water content, nature and concentration of precursor(s) and surfactant, humidity, temperature etc. affect the quality and nature of the final mesostructured material, and these have been investigated previously [6]. The common precursor(s) for the synthesis of titania by EISA include TiCl4 and/or Ti(OCH(CH3)2)4. TiCl4 is highly reactive, toxic, and hazardous and hence titanium alkoxides are preferable. The EISA method involves the use of non-ionic (e.g. pluronic polymers such as P123) or cationic (e.g. cetyltrimethylammonium bromide (CTAB)) surfactants. An advantage of CTAB is that its critical micelle concentration is higher than that of P123. Also, the cloud point is a major issue with P123. Thus, a clear micellar solutions can be readily prepared at room temperature using CTAB. In addition, CTAB can be used at both low and high pH values. Thus, in the present study, Ti(OCH(CH3)2)4 and CTAB were used in the preparation of TiO2. Although several factors have been investigated, surprisingly, a systematic study of aging time has not been explored using the EISA method. This is important because the composition of the solution changes during the evaporation process, and this has profound effect on the nature of the final phase(s) formed.
It has been reported that mixedphases of titania exhibit higher activities in comparison to pure phases [14,15]. This has been the reason for the high activity of Degussa P25 for several photocatalytic reactions. Li et al. reported that the presence of small rutile crystallites in close contact with anatase created catalytic “hot spots” and this was responsible for high photocatalytic activity [16]. Thus, it is important to explore effective methods to prepare mixed-phase titania in a facile manner. Previous attempts to prepare TiO2 with mixed phases using surfactants required calcination (typically at relatively high temperatures in the range of 600 to 1200 oC) [9], use of highly reactive TiCl4 in addition to Ti(OR)4 [17], or hydrothermal treatment [18]. In addition, microemulsion method [19], flame pyrolysis, [20], or physical vapor deposition [21] methods have also led to the formation of mixed phases of anatase and rutile. In comparison to these methods of synthesis, the EISA method seems to relatively easy.
The anatase-to-rutile phase transformation as a function of aging time for the preparation of TiO2 mesostructured materials by the EISA method has not been investigated carefully and provides the impetus for this work. The mesostructured materials were evaluated for solar hydrogen production. The material with anatase (95%) and rutile (5%) exhibited high activity even in the absence of Pt as a co-catalyst. Our results suggest that mixed phases of TiO2 with varying compositions can be obtained by aging using the EISA method and by calcination at moderate temperatures in contrast to previous literature attempts to prepare mixed phases of anatase and rutile. Thus, this synthetic protocol is simple, and the composition of the titania phase(s) can be varied by simply varying the aging time. This study provides an ideal opportunity for making both powders and thin films of mixed phases for various applications in a facile manner.
Commercially available cetyltrimethylammonium bromide (CTAB, Alfa Aesar, 98+%), titanium isopropoxide (Ti(OCH(CH3)2)4, Acros, 98+%), conc. hydrochloric acid (Fisher-Scientific, ACS grade), ethanol (Pharmco-AAPER, ACS/USP grade, 200 proof) were used as received. Deionized water was used throughout the experiments.
The EISA method was used for preparing mesoporous TiO2 materials [12,13,22]. In a typical synthesis, 0.468 g of cetyltrimethylammonium bromide (CTAB) was dissolved in 5 mL of ethanol in a beaker. The solution was heated slowly to 50 °C and the beaker was covered with parafilm to prevent evaporation of ethanol. In another beaker, 4.4 mL of ethanol, 2.4 mL of Ti(OCH(CH3)2)4, and 0.93 mL of conc. HCl were mixed. These two solutions were combined and stirred. Then, 2.46 mL of deionized water was added drop wise and the mixture was stirred. The resulting solution was poured into petri dishes and then placed in an oven and heated to 60 °C and aged for various times. The materials were removed after 0.25,1, and 6 days. Finally, the materials were calcined at 500 °C for 6 h in static air at a heating rate of 3 oC/min to remove the template and named as TiO2-0.25d, TiO2-1d, and TiO2-6d.
Thermogravimetric analysis of the calcined mesostructured material indicates a weight loss of only 0.55 wt.% between 200 and 550 oC. This weight loss corresponds to loss of surface hydroxyl groups from titania, and this indicates that the cationic surfactant was removed after calcination.
TiO2 materials were characterized extensively by a variety of techniques. The powder X-ray diffraction studies of the mesostructured materials were recorded at room temperature using a Rigaku Ultima IV instrument with Cu Kα radiation (λ = 1.5408 Å). The accelerating voltage used was 40 kV, and the emission current was maintained at 44 mA. The samples were scanned with a step size of 0.02°, in the 2θ range from 10 to 80°. The ratios of the mixed phases present in the samples were determined by performing quantitative analysis using the Reference Intensity Ratio (RIR) method in the PDXL software (version 2) provided by Rigaku. Raman spectra were collected using a Horiba Jobin Yvon Labram Aramis Raman spectrometer with a He-Ne laser (532 nm) as the light source. The unfiltered beam of scattered laser radiation was focused onto the materials using a microscope objective (×50) for an acquisition time of typically 10 s. Transmission Electron Microscopic (TEM) images were obtained using a Tecnai G2 instrument operating at 120 kV. Prior to the analysis, the materials were dispersed in ethanol and the suspensions were sonicated for 30 min. Then, one drop of the suspension was placed on a copper grid coated with carbon film, and allowed to dry overnight before conducting the TEM studies. The textural properties, such as surface area, pore volume, and pore size distribution of the materials were analyzed using N2 physisorption measurements. After the samples were dried overnight at 80 °C and degassed at 100 °C extensively, N2 isotherms were obtained at −196 °C using a NOVA 2200e (Quantachrome Instruments) surface area analyzer. The specific surface area was calculated by applying the Brunauer-Emmett-Teller (BET) equation to the relative pressure range (P/P0) of 0.05-0.30. The pore volume was determined from the amount of N2 adsorbed at the highest relative pressure of P/P0 ≈ 0.99. The average pore diameter was calculated by using the formula, average pore diameter = 4 (pore volume) / (specific surface area). The UV-Vis diffuse reflectance spectra were recorded using a Cary 100 Bio UV-Visible spectrophotometer equipped with a praying mantis diffuse reflection accessory (Harrick Scientific). The band gaps of the materials were calculated extrapolating the high slope region to the X-axis in the Tauc plot obtained by transforming the absorbance plot using the Kubelka-Munk function.
The photocatalytic experiments were carried out as follows. A known amount of the photocatalyst (1 g/L) was suspended in a solution of H2O and methanol (molar ratio of [H2O]/[CH3OH] = 8). The suspension was degassed for 30 min. with high-purity argon prior to irradiation. The suspensions were continuously stirred throughout the course of the experiment. A 300 W Xenon lamp (Oriel light source) with an appropriate filter was used as the source of UV radiation. The amount of H2 produced was measured by gas chromatography (SRI 8610 C) equipped with a molecular sieve column and a TCD detector, and by using a calibration curve prepared previously. Photoluminescence (PL) measurements were carried out on a Horiba Jobin Yvon-Fluoromax 4 instrument. The excitation wavelength used was 300 nm, and the emission spectra were monitored in the range of 375-500 nm.
The powder X-ray diffractograms of the titania materials as a function on aging is shown in Figure 1. After aging for 0.25 day, peaks due to (101), (103), (004), (112), (200), (105), (211), (213), (204), (116), (220), and (215) diffraction planes of the anatase phase only are observed.
Figure 1. Powder X-ray diffractograms of mesostructured titanium dioxide.
After aging for 1 day, a small peak appears at 2θ = 27.7o that is due to (110) diffraction plane of the rutile phase. In addition, anatase phase which is predominant in this material can also be clearly seen. However, after 6 days of aging, the percentage of rutile increases significantly, and peaks due to (110), (101), (111), (210), (211), (220), (310), and (301) diffraction planes of rutile can be observed in addition to the anatase phase. The variation in the phase of titania can be explained as follows.
