The fluorescent characterization of the polymerized microtubule-associated protein Tau

Luo, Jun; He, Rong; Li, Wei

doi:10.1016/s0141-8130(00)00126-4

Cited by 16 publications

(18 citation statements)

References 19 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We prepared Ptau freshly and used it within 1 h. So Ptau probably had no chance to aggregate when the kinetics experiments were carried out. Similarly, the effect on GAPDH inactivation and unfolding was not detected after tau was incubated at 37 mC for 24 h. We believed that tau had been polymerized under the conditions, on the basis of the formation of the new fluorescence at 333 nm [9]. This fluorescence formed when tau was incubated in phosphate or Tris (0.1 M, pH 7.2) buffers at 37 mC for over 24 h. This is to say, tau cannot influence denaturation and renaturation of GAPDH when tau is aggregated.…”

Section: Discussionmentioning

confidence: 92%

“…Luo et al [8,9] observed that a new fluorescence would form during tau polymerization. So, formation of the fluorescence at 333 nm was monitored when tau (0.5 mg\ml) was incubated in 0.05 M phosphate buffer (pH 7.2) at 37 mC overnight, until the emission intensity did not change.…”

Section: Preparation Of Aggregated Taumentioning

confidence: 99%

“…Consequently, we are concerned about the fluorescence background from tau, which might interfere with the fluorescence data of GAPDH. In fact, tau does not contain any Trp residues [30] and its intrinsic fluorescence comes from Tyr residues [9], whose fluorescence intensity is much weaker than that of Trp residues. Furthermore, Tyr residues fluoresce at 304 nm, instead of 335 nm in the case of Trp.…”

Section: Figure 1 Changes In the Intrinsic Fluorescence Of Gapdh Withmentioning

confidence: 99%

“…Solubilization of these filaments reveals that they are composed of the microtubule-associated protein tau [6,7]. In this laboratory, a new fluorescence at 333 nm was detected when tau molecules aggregated [8,9]. Effects of ethanol and acetaldehyde on tau aggregation were studied, with an observation that the two compounds could accelerate tau aggregation [10,11].…”

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Effect of human neuronal tau on denaturation and reactivation of rabbit muscle D-glyceraldehyde-3-phosphate dehydrogenase

CHEN

Liu

et al. 2000

Biochemical Journal

View full text Add to dashboard Cite

Human neuronal tau-40 (htau-40) has been used to study denaturation and renaturation of rabbit muscle -glyceraldehyde-3-phosphate dehydrogenase (GAPDH, EC 1.2.1.12). Inactivation of GAPDH incubated with tau was more distinguishably detected than that of control GAPDH during thermal and guanidine hydrochloride (GdnHCl) denaturation. However, tau did not influence the activity of GAPDH at room temperature or in solution without GdnHCl. A marked change in both the emission intensity and emission maximum of the intrinsic fluorescence at 335 nm of GAPDH with tau was observed when GdnHCl concentration was 0.8 M, but that of the control without tau occurred in 1.2 M GdnHCl. The firstorder rate of the decrease in the fluorescence intensity of the enzyme with tau was approximately twice as great as that of GAPDH without tau. Kinetics of inactivation of GAPDH with tau in 0.2 M GdnHCl was a monophasic procedure, instead of

show abstract

Section: Discussionmentioning

confidence: 92%

Section: Preparation Of Aggregated Taumentioning

confidence: 99%

Section: Figure 1 Changes In the Intrinsic Fluorescence Of Gapdh Withmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Effect of human neuronal tau on denaturation and reactivation of rabbit muscle D-glyceraldehyde-3-phosphate dehydrogenase

CHEN

Liu

et al. 2000

Biochemical Journal

View full text Add to dashboard Cite

show abstract

“…In addition, tau is able to stabilize DNA double helices resulting in decrease of the melting temperature, to prevent DNA from denaturation and accelerate the renaturation (30)(31)(32)(33). These effects of tau may be due to its flexibility and worm-like conformation, in which hydrophobic region is exposed and interacts with other proteins (34)(35)(36). Tau is such a flexible protein that it can fold and refold readily by itself, exhibiting resistance to denaturation by heat and denaturants.…”

Section: Introductionmentioning

confidence: 99%

Chaperone-Like Manner of Human Neuronal Tau Towards Lactate Dehydrogenase

Tian

Nie

2004

Neurochem Res

View full text Add to dashboard Cite

In our experiments, inactivation of lactate dehydrogenase (LDH, EC1.1.1.27) in the presence of human microtubule-associated tau is observably suppressed during thermal and guanidine hydrochloride (GdnHCl) denaturation. Kinetic studies show tau can prevent LDH from self-aggregation monitored by light scattering during thermal denaturation. On the other hand, neuronal tau promotes reactivation of LDH and suppresses self-aggregation of non-native LDH when GdnHCl solution is diluted. Furthermore, the reactivation yield of LDH decreases significantly with delayed addition of tau. All experiments were completed in the reducing buffer with 1 mM DTT to avoid between tau and LDH forming the covalent bonds during unfolding and refolding. Thus, Tau prevents proteins from misfolding and aggregating into insoluble, nonfunctional inclusions and assists them to refold to reach the stable native state by binding to the exposed hydrophobic patches on proteins instead of by forming or breaking covalent bonds. Additionally, tau remarkably enhances reactivation of GDH (glutamic dehydrogenase, EC 1.4.1.3), another carbohydrate metabolic enzyme, also showing a chaperone-like manner. It suggests that neuronal tau non-specifically functions a chaperone-like protein towards the enzymes of carbohydrate metabolism.

show abstract

Evaluating triggers and enhancers of tau fibrillization

Kuret

Congdon

et al. 2005

Microscopy Res & Technique

100

View full text Add to dashboard Cite

Alzheimer's disease is characterized in part by the aggregation of tau protein into filamentous inclusions. Because tau filaments form in brain regions associated with memory retention, and because their appearance correlates well with the degree of dementia, they have emerged as robust markers of disease progression. Yet the discovery that mutations in tau protein can lead directly to filament and tangle formation in humans, and that filament formation is linked to neurodegeneration in model biological systems, suggests that tau aggregation may also contribute directly to degeneration in affected neurons. In this context, the mechanism of tau filament formation and its modulation by mutation and posttranslational modification is of fundamental importance. Here, recent progress on the molecular mechanisms underlying tau aggregation deduced from in vivo and in vitro experimentation is reviewed and a model rationalizing the effect of posttranslational and other structural modifications on assembly kinetics and thermodynamics is presented. We hypothesize that tau aggregation can be described as a heterogeneous nucleation reaction, where exogenous effectors, tau gene mutations, or other modifications that stabilize assembly-competent conformations of tau act to trigger the fibrillization reaction. In contrast, those that modulate postnuclear equilibria can enhance fibrillization by increasing the free energy difference between polymers and unincorporated monomers, resulting in stabilization of filaments at low bulk protein concentrations.

show abstract

The fluorescent characterization of the polymerized microtubule-associated protein Tau

Cited by 16 publications

References 19 publications

Effect of human neuronal tau on denaturation and reactivation of rabbit muscle D-glyceraldehyde-3-phosphate dehydrogenase

Effect of human neuronal tau on denaturation and reactivation of rabbit muscle D-glyceraldehyde-3-phosphate dehydrogenase

Chaperone-Like Manner of Human Neuronal Tau Towards Lactate Dehydrogenase

Evaluating triggers and enhancers of tau fibrillization

Contact Info

Product

Resources

About