Review
Biochemistry & Molecular Biology
Roy A. Quinlan, John I. Clark
Summary: In this review, the authors highlight the potential protective effects of post-translational modifications (PTMs) on lens proteins during normal development and propose a forward-looking hypothesis that aims to prevent age-related cataract (ARC) by protecting the biochemical and biophysical properties of lens proteins.
JOURNAL OF BIOLOGICAL CHEMISTRY
(2022)
Article
Biochemistry & Molecular Biology
Jinhee Park, Samantha MacGavin, Laurie Niederbrach, Hassane S. Mchaourab
Summary: A coordinated oxidative stress response, partly triggered by the transcription factor Nrf2, protects cells from harmful reactive oxygen species. The interplay between oxidative stress and chaperone responses in the lens and heart remains unexplored.
FRONTIERS IN MOLECULAR BIOSCIENCES
(2023)
Article
Biochemistry & Molecular Biology
Sidra Islam, Michael T. Do, Brett S. Frank, Grant L. Hom, Samuel Wheeler, Hisashi Fujioka, Benlian Wang, Geeta Minocha, David R. Sell, Xingjun Fan, Kirsten J. Lampi, Vincent M. Monnier
Summary: This study found that closantel and gambogic acid can enhance the stability of α-crystallins and attenuate protein aggregation, potentially providing a therapeutic approach against cataract formation.
JOURNAL OF BIOLOGICAL CHEMISTRY
(2022)
Article
Biochemistry & Molecular Biology
Sidra Islam, Michael T. Do, Brett S. Frank, Grant L. Hom, Samuel Wheeler, Hisashi Fujioka, Benlian Wang, Geeta Minocha, David R. Sell, Xingjun Fan, Kirsten J. Lampi, Vincent M. Monnier
Summary: The drugs closantel and gambogic acid can suppress thermal-induced protein unfolding and aggregation in gamma-crystallins. They bind to hydrophobic sites with medium-to-low affinity. Docking experiments revealed two binding sites for these drugs on gamma-crystallins, overlapping with the binding sites of the protective mini aAcrystallin chaperone MAC peptide.
JOURNAL OF BIOLOGICAL CHEMISTRY
(2022)
Article
Multidisciplinary Sciences
Klaus Hojgaard Jensen, Anna Katharina Stalder, Rasmus Wernersson, Tim-Christoph Roloff-Handschin, Daniel Hvidberg Hansen, Peter M. A. Groenen
Summary: This study investigated the molecular biology of Amyotrophic Lateral Sclerosis (ALS) using protein-protein interaction networks and identified a set of core modules enriched in ALS-associated proteins. These core modules not only captured most of the current knowledge about ALS, but also revealed biological interdependencies and associations with other neurodegenerative diseases. The presence of recently identified ALS-associated proteins in the core modules suggests their potential for identifying novel ALS disease mechanisms.
Article
Cell Biology
Mi-Hyun Nam, Dorota L. Stankowska, Gretchen A. Johnson, Rooban B. Nahomi, Mina B. Pantcheva, Ram H. Nagaraj
Summary: This study investigated the effects of antiapoptotic peptides peptain-1 and peptain-3a on RGC death in vitro and in animal models of ocular hypertension. The results showed that peptains inhibited RGC apoptosis, restricted RGC loss in ischemic/reperfusion injury and elevated intraocular pressure models, and improved anterograde axonal transport in eyes with ocular hypertension. Peptains also suppressed retinal glial activation. Therefore, peptains have potential as therapeutics against neurodegeneration in glaucoma.
CELL DEATH & DISEASE
(2022)
Article
Chemistry, Multidisciplinary
Giovanni Palomino-Vizcaino, Nils Schuth, Jose A. Dominguez-Calva, Oscar Rodriguez-Meza, Eduardo Martinez-Jurado, Eugene Serebryany, Jonathan A. King, Thomas Kroll, Miguel Costas, Liliana Quintanar
Summary: Cataracts are caused by the aggregation of high-molecular-weight proteins in the human eye lens, which scatter light and cause lens opacity. Metal ions play an important role in the development of cataract disease, as human lens gamma-crystallins are susceptible to metal-induced aggregation.