A typical EISA synthesis involves multiple steps, and the choice of the solvent, acid, amount of water, titania precursor, and surfactant is critical, apart from the aging temperature and time [7]. In the present work, the molar ratio of [water]/[titanium isopropoxide] used was relatively high, i.e. ~17. At such high ratios, both hydrolysis and condensation of the titania precursor occur rapidly. This leads to the formation of titania oxo clusters first, prior to self-assembly. As evaporation of the most volatile component (ethanol) takes place initially, there is an increase in the concentration of the titania oligomers and the non-volatile surfactant. This triggers the self-assembly process and leads to the formation of a titania-surfactant hybrid phase. The hybrid “titaniatropic” phase consists of pre-formed titania nanobuilding blocks that are self-assembled around the surfactant molecules. These interactions are of the type, Ti-OH+…X−…CTAB+, where X represents bromide ions from CTAB, or chloride ions from HCl used in the synthesis. In the next steps, equilibration of water and solvent between the hybrid phase and the environment takes place. The continued evaporation of the solvent (ethanol and water) promotes the formation of a mesostructure. As the aging time is increased, the solution is progressively enriched with acid. Even though, most of the HCl eventually evaporates, some amount of residual Cl− ions persist leading to a condensed mesoporous network of the type TiO2-x/2(OH, Cl)x [23]. It has been reported that as the acid concentration increases, the edge shared bonds between the titania octahedral clusters and oxygen atoms decreases and the corner shared bonds between the titania oxo clusters and oxygen increases [24,25]. In the rutile structure, each titania octahedron is linked to two edge shared and eight corner shared oxygen atoms, respectively. On the other hand, in the anatase structure, the titania octahedron are connected to four edge and four corner sharing oxygen pairs. The reorientation of the TiO6 clusters due to the increase in the localized concentration of acid with aging time results in the formation of rutile phase. Hence, by changing the aging time, one can modulate the phase(s) of titania. In this study, the amount of rutile content continues to progressively increase with increase in aging time. For example, with an aging time of 6 h (TiO2-0.25d), the rutile content was found to be 0% whereas after 6 days of aging (TiO2-6d), a predominantly rutile phase (71%) was obtained. Further increase in aging time does not seem to increase the amount of rutile phase. For sake of briefness, we are discussing results pertaining to aging times of 6 h (TiO2-0.25d), 1 day (TiO2-1d), and 6 days (TiO2-6d) in this study.
Raman studies indicate the presence of only anatase in TiO2-0.25d (Figure 2A) and is consistent with powder XRD studies. Peaks at 148 cm−1 (Eg), 393 cm−1 (B1g),519 cm−1 (A1g and B1g), and 643 cm−1 (Eg) attributed to the anatase phase can be clearly seen. Figure 2B shows the Raman spectra of TiO2-1d. The highest intense peak seems to be slightly shifted to 143 cm−1 (Eg), whereas the other peaks appear at wavenumbers similar to those observed in TiO2-0.25d. However, the Raman spectra of TiO2-1d show phonon modes due to the anatase phase only. This may be due to the relatively low amounts of rutile (5%) and sensitivity of the instrument that preclude the observation of phonon modes of rutile. However, the material aged after 6 days, TiO2-6d show peaks due to both anatase and rutile phases. In addition to the phonon modes of anatase described previously for TiO2-0.25d and TiO2-1d, peaks at 230 cm−1 (Eg), 442 cm−1 (Eg), and 610 cm−1 (A1g) that may be ascribed to the rutile phase can also be seen as indicated in Figure 2C. Thus, the Raman studies confirm the findings of the powder XRD studies.
Figure 2. Raman spectra of A) TiO2-0.25d, B) TiO2-1d, and C) TiO2-6d. A and R in Figure 2C denote anatase and rutile phases respectively.
Transmission electron microscopic (TEM) studies were also conducted to discern the morphology and phase. The TEM image of TiO2-0.25d shown in Figure 3A,indicate the presence of irregularly shaped titania particles that are fairly compact in nature, i.e. less porous in nature. The high resolution TEM images are shown in the inset in Figure 3A. Lattice fringes with d spacing values of 3.50 Å can be seen. This value is close to the d spacing (3.52 Å) of the (101) plane that is predominant in anatase. The TEM of TiO2-6d (Figure 3B) indicate a more open porous structure. The inset in Figure 3B shows the presence of both anatase (due to d (101) with a value of 3.50 Å) and rutile (due to d (110) with a value of 3.23 Å) phases, and is consistent with powder XRD and Raman studies. In summary, powder XRD, Raman, and TEM studies indicate the presence of a mixed phase in the sample aged for 6 days, whereas only anatase phase is present after 6 hours of aging. Aging for 1 day results in the presence of small amounts (5 wt.%) of rutile phase, which can be discerned from powder XRD studies only.
Figure 3. Transmission electron microscopic images of A) TiO2-0.25d and B) TiO2-6d.
The textural properties of the mesostructured materials were investigated, and the results are shown in Figure 4. The materials exhibit type IV (IUPAC classification) isotherms, which are typical of mesoporous materials.
Figure 4. Nitrogen physisorption isotherms of A) TiO2-0.25d, B) TiO2-1d, and C)TiO2-6d. The pore size distribution plots are shown in the inset.
Figure 4A shows the nitrogen isotherm for TiO2-0.25d. At low values of relative pressures (P/P0), monolayer adsorption of N2 takes place. This is followed by multilayer adsorption and capillary condensation at higher relative pressures. Owing to the differences in pressures at which capillary evaporation and condensation take place, the isotherms display hysteresis. The hysteresis observed in this material, can be classified as H1 type. This type of hysteresis loop is typical of materials that contain aggregates that are fairly compact and having high degree of pore uniformity [26]. The pore volume (0.15 cm3/g) and specific surface area (72 m2/g) of this material is relatively low. The inset in Figure 4A shows the pore size distribution. As can be seen in the inset, the pore size is fairly uniform and centered near 80 Å. On increasing the aging time to 1 day, the specific surface area increases dramatically from 72 m2/g (for the sample, TiO2-0.25d) to 161 m2/g in TiO2-1d. The isotherm (Figure 4B) indicates that the hysteresis loops do not level off at relative pressures close to the saturation vapor pressure, suggesting that the materials are composed of loose assemblies of irregular shaped plate-like particles forming slit-like pores of broad pore size distribution. The broad pore size distribution can be seen in the inset in Figure 4B. A hierarchical set of pores centered near 50 Å and 100 Å, and extending into the upper range of mesopore (500 Å) can be observed. Increasing the aging time to 6 days, preserves the mesoporosity and the specific surface area drops slightly to 145 m2/g. However, the pore volume is still large. The isotherm and the pore size distribution for TiO2-6d is shown in Figure 4C. The results are similar to that observed for the sample aged for 1 day,i.e., TiO2-1d. The textural properties of the mesostructured materials are listed in Table 1. In summary, the textural properties of the mesostructured materials indicate that extending the aging time facilitates in creating more open and porous mesostructures with higher specific surface area and larger pore volumes.
