scholarly journals Drosophila p38 MAPK Interacts with BAG-3/starvin to Regulate Age-dependent Protein Homeostasis

2019 ◽  
Author(s):  
Sarah M. Ryan ◽  
Michael Almassey ◽  
Amelia M. Burch ◽  
Gia Ngo ◽  
Julia M. Martin ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
P38 Mapk ◽  
Protein Aggregates ◽  
Protein Homeostasis ◽  
Selective Autophagy ◽  
Age Related ◽  
Age Dependent ◽  
Dependent Protein ◽  
Locomotor Behaviors ◽  
The Relationship

SummaryAs organisms age, they often accumulate protein aggregates that are thought to be toxic, potentially leading to age-related diseases. This accumulation of protein aggregates is partially attributed to a failure to maintain protein homeostasis. A variety of genetic factors have been linked to longevity, but how these factors also contribute to protein homeostasis is not completely understood. In order to understand the relationship between aging and protein aggregation, we tested how a gene that regulates lifespan and age-dependent locomotor behaviors, p38 MAPK (p38Kb), influences protein homeostasis as an organism ages. We find that p38Kb regulates age-dependent protein aggregation through an interaction with the Chaperone-Assisted Selective Autophagy complex. Furthermore, we have identified Lamin as an age-dependent target of p38Kb and the Chaperone-Assisted Selective Autophagy complex.

Free thyroid hormone index, thyroid hormone/thyroxin-binding globulin ratio, triiodothyronine uptake, and thyroxin-binding globulin compared for diagnostic value regarding thyroid function.

1983 ◽  
Vol 29 (1) ◽  
pp. 74-79 ◽  
Author(s):  
T J Wilke
Keyword(s):  
Thyroid Hormone ◽  
Thyroid Function ◽  
Diagnostic Value ◽  
Clinical Findings ◽  
Thyroid Function Tests ◽  
Free Thyroid Hormone ◽  
Age Related ◽  
Age Dependent ◽  
Uptake Test ◽  
The Relationship

Abstract The thyroid hormone/thyroxin-binding globulin (TBG) ratio and the free thyroid hormone index (FTI) were compared in 372 subjects classified according to age, sex, and biochemical and clinical findings. Age-related variations in thyroid function tests were investigated, as was the relationship between triiodothyronine uptake and TBG. Men, but not women, showed significant age-dependent changes in concentrations of thyroid hormones. FTI was as good as the thyroid hormone/TBG ratio in hyperthyroidism and was a better index of thyroid status in pregnancy, TBG deficiency, and hypothyroidism. In addition, the triiodothyronine uptake correlated extremely well with TBG (r = -0.95, p less than 0.001) and was very efficient in detecting decreased and significantly increased concentrations of TBG. I conclude that FTI is a better discriminator of functional status of the thyroid over a wider range of TBG values than is the thyroid hormone/TBG ratio. Further, the triiodothyronine uptake test produced diagnostic information equivalent to that of TBG estimation and thus should not be replaced in routine use.

scholarly journals PIP3-binding proteins promote age-dependent protein aggregation and limit survival in C. elegans

Oncotarget ◽  
2016 ◽  
Vol 7 (31) ◽  
pp. 48870-48886 ◽  
Author(s):  
Srinivas Ayyadevara ◽  
Meenakshisundaram Balasubramaniam ◽  
Jay Johnson ◽  
Ramani Alla ◽  
Samuel G. Mackintosh ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Binding Proteins ◽  
C Elegans ◽  
Age Dependent ◽  
Dependent Protein

scholarly journals Mitochondrial Impairment in Sarcopenia

Biology ◽  
2021 ◽  
Vol 10 (1) ◽  
pp. 31
Author(s):  
Francesco Bellanti ◽  
Aurelio Lo Buglio ◽  
Gianluigi Vendemiale
Keyword(s):  
Skeletal Muscle ◽  
Muscle Quality ◽  
Protein Homeostasis ◽  
Related Condition ◽  
Selective Autophagy ◽  
Mitochondrial Homeostasis ◽  
Mitochondrial Alterations ◽  
Mitochondrial Impairment ◽  
Age Related ◽  
And Function