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
(2023)
Article
Biology
Eugene Serebryany, Sourav Chowdhury, Christopher N. Woods, David C. Thorn, Nicki E. Watson, Arthur A. McClelland, Rachel E. Klevit, Eugene Shakhnovich
Summary: Cataract, a protein aggregation disorder, is a common cause of vision loss worldwide. Researchers have discovered that myo-inositol, an abundant lens metabolite, can suppress the aggregation of lens crystallins, suggesting it as a potential strategy to prevent or delay age-onset cataracts.
Article
Biochemistry & Molecular Biology
Susanne Weininger, Malte Neudorf, Stefan Groeger, Eric Plato, Robert Broneske, Kay Saalwaechter, Ulrich Weininger, Jochen Balbach
Summary: Crystallin proteins in the human eye lenses play a role in maintaining transparency, light refraction, and UV light protection. Imbalance in the interaction between alpha-, beta-, and gamma-crystallin can lead to cataracts. The research looks into the effects of UV-B radiation on gamma D-crystallin, specifically observing changes in the N-terminal domain. It is found that some photoprotective properties remain in extracts from cataract patients. Additionally, a genetic mutation in the eye lens core of infants with cataracts increases sensitivity to UV-B irradiation.
MACROMOLECULAR BIOSCIENCE
(2023)
Review
Biochemistry & Molecular Biology
K. Sooraj, Swati Shukla, Ranjeet Kaur, Jeewan Singh Titiyal, Jasbir Kaur
Summary: Heat shock proteins (HSPs) are stress-induced proteins involved in the cell's defense system. Heat shock protein 27 (HSP27) plays a central role in the eye and has protective effects against ocular diseases, but it can also have destructive effects on retinal ganglionic cells.
MOLECULAR BIOLOGY REPORTS
(2022)
Article
Parasitology
Nancy A. Aguoru, Ruth S. Kirk, Anthony J. Walker
Summary: This study provides a detailed molecular bioinformatic analysis of heat shock proteins (HSPs) in the human parasitic blood fluke Schistosoma mansoni. The results reveal the classification, expression patterns, protein interactions, and phosphorylation sites of HSPs in different stages of the parasite's life cycle. The findings suggest that HSPs play important roles in parasite survival and development, and offer insights for future investigations and therapeutics development against schistosomiasis.
PARASITES & VECTORS
(2022)
Editorial Material
Cell Biology
Christopher M. Jakobson, Daniel F. Jarosz
Summary: Cells reorganize their contents into subcellular structures in response to stimuli, with new research showing that proteins interact with substrates to coordinate disassembly of cellular structures and directly sense the cellular energy state for adaptive reorganization.
NATURE CELL BIOLOGY
(2021)
Review
Plant Sciences
Norbert Andrasi, Aladar Pettko-Szandtner, Laszlo Szabados
Summary: Plant heat shock factors (HSFs) are encoded by large gene families and are involved in responses to high temperatures and various abiotic stresses. They are regulated primarily at the transcript level, with alternative splicing and post-translational modifications providing additional variability. Plant HSFs participate in a complex network of protein-protein interactions and play crucial roles in transcriptional control.
JOURNAL OF EXPERIMENTAL BOTANY
(2021)
Article
Biochemistry & Molecular Biology
Binyou Wang, Stuart P. Moon, Giuliano Cutolo, Afraah Javed, Benjamin S. Ahn, Andrew H. Ryu, Matthew R. Pratt
Summary: O-GlcNAc modification protects cells against stress-induced cell death by directly inhibiting the apoptotic pathway. The modified chaperone, HSP27, exhibits enhanced antiapoptotic function in an in vitro context. These findings provide molecular insights into how O-GlcNAc serves as a mediator of cellular stress and have important implications for human diseases like cancer and neurodegeneration.
ACS CHEMICAL BIOLOGY
(2023)
Article
Cell Biology
Lorenz Weidenauer, Manfredo Quadroni
Summary: Our study revealed that phosphorylation events at specific sites on Hsp90 beta regulate its interactions and secretion, with mutations affecting protein binding and sensitivity to cleavage. Furthermore, decreased phosphorylation at certain sites was associated with increased secretion efficiency, indicating a role for phosphorylation in regulating Hsp90 beta function and activity.