| Material | Anatase Crystallite Size (nm)a | Anatase (%)b | Rutile (%)b | Specific Surface Area (m2/g)c | Pore Volume (cc/g)d | Average Pore Diameter (Å) | Bandgap (eV)f | H2 (mmole /g TiO2) |
| TiO2-0.25d | 10 | 100 | 0 | 72 | 0.15 | 84 | 3.22 | 0.27 |
| TiO2-1d | 16 | 95 | 5 | 161 | 0.28 | 70 | 3.09 | 0.51 |
| TiO2-6d | 13 | 29 | 71 | 145 | 0.30 | 83 | 3.04 | 0.09 |
| a. Crystallite size was calculated using the Debye-Scherrer method by selecting the highest intense peak for anatase at 2θ = 25.36° (d101). b. TiO2 phase percentages were calculated using reference intensity ratio (RIR) using the Rigaku PDXL software. c. Specific surface area was determined by applying the Brunauer-Emmett-Teller (BET) equation to the relative pressure range of P/P0 = 0.05-0.30. d. The pore volume was determined from the amount of N2 adsorbed at the highest relative pressure (P/P0) of approximately 0.99. e. The bandgap was estimated by extrapolation of the high slope value from the Kubelka-Munk plot on the X-axis. |
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DownLoad: CSVDiffuse reflectance (DR) spectral studies were carried out in order to discern the band gap. The absorption edge was calculated by plotting the Kubelka-Munk function, [KE] 1/2 against the photon energy, E, measured in eV (Figure 5). The band gap energy (Eg) was estimated by extrapolating the linear portion of the spectra to [KE]1/2 = 0. The DRS studies indicate that the band gap decreases as the rutile content increases, as indicated in Table 1. This is consistent with the fact that the band gap of anatase and rutile are ~3.2 and ~3.0 eV, respectively. Increase in the aging time increases the amount of rutile, and the DRS results obtained in this study are consistent with the expected trend.
Figure 5. Tauc plots (obtained by transformation of the Kubelka-Munk equation) for the mesostructured titanium dioxide materials.
The photocatalytic activity of the materials was investigated, and the results are shown in Figure 6. After four hours of irradiation, the activity is found to be in the order TiO2-1d > TiO2-0.25d > TiO2-6d.
Figure 6. Variation in hydrogen yields for the mesostructured titanium dioxide materials.
TiO2-1d has 95% anatase and 5% rutile phases, whereas TiO2-0.25d has only anatase phase. TiO2-6d showed 29% anatase and 71% rutile. The conduction band edge of rutile is relatively more positive as compared to anatase, and the presence of excess rutile content is detrimental to photocatalytic activity [14]. These results suggest an optimal amount of rutile is conducive to enhanced activity.
The photocatalytic activity of TiO2 is dependent on the crystallinity, crystallite size, surface area, porosity, phase etc. Even though the crystallinity of TiO2-0.25d is higher than that of other materials prepared in this study, its activity is lower in comparison to the material, TiO2-1d. This may be due to its relatively low surface area. The crystallite sizes of the materials lie in a narrow range and cannot account for the differences in activity. The high activity of TiO2-1d may be attributed to its high specific surface area and most importantly because of the presence of an optimal amount of mixed phases of anatase and rutile that minimizes electron-hole recombination. The presence of mixed phases of titania has been shown to have important implications in photocatalysis. The synergistic effect in the material, TiO2-1d is due to the effective trapping and separation of the charge-carriers across the two different crystallite phases [14]. This has been observed previously and our results are consistent with prior observations.
In order to understand the trends in photocatalytic activities, photoluminescence (PL) studies were carried out. PL experiments (Figure 7) confirm the trends in photocatalytic activities. TiO2-1d shows the least emission indicating that the recombination of electron-hole pairs are minimized the most in this material.
Figure 7. Photoluminescence spectral emissions from the mesostructured titanium dioxide materials.
TiO2-6d show higher emission indicating enhanced recombination of the charge-carriers. The high rate of recombination of the charge-carriers results in low activity and the presence of large amounts of rutile is detrimental to its activity because its conduction band is located at relatively more positive values to the H+/H2 redox couple. The emission observed in the mesostructured titania materials are the characteristic emissions due to the recombination of free and bound excitons.
EISA is a versatile method for the preparation of hierarchical mesostructured TiO2. By changing the aging time, one can successfully prepare controlled amounts of mixed phases by using a convenient titania precursor and a readily available surfactant. A mixed mesostructured titania consisting of anatase (95%) and rutile (5%) showed high photocatalytic activity due to minimized electron-hole recombination and enhanced specific surface area. This facile method paves the way for the fabrication of hierarchical porous TiO2 for other applications such as degradation of dyes.
This work was supported by DE-EE-0000270, NSF-CHE-0722632, NSF-CHE-0840507, NSF-DGE-0903685, NSF-EPS-0903804, and SD NASA-EPSCOR NNX12AB17G. We are thankful to Dr. C.Y. Jiang for Raman studies.
The authors declare no conflicts of interest in this paper.
| [1] |
Powers ET, Morimoto RI, Dillin A, et al. (2009) Biological and chemical approaches to diseases of proteostasis deficiency. Annu Rev Biochem 78: 959-991. doi: 10.1146/annurev.biochem.052308.114844
|
| [2] |
Hartl FU, Bracher A, Hayer-Hartl M (2011) Molecular chaperones in protein folding and proteostasis. Nature 475: 324-332. doi: 10.1038/nature10317
|
| [3] |
Balch WE, Morimoto RI, Dillin A, et al. (2008) Adapting proteostasis for disease intervention. Science 319: 916-919. doi: 10.1126/science.1141448
|
| [4] |
Tanaka K (2013) The proteasome: from basic mechanisms to emerging roles. Keio J Med 62: 1-12. doi: 10.2302/kjm.2012-0006-RE
|
| [5] | Wong E, Cuervo AM (2010) Integration of clearance mechanisms: the proteasome and autophagy. Cold Spring Harb Perspect Biol 2: a006734. |
| [6] |
Finley D (2009) Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu Rev Biochem 78: 477-513. doi: 10.1146/annurev.biochem.78.081507.101607
|
| [7] |
Lopez-Otin C, Blasco MA, Partridge L, et al. (2013) The hallmarks of aging. Cell 153: 1194-1217. doi: 10.1016/j.cell.2013.05.039
|
| [8] | Selkoe DJ (2011) Alzheimer's disease. Cold Spring Harb Perspect Biol 3. |