Sarcopenia is defined by the age-related loss of skeletal muscle quality, which relies on mitochondrial homeostasis. During aging, several mitochondrial features such as bioenergetics, dynamics, biogenesis, and selective autophagy (mitophagy) are altered and impinge on protein homeostasis, resulting in loss of muscle mass and function. Thus, mitochondrial dysfunction contributes significantly to the complex pathogenesis of sarcopenia, and mitochondria are indicated as potential targets to prevent and treat this age-related condition. After a concise presentation of the age-related modifications in skeletal muscle quality and mitochondrial homeostasis, the present review summarizes the most relevant findings related to mitochondrial alterations in sarcopenia.

scholarly journals Intrinsically aggregation-prone proteins form amyloid-like aggregates and contribute to tissue aging in Caenorhabditis elegans

eLife ◽  
2019 ◽  
Vol 8 ◽  
Author(s):  
Chaolie Huang ◽  
Sara Wagner-Valladolid ◽  
Amberley D Stephens ◽  
Raimund Jung ◽  
Chetan Poudel ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Aging Process ◽  
Amyloid Fibrils ◽  
Functional Decline ◽  
Molecular Feature ◽  
C Elegans ◽  
Age Dependent ◽  
Dependent Protein ◽  
Tissue Aging ◽  
Different Tissues

Reduced protein homeostasis leading to increased protein instability is a common molecular feature of aging, but it remains unclear whether this is a cause or consequence of the aging process. In neurodegenerative diseases and other amyloidoses, specific proteins self-assemble into amyloid fibrils and accumulate as pathological aggregates in different tissues. More recently, widespread protein aggregation has been described during normal aging. Until now, an extensive characterization of the nature of age-dependent protein aggregation has been lacking. Here, we show that age-dependent aggregates are rapidly formed by newly synthesized proteins and have an amyloid-like structure resembling that of protein aggregates observed in disease. We then demonstrate that age-dependent protein aggregation accelerates the functional decline of different tissues in C. elegans. Together, these findings imply that amyloid-like aggregates contribute to the aging process and therefore could be important targets for strategies designed to maintain physiological functions in the late stages of life.

scholarly journals Age-Dependent Protein Aggregation Initiates Amyloid-β Aggregation

2017 ◽  
Vol 9 ◽  
Author(s):  
Nicole Groh ◽  
Anika Bühler ◽  
Chaolie Huang ◽  
Ka Wan Li ◽  
Pim van Nierop ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Amyloid Β ◽  
Age Dependent ◽  
Dependent Protein

scholarly journals Age-dependent changes in mean and variance of gene expression across tissues in a twin cohort

2016 ◽  
Author(s):  
Ana Viñuela ◽  
Andrew A Brown ◽  
Alfonso Buil ◽  
Pei-Chien Tsai ◽  
Matthew N Davies ◽  
...  
Keyword(s):  
Gene Expression ◽  
Healthy Aging ◽  
Process Analysis ◽  
Strong Relationship ◽  
Methylation Array ◽  
Age Related ◽  
Age Dependent ◽  
Mean And Variance ◽  
The Relationship ◽  
Age Related Changes

AbstractGene expression changes with age have consequences for healthy aging and disease development. Here we investigate age-related changes in gene expression measured by RNA-seq in four tissues and the interplay between genotypes and age-related changes in expression. Using concurrently measured methylation array data from fat we also investigate the relationship between methylation, gene expression and age. We identified age-dependent changes in mean levels of gene expression in 5,631 genes and in splicing of 904 genes. Age related changes were widely shared across tissues, with up to 60% of age-related changes in expression and 47% on splicing in multi-exonic genes shared; amongst these we highlight effects on genes involved in diseases such as Alzheimer and cancer. We identified 137 genes with age-related changes in variance and 42 genes with age-dependent discordance between genetically identical individuals; implying the latter are driven by environmental effects. We also give four examples where genetic control of expression is affected by the aging process. Analysis of methylation observed a widespread and stronger effect of age on methylation than expression; however we did not find a strong relationship between age-related changes in both expression and methylation. In summary, we quantified aging affects in splicing, level and variance of gene expression, and show that these processes can be both environmentally and genetically influenced.

scholarly journals The understudied links of the retromer complex to age-related pathways

