Measuring in Unfolded Proteins with Tetraphenylethene and its Analogs

2022 ◽  
pp. 3-18
Author(s):  
Shouxiang Zhang ◽  
Yuning Hong
Keyword(s):  
Unfolded Proteins

Inhibition of Autophagy Potentiated Hippocampal Cell Death Induced by Endoplasmic Reticulum Stress and its Activation by Trehalose Failed to be Neuroprotective

2019 ◽  
Vol 16 (1) ◽  
pp. 3-11
Author(s):  
Luisa Halbe ◽  
Abdelhaq Rami
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Death ◽  
Er Stress ◽  
Cell Damage ◽  
Protective Mechanism ◽  
Unfolded Proteins ◽  
Neuronal Viability ◽  
Hippocampal Cell ◽  
Trigger Cell Death ◽  
Autophagy Inhibition

Introduction: Endoplasmic reticulum (ER) stress induced the mobilization of two protein breakdown routes, the proteasomal- and autophagy-associated degradation. During ERassociated degradation, unfolded ER proteins are translocated to the cytosol where they are cleaved by the proteasome. When the accumulation of misfolded or unfolded proteins excels the ER capacity, autophagy can be activated in order to undertake the degradative machinery and to attenuate the ER stress. Autophagy is a mechanism by which macromolecules and defective organelles are included in autophagosomes and delivered to lysosomes for degradation and recycling of bioenergetics substrate. Materials and Methods: Autophagy upon ER stress serves initially as a protective mechanism, however when the stress is more pronounced the autophagic response will trigger cell death. Because autophagy could function as a double edged sword in cell viability, we examined the effects autophagy modulation on ER stress-induced cell death in HT22 murine hippocampal neuronal cells. We investigated the effects of both autophagy-inhibition by 3-methyladenine (3-MA) and autophagy-activation by trehalose on ER-stress induced damage in hippocampal HT22 neurons. We evaluated the expression of ER stress- and autophagy-sensors as well as the neuronal viability. Results and Conclusion: Based on our findings, we conclude that under ER-stress conditions, inhibition of autophagy exacerbates cell damage and induction of autophagy by trehalose failed to be neuroprotective.

scholarly journals The Mysterious Unfoldome: Structureless, Underappreciated, Yet Vital Part of Any Given Proteome

2010 ◽  
Vol 2010 ◽  
pp. 1-14 ◽  
Author(s):  
Vladimir N. Uversky
Keyword(s):  
Large Scale ◽  
Intrinsically Disordered Proteins ◽  
Biologically Active ◽  
Disordered Proteins ◽  
Unfolded Proteins ◽  
Intrinsically Disordered ◽  
Proteome Level ◽  
Natively Unfolded ◽  
Natively Unfolded Proteins

Contrarily to the general believe, many biologically active proteins lack stable tertiary and/or secondary structure under physiological conditions in vitro. These intrinsically disordered proteins (IDPs) are highly abundant in nature and many of them are associated with various human diseases. The functional repertoire of IDPs complements the functions of ordered proteins. Since IDPs constitute a significant portion of any given proteome, they can be combined in an unfoldome; which is a portion of the proteome including all IDPs (also known as natively unfolded proteins, therefore, unfoldome), and describing their functions, structures, interactions, evolution, and so forth. Amino acid sequence and compositions of IDPs are very different from those of ordered proteins, making possible reliable identification of IDPs at the proteome level by various computational means. Furthermore, IDPs possess a number of unique structural properties and are characterized by a peculiar conformational behavior, including their high stability against low pH and high temperature and their structural indifference toward the unfolding by strong denaturants. These peculiarities were shown to be useful for elaboration of the experimental techniques for the large-scale identification of IDPs in various organisms. Some of the computational and experimental tools for the unfoldome discovery are discussed in this review.

Effects of charge–charge interactions on dimensions of unfolded proteins: A Monte Carlo study

2003 ◽  
Vol 119 (6) ◽  
pp. 3574-3581 ◽  
Author(s):  
Petras J. Kundrotas ◽  
Andrey Karshikoff
Keyword(s):  
Monte Carlo ◽  
Monte Carlo Study ◽  
Unfolded Proteins ◽  
Charge Interactions

scholarly journals Protein Folding by Domain V of Escherichia coli 23S rRNA: Specificity of RNA-Protein Interactions

2008 ◽  
Vol 190 (9) ◽  
pp. 3344-3352 ◽  
Author(s):  
Dibyendu Samanta ◽  
Debashis Mukhopadhyay ◽  
Saheli Chowdhury ◽  
Jaydip Ghosh ◽  
Saumen Pal ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Protein Folding ◽  
Carbonic Anhydrase ◽  
Protein Interactions ◽  
23S Rrna ◽  
Unfolded Proteins ◽  
Bovine Carbonic Anhydrase ◽  
Egg White Lysozyme ◽  
General Protein ◽  
Domain V

ABSTRACT The peptidyl transferase center, present in domain V of 23S rRNA of eubacteria and large rRNA of plants and animals, can act as a general protein folding modulator. Here we show that a few specific nucleotides in Escherichia coli domain V RNA bind to unfolded proteins and, as shown previously, bring the trapped proteins to a folding-competent state before releasing them. These nucleotides are the same for the proteins studied so far: bovine carbonic anhydrase, lactate dehydrogenase, malate dehydrogenase, and chicken egg white lysozyme. The amino acids that interact with these nucleotides are also found to be specific in the two cases tested: bovine carbonic anhydrase and lysozyme. They are either neutral or positively charged and are present in random coils on the surface of the crystal structure of both the proteins. In fact, two of these amino acid-nucleotide pairs are identical in the two cases. How these features might help the process of protein folding is discussed.

Fold and function of polypeptide transport-associated domains responsible for delivering unfolded proteins to membranes

2008 ◽  
Vol 68 (5) ◽  
pp. 1216-1227 ◽  
Author(s):  
Timothy J. Knowles ◽  
Mark Jeeves ◽  
Saeeda Bobat ◽  
Felician Dancea ◽  
Darren McClelland ◽  
...  
Keyword(s):  
Unfolded Proteins ◽  
And Function

Natively unfolded proteins

2005 ◽  
Vol 15 (1) ◽  
pp. 35-41 ◽  
Author(s):  
Anthony L Fink
Keyword(s):  
Unfolded Proteins ◽  
Natively Unfolded ◽  
Natively Unfolded Proteins
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