| [9] | Bosco DA, LaVoie MJ, Petsko GA, et al. (2011) Proteostasis and movement disorders: Parkinson's disease and amyotrophic lateral sclerosis. Cold Spring Harb Perspect Biol 3: a007500. |
| [10] | Finkbeiner S (2011) Huntington's Disease. Cold Spring Harb Perspect Biol 3. |
| [11] |
Schmidt M, Finley D (2014) Regulation of proteasome activity in health and disease. Biochim Biophys Acta 1843: 13-25. doi: 10.1016/j.bbamcr.2013.08.012
|
| [12] |
Tanaka K, Matsuda N (2014) Proteostasis and neurodegeneration: the roles of proteasomal degradation and autophagy. Biochim Biophys Acta 1843: 197-204. doi: 10.1016/j.bbamcr.2013.03.012
|
| [13] |
Vernace VA, Schmidt-Glenewinkel T, Figueiredo-Pereira ME (2007) Aging and regulated protein degradation: who has the UPPer hand? Aging Cell 6: 599-606. doi: 10.1111/j.1474-9726.2007.00329.x
|
| [14] | Taylor RC, Dillin A (2011) Aging as an event of proteostasis collapse. Cold Spring Harb Perspect Biol 3. |
| [15] |
Buckley SM, Aranda-Orgilles B, Strikoudis A, et al. (2012) Regulation of pluripotency and cellular reprogramming by the ubiquitin-proteasome system. Cell Stem Cell 11: 783-798. doi: 10.1016/j.stem.2012.09.011
|
| [16] |
Okita Y, Nakayama KI (2012) UPS delivers pluripotency. Cell Stem Cell 11: 728-730. doi: 10.1016/j.stem.2012.11.009
|
| [17] |
Vilchez D, Boyer L, Morantte I, et al. (2012) Increased proteasome activity in human embryonic stem cells is regulated by PSMD11. Nature 489: 304-308. doi: 10.1038/nature11468
|
| [18] |
Iwai K (2012) Diverse ubiquitin signaling in NF-kappaB activation. Trends Cell Biol 22: 355-364. doi: 10.1016/j.tcb.2012.04.001
|
| [19] |
Thrower JS, Hoffman L, Rechsteiner M, et al. (2000) Recognition of the polyubiquitin proteolytic signal. EMBO J 19: 94-102. doi: 10.1093/emboj/19.1.94
|
| [20] |
Kisselev AF, Goldberg AL (2005) Monitoring activity and inhibition of 26S proteasomes with fluorogenic peptide substrates. Methods Enzymol 398: 364-378. doi: 10.1016/S0076-6879(05)98030-0
|
| [21] | Jung T, Höhn A, Grune T (2013) The proteasome and the degradation of oxidized proteins: PartII - proteinoxidationandproteasomaldegradation. Redox Biology 2: 99-104. |
| [22] |
Demartino GN, Gillette TG (2007) Proteasomes: machines for all reasons. Cell 129: 659-662. doi: 10.1016/j.cell.2007.05.007
|
| [23] | Forster A, Masters EI, Whitby FG, et al. (2005) The 1.9 A structure of a proteasome-11S activator complex and implications for proteasome-PAN/PA700 interactions. Mol Cell 18: 589-599. |
| [24] | Dubiel W, Pratt G, Ferrell K, et al. (1992) Purification of an 11 S regulator of the multicatalytic protease. J Biol Chem 267: 22369-22377. |
| [25] | Ma CP, Slaughter CA, DeMartino GN (1992) Identification, purification, and characterization of a protein activator (PA28) of the 20 S proteasome (macropain). J Biol Chem 267: 10515-10523. |
| [26] |
Realini C, Jensen CC, Zhang Z, et al. (1997) Characterization of recombinant REGalpha, REGbeta, and REGgamma proteasome activators. J Biol Chem 272: 25483-25492. doi: 10.1074/jbc.272.41.25483
|
| [27] |
Sijts A, Sun Y, Janek K, et al. (2002) The role of the proteasome activator PA28 in MHC class I antigen processing. Mol Immunol 39: 165-169. doi: 10.1016/S0161-5890(02)00099-8
|
| [28] |
Li X, Amazit L, Long W, et al. (2007) Ubiquitin- and ATP-independent proteolytic turnover of p21 by the REGgamma-proteasome pathway. Mol Cell 26: 831-842. doi: 10.1016/j.molcel.2007.05.028
|
| [29] |
Blickwedehl J, Agarwal M, Seong C, et al. (2008) Role for proteasome activator PA200 and postglutamyl proteasome activity in genomic stability. Proc Natl Acad Sci U S A 105: 16165-16170. doi: 10.1073/pnas.0803145105
|
| [30] |
Schmidt M, Haas W, Crosas B, et al. (2005) The HEAT repeat protein Blm10 regulates the yeast proteasome by capping the core particle. Nat Struct Mol Biol 12: 294-303. doi: 10.1038/nsmb914
|
| [31] |
Egan D, Kim J, Shaw RJ, et al. (2011) The autophagy initiating kinase ULK1 is regulated via opposing phosphorylation by AMPK and mTOR. Autophagy 7: 643-644. doi: 10.4161/auto.7.6.15123
|
| [32] |
Rubinsztein DC, Marino G, Kroemer G (2011) Autophagy and aging. Cell 146: 682-695. doi: 10.1016/j.cell.2011.07.030
|
| [33] |
Ravikumar B, Sarkar S, Davies JE, et al. (2010) Regulation of mammalian autophagy in physiology and pathophysiology. Physiol Rev 90: 1383-1435. doi: 10.1152/physrev.00030.2009
|
| [34] |
Nixon RA (2013) The role of autophagy in neurodegenerative disease. Nat Med 19: 983-997. doi: 10.1038/nm.3232
|
| [35] |
Martinez-Vicente M, Cuervo AM (2007) Autophagy and neurodegeneration: when the cleaning crew goes on strike. Lancet Neurol 6: 352-361. doi: 10.1016/S1474-4422(07)70076-5
|
| [36] |
Cuervo AM (2004) Autophagy: in sickness and in health. Trends Cell Biol 14: 70-77. doi: 10.1016/j.tcb.2003.12.002
|
| [37] |
Mizushima N, Levine B, Cuervo AM, et al. (2008) Autophagy fights disease through cellular self-digestion. Nature 451: 1069-1075. doi: 10.1038/nature06639
|
| [38] |
Mizushima N, Komatsu M (2011) Autophagy: renovation of cells and tissues. Cell 147: 728-741. doi: 10.1016/j.cell.2011.10.026
|
| [39] |
Cuervo AM (2010) Chaperone-mediated autophagy: selectivity pays off. Trends Endocrinol Metab 21: 142-150. doi: 10.1016/j.tem.2009.10.003
|
| [40] |
He C, Klionsky DJ (2009) Regulation mechanisms and signaling pathways of autophagy. Annu Rev Genet 43: 67-93. doi: 10.1146/annurev-genet-102808-114910
|
| [41] |
Klionsky DJ, Cregg JM, Dunn WA, Jr., et al. (2003) A unified nomenclature for yeast autophagy-related genes. Dev Cell 5: 539-545. doi: 10.1016/S1534-5807(03)00296-X
|
| [42] |
Dubouloz F, Deloche O, Wanke V, et al. (2005) The TOR and EGO protein complexes orchestrate microautophagy in yeast. Mol Cell 19: 15-26. doi: 10.1016/j.molcel.2005.05.020
|
| [43] |
Marzella L, Ahlberg J, Glaumann H (1981) Autophagy, heterophagy, microautophagy and crinophagy as the means for intracellular degradation. Virchows Arch B Cell Pathol Incl Mol Pathol 36: 219-234. doi: 10.1007/BF02912068
|
| [44] | Mortimore GE, Lardeux BR, Adams CE (1988) Regulation of microautophagy and basal protein turnover in rat liver. Effects of short-term starvation. J Biol Chem 263: 2506-2512. |
| [45] |
Cuervo AM, Dice JF (1996) A receptor for the selective uptake and degradation of proteins by lysosomes. Science 273: 501-503. doi: 10.1126/science.273.5274.501
|
| [46] |
Rubinsztein DC, DiFiglia M, Heintz N, et al. (2005) Autophagy and its possible roles in nervous system diseases, damage and repair. Autophagy 1: 11-22. doi: 10.4161/auto.1.1.1513
|
| [47] |
Lee CK, Klopp RG, Weindruch R, et al. (1999) Gene expression profile of aging and its retardation by caloric restriction. Science 285: 1390-1393. doi: 10.1126/science.285.5432.1390