GeroScience ◽  
2021 ◽  
Author(s):  
Kenneth A. Wilson
Keyword(s):  
Disease Progression ◽  
Neurodegenerative Disorders ◽  
Memory Impairment ◽  
Functional Decline ◽  
Protein Aggregates ◽  
Structure And Function ◽  
Retromer Complex ◽  
Age Related ◽  
Age Dependent ◽  
And Function

AbstractNeuronal aging is associated with numerous diseases resulting in memory impairment and functional decline. A common hallmark of these disorders is the accumulation of intracellular and extracellular protein aggregates. The retromer complex plays a central role in sorting proteins by marking them for reuse rather than degradation. Retromer dysfunction has been shown to induce protein aggregates and neurodegeneration, suggesting that it may be important for age-related neuronal decline and disease progression. Despite this, little is known about how aging influences retromer stability and the proteins with which it interacts. Detailed insights into age-dependent changes in retromer structure and function could provide valuable information towards treating and preventing many age-related neurodegenerative disorders. Here, we visit age-related pathways which interact with retromer function that ought to be further explored to determine its role in age-related neurodegeneration.

scholarly journals Intrinsically aggregation-prone proteins form amyloid-like aggregates and contribute to tissue aging in C. elegans

2018 ◽  
Author(s):  
C. Huang ◽  
S. Wagner-Valladolid ◽  
A.D. Stephens ◽  
R. Jung ◽  
C. Poudel ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Amyloid Fibrils ◽  
Functional Decline ◽  
C Elegans ◽  
Amyloid Aggregates ◽  
Age Dependent ◽  
Dependent Protein ◽  
Specific Proteins ◽  
Protein Instability ◽  
Tissue Aging

AbstractReduced protein homeostasis and increased protein instability is a common feature of aging. Yet it remains unclear whether protein instability is a cause of aging. In neurodegenerative diseases and amyloidoses, specific proteins self-assemble into amyloid fibrils and accumulate as pathological solid aggregates in a variety of tissues. More recently, widespread protein aggregation has been described during normal aging, in the absence of disease processes. Until now, an extensive characterization of the nature of age-dependent protein aggregation and its consequences for aging has been lacking. Here, we show that age-dependent aggregates are rapidly formed by newly synthesized proteins and contain amyloid-like structures similar to disease-associated protein aggregates. Moreover, we demonstrate that age-dependent protein aggregation accelerates the functional decline of different tissues in C. elegans. Together, these finding reveal that the formation of amyloid aggregates is a generic problem of aging and likely to be an important target for strategies designed to maintain physiological functions in later stages of life.

scholarly journals Protein aggregation in bacteria

2019 ◽  
Vol 44 (1) ◽  
pp. 54-72 ◽  
Author(s):  
Frederic D Schramm ◽  
Kristen Schroeder ◽  
Kristina Jonas
Keyword(s):  
Protein Aggregation ◽  
Stress Resistance ◽  
Protein Quality ◽  
Protein Aggregates ◽  
Protein Homeostasis ◽  
Bacterial Protein ◽  
Bacterial Populations ◽  
Regulate Gene Expression ◽  
Specific Proteins ◽  
Cellular Stresses

ABSTRACT Protein aggregation occurs as a consequence of perturbations in protein homeostasis that can be triggered by environmental and cellular stresses. The accumulation of protein aggregates has been associated with aging and other pathologies in eukaryotes, and in bacteria with changes in growth rate, stress resistance and virulence. Numerous past studies, mostly performed in Escherichia coli, have led to a detailed understanding of the functions of the bacterial protein quality control machinery in preventing and reversing protein aggregation. However, more recent research points toward unexpected diversity in how phylogenetically different bacteria utilize components of this machinery to cope with protein aggregation. Furthermore, how persistent protein aggregates localize and are passed on to progeny during cell division and how their presence impacts reproduction and the fitness of bacterial populations remains a controversial field of research. Finally, although protein aggregation is generally seen as a symptom of stress, recent work suggests that aggregation of specific proteins under certain conditions can regulate gene expression and cellular resource allocation. This review discusses recent advances in understanding the consequences of protein aggregation and how this process is dealt with in bacteria, with focus on highlighting the differences and similarities observed between phylogenetically different groups of bacteria.

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