|
| [48] |
Ly DH, Lockhart DJ, Lerner RA, et al. (2000) Mitotic misregulation and human aging. Science 287: 2486-2492. doi: 10.1126/science.287.5462.2486
|
| [49] | Ferrington DA, Husom AD, Thompson LV (2005) Altered proteasome structure, function, and oxidation in aged muscle. FASEB J 19: 644-646. |
| [50] |
Vernace VA, Arnaud L, Schmidt-Glenewinkel T, et al. (2007) Aging perturbs 26S proteasome assembly in Drosophila melanogaster. FASEB J 21: 2672-2682. doi: 10.1096/fj.06-6751com
|
| [51] |
Grune T, Jung T, Merker K, et al. (2004) Decreased proteolysis caused by protein aggregates, inclusion bodies, plaques, lipofuscin, ceroid, and 'aggresomes' during oxidative stress, aging, and disease. Int J Biochem Cell Biol 36: 2519-2530. doi: 10.1016/j.biocel.2004.04.020
|
| [52] | Andersson V, Hanzen S, Liu B, et al. (2013) Enhancing protein disaggregation restores proteasome activity in aged cells. Aging (Albany NY) 11: 802-812. |
| [53] |
Bulteau AL, Petropoulos I, Friguet B (2000) Age-related alterations of proteasome structure and function in aging epidermis. Exp Gerontol 35: 767-777. doi: 10.1016/S0531-5565(00)00136-4
|
| [54] |
Carrard G, Dieu M, Raes M, et al. (2003) Impact of ageing on proteasome structure and function in human lymphocytes. Int J Biochem Cell Biol 35: 728-739. doi: 10.1016/S1357-2725(02)00356-4
|
| [55] |
Chondrogianni N, Stratford FL, Trougakos IP, et al. (2003) Central role of the proteasome in senescence and survival of human fibroblasts: induction of a senescence-like phenotype upon its inhibition and resistance to stress upon its activation. J Biol Chem 278: 28026-28037. doi: 10.1074/jbc.M301048200
|
| [56] |
Petropoulos I, Conconi M, Wang X, et al. (2000) Increase of oxidatively modified protein is associated with a decrease of proteasome activity and content in aging epidermal cells. J Gerontol A Biol Sci Med Sci 55: B220-227. doi: 10.1093/gerona/55.5.B220
|
| [57] |
Wagner BJ, Margolis JW (1995) Age-dependent association of isolated bovine lens multicatalytic proteinase complex (proteasome) with heat-shock protein 90, an endogenous inhibitor. Arch Biochem Biophys 323: 455-462. doi: 10.1006/abbi.1995.0067
|
| [58] |
Bardag-Gorce F, Farout L, Veyrat-Durebex C, et al. (1999) Changes in 20S proteasome activity during ageing of the LOU rat. Mol Biol Rep 26: 89-93. doi: 10.1023/A:1006968208077
|
| [59] |
Bulteau AL, Szweda LI, Friguet B (2002) Age-dependent declines in proteasome activity in the heart. Arch Biochem Biophys 397: 298-304. doi: 10.1006/abbi.2001.2663
|
| [60] |
Conconi M, Szweda LI, Levine RL, et al. (1996) Age-related decline of rat liver multicatalytic proteinase activity and protection from oxidative inactivation by heat-shock protein 90. Arch Biochem Biophys 331: 232-240. doi: 10.1006/abbi.1996.0303
|
| [61] |
Husom AD, Peters EA, Kolling EA, et al. (2004) Altered proteasome function and subunit composition in aged muscle. Arch Biochem Biophys 421: 67-76. doi: 10.1016/j.abb.2003.10.010
|
| [62] |
Keller JN, Hanni KB, Markesbery WR (2000) Possible involvement of proteasome inhibition in aging: implications for oxidative stress. Mech Ageing Dev 113: 61-70. doi: 10.1016/S0047-6374(99)00101-3
|
| [63] | Shibatani T, Nazir M, Ward WF (1996) Alteration of rat liver 20S proteasome activities by age and food restriction. J Gerontol A Biol Sci Med Sci 51: B316-322. |
| [64] |
Tomaru U, Takahashi S, Ishizu A, et al. (2012) Decreased proteasomal activity causes age-related phenotypes and promotes the development of metabolic abnormalities. Am J Pathol 180: 963-972. doi: 10.1016/j.ajpath.2011.11.012
|
| [65] |
Bergamini E (2006) Autophagy: a cell repair mechanism that retards ageing and age-associated diseases and can be intensified pharmacologically. Mol Aspects Med 27: 403-410. doi: 10.1016/j.mam.2006.08.001
|
| [66] |
Cuervo AM (2008) Autophagy and aging: keeping that old broom working. Trends Genet 24: 604-612. doi: 10.1016/j.tig.2008.10.002
|
| [67] |
Cuervo AM, Dice JF (2000) Age-related decline in chaperone-mediated autophagy. J Biol Chem 275: 31505-31513. doi: 10.1074/jbc.M002102200
|
| [68] | Terman A (1995) The effect of age on formation and elimination of autophagic vacuoles in mouse hepatocytes. Gerontology 41 Suppl 2: 319-326. |
| [69] |
Vittorini S, Paradiso C, Donati A, et al. (1999) The age-related accumulation of protein carbonyl in rat liver correlates with the age-related decline in liver proteolytic activities. J Gerontol A Biol Sci Med Sci 54: B318-323. doi: 10.1093/gerona/54.8.B318
|
| [70] |
Terman A, Brunk UT (2006) Oxidative stress, accumulation of biological 'garbage', and aging. Antioxid Redox Signal 8: 197-204. doi: 10.1089/ars.2006.8.197
|
| [71] |
Yen WL, Klionsky DJ (2008) How to live long and prosper: autophagy, mitochondria, and aging. Physiology (Bethesda) 23: 248-262. doi: 10.1152/physiol.00013.2008
|
| [72] |
Lipinski MM, Zheng B, Lu T, et al. (2010) Genome-wide analysis reveals mechanisms modulating autophagy in normal brain aging and in Alzheimer's disease. Proc Natl Acad Sci U S A 107: 14164-14169. doi: 10.1073/pnas.1009485107
|
| [73] | Carames B, Taniguchi N, Otsuki S, et al. (2010) Autophagy is a protective mechanism in normal cartilage, and its aging-related loss is linked with cell death and osteoarthritis. Arthritis Rheum 62: 791-801. |
| [74] |
Donati A, Cavallini G, Paradiso C, et al. (2001) Age-related changes in the regulation of autophagic proteolysis in rat isolated hepatocytes. J Gerontol A Biol Sci Med Sci 56: B288-293. doi: 10.1093/gerona/56.7.B288
|
| [75] |
Matecic M, Smith DL, Pan X, et al. (2010) A microarray-based genetic screen for yeast chronological aging factors. PLoS Genet 6: e1000921. doi: 10.1371/journal.pgen.1000921
|
| [76] |
Hars ES, Qi H, Ryazanov AG, et al. (2007) Autophagy regulates ageing in C. elegans. Autophagy 3: 93-95. doi: 10.4161/auto.3636
|
| [77] |
Toth ML, Sigmond T, Borsos E, et al. (2008) Longevity pathways converge on autophagy genes to regulate life span in Caenorhabditis elegans. Autophagy 4: 330-338. doi: 10.4161/auto.5618
|
| [78] |
Simonsen A, Cumming RC, Brech A, et al. (2008) Promoting basal levels of autophagy in the nervous system enhances longevity and oxidant resistance in adult Drosophila. Autophagy 4: 176-184. doi: 10.4161/auto.5269
|
| [79] |
Kuma A, Hatano M, Matsui M, et al. (2004) The role of autophagy during the early neonatal starvation period. Nature 432: 1032-1036. doi: 10.1038/nature03029
|
| [80] |
Levine B, Kroemer G (2008) Autophagy in the pathogenesis of disease. Cell 132: 27-42. doi: 10.1016/j.cell.2007.12.018
|
| [81] |
Hara T, Nakamura K, Matsui M, et al. (2006) Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice. Nature 441: 885-889. doi: 10.1038/nature04724
|
| [82] |
Komatsu M, Waguri S, Chiba T, et al. (2006) Loss of autophagy in the central nervous system causes neurodegeneration in mice. Nature 441: 880-884. doi: 10.1038/nature04723
|
| [83] |
Komatsu M, Wang QJ, Holstein GR, et al. (2007) Essential role for autophagy protein Atg7 in the maintenance of axonal homeostasis and the prevention of axonal degeneration. Proc Natl Acad Sci U S A 104: 14489-14494. doi: 10.1073/pnas.0701311104
|
| [84] |
Liang CC, Wang C, Peng X, et al. (2010) Neural-specific deletion of FIP200 leads to cerebellar degeneration caused by increased neuronal death and axon degeneration. J Biol Chem 285: 3499-3509. doi: 10.1074/jbc.M109.072389
|
| [85] |
Masiero E, Agatea L, Mammucari C, et al. (2009) Autophagy is required to maintain muscle mass. Cell Metab 10: 507-515. doi: 10.1016/j.cmet.2009.10.008
|
| [86] |
Singh R, Kaushik S, Wang Y, et al. (2009) Autophagy regulates lipid metabolism. Nature 458: 1131-1135. doi: 10.1038/nature07976
|
| [87] |
Yang L, Li P, Fu S, et al. (2010) Defective hepatic autophagy in obesity promotes ER stress and causes insulin resistance. Cell Metab 11: 467-478. doi: 10.1016/j.cmet.2010.04.005
|
| [88] |
Jung HS, Chung KW, Won Kim J, et al. (2008) Loss of autophagy diminishes pancreatic beta cell mass and function with resultant hyperglycemia. Cell Metab 8: 318-324. doi: 10.1016/j.cmet.2008.08.013
|
| [89] |
Hartleben B, Godel M, Meyer-Schwesinger C, et al. (2010) Autophagy influences glomerular disease susceptibility and maintains podocyte homeostasis in aging mice. J Clin Invest 120: 1084-1096. doi: 10.1172/JCI39492
|
| [90] | Dice JF (1982) Altered degradation of proteins microinjected into senescent human fibroblasts. J Biol Chem 257: 14624-14627. |
| [91] |
Kiffin R, Kaushik S, Zeng M, et al. (2007) Altered dynamics of the lysosomal receptor for chaperone-mediated autophagy with age. J Cell Sci 120: 782-791. doi: 10.1242/jcs.001073
|
| [92] |
Zhang C, Cuervo AM (2008) Restoration of chaperone-mediated autophagy in aging liver improves cellular maintenance and hepatic function. Nat Med 14: 959-965. doi: 10.1038/nm.1851
|
| [93] |
Bandyopadhyay U, Kaushik S, Varticovski L, et al. (2008) The chaperone-mediated autophagy receptor organizes in dynamic protein complexes at the lysosomal membrane. Mol Cell Biol 28: 5747-5763. doi: 10.1128/MCB.02070-07
|
| [94] |
Soti C, Csermely P (2003) Aging and molecular chaperones. Exp Gerontol 38: 1037-1040. doi: 10.1016/S0531-5565(03)00185-2
|
| [95] |
Nardai G, Csermely P, Soti C (2002) Chaperone function and chaperone overload in the aged. A preliminary analysis. Exp Gerontol 37: 1257-1262. doi: 10.1016/S0531-5565(02)00134-1
|
| [96] |
Cohen E, Dillin A (2008) The insulin paradox: aging, proteotoxicity and neurodegeneration. Nat Rev Neurosci 9: 759-767. doi: 10.1038/nrn2474
|
| [97] |
Zabel C, Nguyen HP, Hin SC, et al. (2010) Proteasome and oxidative phoshorylation changes may explain why aging is a risk factor for neurodegenerative disorders. J Proteomics 73: 2230-2238. doi: 10.1016/j.jprot.2010.08.008
|
| [98] | Matsuda N, Tanaka K (2010) Does impairment of the ubiquitin-proteasome system or the autophagy-lysosome pathway predispose individuals to neurodegenerative disorders such as Parkinson's disease? J Alzheimers Dis 19: 1-9. |
| [99] |
Saez I, Vilchez D (2014) The Mechanistic Links Between Proteasome Activity, Aging and Age-related Diseases. Curr Genomics 15: 38-51. doi: 10.2174/138920291501140306113344
|
| [100] |
Massey AC, Kaushik S, Sovak G, et al. (2006) Consequences of the selective blockage of chaperone-mediated autophagy. Proc Natl Acad Sci U S A 103: 5805-5810. doi: 10.1073/pnas.0507436103
|
| [101] |
Ravikumar B, Vacher C, Berger Z, et al. (2004) Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease. Nat Genet 36: 585-595. doi: 10.1038/ng1362
|
| [102] |
Cuervo AM (2006) Autophagy in neurons: it is not all about food. Trends Mol Med 12: 461-464. doi: 10.1016/j.molmed.2006.08.003
|
| [103] |
Keck S, Nitsch R, Grune T, et al. (2003) Proteasome inhibition by paired helical filament-tau in brains of patients with Alzheimer's disease. J Neurochem 85: 115-122. doi: 10.1046/j.1471-4159.2003.01642.x
|
| [104] |
Grune T, Botzen D, Engels M, et al. (2010) Tau protein degradation is catalyzed by the ATP/ubiquitin-independent 20S proteasome under normal cell conditions. Arch Biochem Biophys 500: 181-188. doi: 10.1016/j.abb.2010.05.008
|
| [105] |
Dickey CA, Koren J, Zhang YJ, et al. (2008) Akt and CHIP coregulate tau degradation through coordinated interactions. Proc Natl Acad Sci U S A 105: 3622-3627. doi: 10.1073/pnas.0709180105
|
| [106] |
Petrucelli L, Dickson D, Kehoe K, et al. (2004) CHIP and Hsp70 regulate tau ubiquitination, degradation and aggregation. Hum Mol Genet 13: 703-714. doi: 10.1093/hmg/ddh083
|
| [107] |
Dange T, Smith D, Noy T, et al. (2011) Blm10 protein promotes proteasomal substrate turnover by an active gating mechanism. J Biol Chem 286: 42830-42839. doi: 10.1074/jbc.M111.300178
|
| [108] |
Jinwal UK, Koren J, 3rd, Borysov SI, et al. (2010) The Hsp90 cochaperone, FKBP51, increases Tau stability and polymerizes microtubules. J Neurosci 30: 591-599. doi: 10.1523/JNEUROSCI.4815-09.2010
|
| [109] |
Blair LJ, Nordhues BA, Hill SE, et al. (2013) Accelerated neurodegeneration through chaperone-mediated oligomerization of tau. J Clin Invest 123: 4158-4169. doi: 10.1172/JCI69003
|
| [110] | Nixon RA, Wegiel J, Kumar A, et al. (2005) Extensive involvement of autophagy in Alzheimer disease: an immuno-electron microscopy study. J Neuropathol Exp Neurol 64: 113-122. |
| [111] | Berger Z, Ravikumar B, Menzies FM, et al. (2006) Rapamycin alleviates toxicity of different aggregate-prone proteins. Hum Mol Genet 15: 433-442. |
| [112] |
Caccamo A, Majumder S, Richardson A, et al. (2010) Molecular interplay between mammalian target of rapamycin (mTOR), amyloid-beta, and Tau: effects on cognitive impairments. J Biol Chem 285: 13107-13120. doi: 10.1074/jbc.M110.100420
|
| [113] |
Tseng BP, Green KN, Chan JL, et al. (2008) Abeta inhibits the proteasome and enhances amyloid and tau accumulation. Neurobiol Aging 29: 1607-1618. doi: 10.1016/j.neurobiolaging.2007.04.014
|
| [114] |
Yu WH, Cuervo AM, Kumar A, et al. (2005) Macroautophagy--a novel Beta-amyloid peptide-generating pathway activated in Alzheimer's disease. J Cell Biol 171: 87-98. doi: 10.1083/jcb.200505082
|
| [115] |
Cataldo AM, Barnett JL, Berman SA, et al. (1995) Gene expression and cellular content of cathepsin D in Alzheimer's disease brain: evidence for early up-regulation of the endosomal-lysosomal system. Neuron 14: 671-680. doi: 10.1016/0896-6273(95)90324-0
|
| [116] |
Boland B, Kumar A, Lee S, et al. (2008) Autophagy induction and autophagosome clearance in neurons: relationship to autophagic pathology in Alzheimer's disease. J Neurosci 28: 6926-6937. doi: 10.1523/JNEUROSCI.0800-08.2008
|
| [117] |
Rozmahel R, Huang J, Chen F, et al. (2002) Normal brain development in PS1 hypomorphic mice with markedly reduced gamma-secretase cleavage of betaAPP. Neurobiol Aging 23: 187-194. doi: 10.1016/S0197-4580(01)00267-6
|
| [118] | Pickford F, Masliah E, Britschgi M, et al. (2008) The autophagy-related protein beclin 1 shows reduced expression in early Alzheimer disease and regulates amyloid beta accumulation in mice. J Clin Invest 118: 2190-2199. |
| [119] |
Jaeger PA, Pickford F, Sun CH, et al. (2010) Regulation of amyloid precursor protein processing by the Beclin 1 complex. PLoS One 5: e11102. doi: 10.1371/journal.pone.0011102
|
| [120] |
McNaught KS, Perl DP, Brownell AL, et al. (2004) Systemic exposure to proteasome inhibitors causes a progressive model of Parkinson's disease. Ann Neurol 56: 149-162. doi: 10.1002/ana.20186
|
| [121] |
Bedford L, Hay D, Devoy A, et al. (2008) Depletion of 26S proteasomes in mouse brain neurons causes neurodegeneration and Lewy-like inclusions resembling human pale bodies. J Neurosci 28: 8189-8198. doi: 10.1523/JNEUROSCI.2218-08.2008
|
| [122] |
Wahl C, Kautzmann S, Krebiehl G, et al. (2008) A comprehensive genetic study of the proteasomal subunit S6 ATPase in German Parkinson's disease patients. J Neural Transm 115: 1141-1148. doi: 10.1007/s00702-008-0054-3
|
| [123] |
Tofaris GK, Layfield R, Spillantini MG (2001) alpha-synuclein metabolism and aggregation is linked to ubiquitin-independent degradation by the proteasome. FEBS Lett 509: 22-26. doi: 10.1016/S0014-5793(01)03115-5
|
| [124] | Anglade P, Vyas S, Javoy-Agid F, et al. (1997) Apoptosis and autophagy in nigral neurons of patients with Parkinson's disease. Histol Histopathol 12: 25-31. |
| [125] |
Vogiatzi T, Xilouri M, Vekrellis K, et al. (2008) Wild type alpha-synuclein is degraded by chaperone-mediated autophagy and macroautophagy in neuronal cells. J Biol Chem 283: 23542-23556. doi: 10.1074/jbc.M801992200
|
| [126] |
Webb JL, Ravikumar B, Atkins J, et al. (2003) Alpha-Synuclein is degraded by both autophagy and the proteasome. J Biol Chem 278: 25009-25013. doi: 10.1074/jbc.M300227200
|
| [127] |
Cuervo AM, Stefanis L, Fredenburg R, et al. (2004) Impaired degradation of mutant alpha-synuclein by chaperone-mediated autophagy. Science 305: 1292-1295. doi: 10.1126/science.1101738
|
| [128] |
Spencer B, Potkar R, Trejo M, et al. (2009) Beclin 1 gene transfer activates autophagy and ameliorates the neurodegenerative pathology in alpha-synuclein models of Parkinson's and Lewy body diseases. J Neurosci 29: 13578-13588. doi: 10.1523/JNEUROSCI.4390-09.2009
|
| [129] |
Narendra D, Tanaka A, Suen DF, et al. (2008) Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J Cell Biol 183: 795-803. doi: 10.1083/jcb.200809125
|
| [130] |
Narendra DP, Jin SM, Tanaka A, et al. (2010) PINK1 is selectively stabilized on impaired mitochondria to activate Parkin. PLoS Biol 8: e1000298. doi: 10.1371/journal.pbio.1000298
|
| [131] |
Tashiro Y, Urushitani M, Inoue H, et al. (2012) Motor neuron-specific disruption of proteasomes, but not autophagy, replicates amyotrophic lateral sclerosis. J Biol Chem 287: 42984-42994. doi: 10.1074/jbc.M112.417600
|
| [132] |
Gusella JF, MacDonald ME, Ambrose CM, et al. (1993) Molecular genetics of Huntington's disease. Arch Neurol 50: 1157-1163. doi: 10.1001/archneur.1993.00540110037003
|
| [133] |
Vonsattel JP, DiFiglia M (1998) Huntington disease. J Neuropathol Exp Neurol 57: 369-384. doi: 10.1097/00005072-199805000-00001
|
| [134] | (1993) A novel gene containing a trinucleotide repeat that is expanded and unstable on Huntington's disease chromosomes. The Huntington's Disease Collaborative Research Group. Cell 72: 971-983. |
| [135] |
Sanchez I, Mahlke C, Yuan J (2003) Pivotal role of oligomerization in expanded polyglutamine neurodegenerative disorders. Nature 421: 373-379. doi: 10.1038/nature01301
|
| [136] |
Snell RG, MacMillan JC, Cheadle JP, et al. (1993) Relationship between trinucleotide repeat expansion and phenotypic variation in Huntington's disease. Nat Genet 4: 393-397. doi: 10.1038/ng0893-393
|
| [137] |
Nance MA, Myers RH (2001) Juvenile onset Huntington's disease--clinical and research perspectives. Ment Retard Dev Disabil Res Rev 7: 153-157. doi: 10.1002/mrdd.1022
|
| [138] |
Holmberg CI, Staniszewski KE, Mensah KN, et al. (2004) Inefficient degradation of truncated polyglutamine proteins by the proteasome. EMBO J 23: 4307-4318. doi: 10.1038/sj.emboj.7600426
|
| [139] |
Seo H, Sonntag KC, Kim W, et al. (2007) Proteasome activator enhances survival of Huntington's disease neuronal model cells. PLoS One 2: e238. doi: 10.1371/journal.pone.0000238
|
| [140] | Vilchez D, Morantte I, Liu Z, et al. (2012) RPN-6 determines C. elegans longevity under proteotoxic stress conditions. Nature 489: 263-268. |
| [141] |
Tonoki A, Kuranaga E, Tomioka T, et al. (2009) Genetic evidence linking age-dependent attenuation of the 26S proteasome with the aging process. Mol Cell Biol 29: 1095-1106. doi: 10.1128/MCB.01227-08
|
| [142] |
Hipp MS, Patel CN, Bersuker K, et al. (2012) Indirect inhibition of 26S proteasome activity in a cellular model of Huntington's disease. J Cell Biol 196: 573-587. doi: 10.1083/jcb.201110093
|
| [143] |
Kalchman MA, Graham RK, Xia G, et al. (1996) Huntingtin is ubiquitinated and interacts with a specific ubiquitin-conjugating enzyme. J Biol Chem 271: 19385-19394. doi: 10.1074/jbc.271.32.19385
|
| [144] |
Finkbeiner S, Mitra S (2008) The ubiquitin-proteasome pathway in Huntington's disease. ScientificWorldJournal 8: 421-433. doi: 10.1100/tsw.2008.60
|
| [145] |
Sieradzan KA, Mechan AO, Jones L, et al. (1999) Huntington's disease intranuclear inclusions contain truncated, ubiquitinated huntingtin protein. Exp Neurol 156: 92-99. doi: 10.1006/exnr.1998.7005
|
| [146] |
Waelter S, Boeddrich A, Lurz R, et al. (2001) Accumulation of mutant huntingtin fragments in aggresome-like inclusion bodies as a result of insufficient protein degradation. Mol Biol Cell 12: 1393-1407. doi: 10.1091/mbc.12.5.1393
|
| [147] |
Ardley HC, Hung CC, Robinson PA (2005) The aggravating role of the ubiquitin-proteasome system in neurodegeneration. FEBS Lett 579: 571-576. doi: 10.1016/j.febslet.2004.12.058
|
| [148] |
Ciechanover A, Brundin P (2003) The ubiquitin proteasome system in neurodegenerative diseases: sometimes the chicken, sometimes the egg. Neuron 40: 427-446. doi: 10.1016/S0896-6273(03)00606-8
|
| [149] |
Venkatraman P, Wetzel R, Tanaka M, et al. (2004) Eukaryotic proteasomes cannot digest polyglutamine sequences and release them during degradation of polyglutamine-containing proteins. Mol Cell 14: 95-104. doi: 10.1016/S1097-2765(04)00151-0
|
| [150] |
Bennett EJ, Bence NF, Jayakumar R, et al. (2005) Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation. Mol Cell 17: 351-365. doi: 10.1016/j.molcel.2004.12.021
|
| [151] |
Pratt G, Rechsteiner M (2008) Proteasomes cleave at multiple sites within polyglutamine tracts: activation by PA28gamma(K188E). J Biol Chem 283: 12919-12925. doi: 10.1074/jbc.M709347200
|
| [152] |
Tellez-Nagel I, Johnson AB, Terry RD (1974) Studies on brain biopsies of patients with Huntington's chorea. J Neuropathol Exp Neurol 33: 308-332. doi: 10.1097/00005072-197404000-00008
|
| [153] |
Qin ZH, Wang Y, Kegel KB, et al. (2003) Autophagy regulates the processing of amino terminal huntingtin fragments. Hum Mol Genet 12: 3231-3244. doi: 10.1093/hmg/ddg346
|
| [154] |
Ravikumar B, Duden R, Rubinsztein DC (2002) Aggregate-prone proteins with polyglutamine and polyalanine expansions are degraded by autophagy. Hum Mol Genet 11: 1107-1117. doi: 10.1093/hmg/11.9.1107
|
| [155] |
Sarkar S, Perlstein EO, Imarisio S, et al. (2007) Small molecules enhance autophagy and reduce toxicity in Huntington's disease models. Nat Chem Biol 3: 331-338. doi: 10.1038/nchembio883
|
| [156] |
Martinez-Vicente M, Talloczy Z, Wong E, et al. (2010) Cargo recognition failure is responsible for inefficient autophagy in Huntington's disease. Nat Neurosci 13: 567-576. doi: 10.1038/nn.2528
|
| [157] |
Shibata M, Lu T, Furuya T, et al. (2006) Regulation of intracellular accumulation of mutant Huntingtin by Beclin 1. J Biol Chem 281: 14474-14485. doi: 10.1074/jbc.M600364200
|
| [158] |
Atwal RS, Truant R (2008) A stress sensitive ER membrane-association domain in Huntingtin protein defines a potential role for Huntingtin in the regulation of autophagy. Autophagy 4: 91-93. doi: 10.4161/auto.5201
|
| [159] |
Cattaneo E, Zuccato C, Tartari M (2005) Normal huntingtin function: an alternative approach to Huntington's disease. Nat Rev Neurosci 6: 919-930. doi: 10.1038/nrn1806
|
| [160] |
Ravikumar B, Acevedo-Arozena A, Imarisio S, et al. (2005) Dynein mutations impair autophagic clearance of aggregate-prone proteins. Nat Genet 37: 771-776. doi: 10.1038/ng1591
|
| [161] |
Hassan WM, Merin DA, Fonte V, et al. (2009) AIP-1 ameliorates beta-amyloid peptide toxicity in a Caenorhabditis elegans Alzheimer's disease model. Hum Mol Genet 18: 2739-2747. doi: 10.1093/hmg/ddp209
|
| [162] |
Yun C, Stanhill A, Yang Y, et al. (2008) Proteasomal adaptation to environmental stress links resistance to proteotoxicity with longevity in Caenorhabditis elegans. Proc Natl Acad Sci U S A 105: 7094-7099. doi: 10.1073/pnas.0707025105
|
| [163] |
Nakatogawa H, Suzuki K, Kamada Y, et al. (2009) Dynamics and diversity in autophagy mechanisms: lessons from yeast. Nat Rev Mol Cell Biol 10: 458-467. doi: 10.1038/nrm2708
|
| [164] |
Xie Z, Klionsky DJ (2007) Autophagosome formation: core machinery and adaptations. Nat Cell Biol 9: 1102-1109. doi: 10.1038/ncb1007-1102
|
| [165] | Yang Z, Klionsky DJ (2009) An overview of the molecular mechanism of autophagy. Curr Top Microbiol Immunol 335: 1-32. |
| [166] |
Hanada T, Noda NN, Satomi Y, et al. (2007) The Atg12-Atg5 conjugate has a novel E3-like activity for protein lipidation in autophagy. J Biol Chem 282: 37298-37302. doi: 10.1074/jbc.C700195200
|
| [167] |
Hanada T, Satomi Y, Takao T, et al. (2009) The amino-terminal region of Atg3 is essential for association with phosphatidylethanolamine in Atg8 lipidation. FEBS Lett 583: 1078-1083. doi: 10.1016/j.febslet.2009.03.009
|
| [168] |
Komatsu M, Waguri S, Ueno T, et al. (2005) Impairment of starvation-induced and constitutive autophagy in Atg7-deficient mice. J Cell Biol 169: 425-434. doi: 10.1083/jcb.200412022
|
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Figures(1) / Tables(1)
Isabel Saez, David Vilchez. Protein clearance mechanisms and their demise in age-related neurodegenerative diseases[J]. AIMS Molecular Science, 2015, 1(1): 1-21. doi: 10.3934/molsci.2015.1.1
| Material | Anatase Crystallite Size (nm)a | Anatase (%)b | Rutile (%)b | Specific Surface Area (m2/g)c | Pore Volume (cc/g)d | Average Pore Diameter (Å) | Bandgap (eV)f | H2 (mmole /g TiO2) |
| TiO2-0.25d | 10 | 100 | 0 | 72 | 0.15 | 84 | 3.22 | 0.27 |
| TiO2-1d | 16 | 95 | 5 | 161 | 0.28 | 70 | 3.09 | 0.51 |
| TiO2-6d | 13 | 29 | 71 | 145 | 0.30 | 83 | 3.04 | 0.09 |
| a. Crystallite size was calculated using the Debye-Scherrer method by selecting the highest intense peak for anatase at 2θ = 25.36° (d101). b. TiO2 phase percentages were calculated using reference intensity ratio (RIR) using the Rigaku PDXL software. c. Specific surface area was determined by applying the Brunauer-Emmett-Teller (BET) equation to the relative pressure range of P/P0 = 0.05-0.30. d. The pore volume was determined from the amount of N2 adsorbed at the highest relative pressure (P/P0) of approximately 0.99. e. The bandgap was estimated by extrapolation of the high slope value from the Kubelka-Munk plot on the X-axis. |
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DownLoad: CSV| Material | Anatase Crystallite Size (nm)a | Anatase (%)b | Rutile (%)b | Specific Surface Area (m2/g)c | Pore Volume (cc/g)d | Average Pore Diameter (Å) | Bandgap (eV)f | H2 (mmole /g TiO2) |
| TiO2-0.25d | 10 | 100 | 0 | 72 | 0.15 | 84 | 3.22 | 0.27 |
| TiO2-1d | 16 | 95 | 5 | 161 | 0.28 | 70 | 3.09 | 0.51 |
| TiO2-6d | 13 | 29 | 71 | 145 | 0.30 | 83 | 3.04 | 0.09 |
| a. Crystallite size was calculated using the Debye-Scherrer method by selecting the highest intense peak for anatase at 2θ = 25.36° (d101). b. TiO2 phase percentages were calculated using reference intensity ratio (RIR) using the Rigaku PDXL software. c. Specific surface area was determined by applying the Brunauer-Emmett-Teller (BET) equation to the relative pressure range of P/P0 = 0.05-0.30. d. The pore volume was determined from the amount of N2 adsorbed at the highest relative pressure (P/P0) of approximately 0.99. e. The bandgap was estimated by extrapolation of the high slope value from the Kubelka-Munk plot on the X-axis. |
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