scholarly journals Long-Term Recreational Football Training and Health in Aging

2020 ◽  
Vol 17 (6) ◽  
pp. 2087
Author(s):  
Esther Imperlini ◽  
Annamaria Mancini ◽  
Stefania Orrù ◽  
Daniela Vitucci ◽  
Valeria Di Onofrio ◽  
...  
Keyword(s):  
Quality Control ◽  
Dna Repair ◽  
Successful Aging ◽  
Protein Quality ◽  
Metabolic Diseases ◽  
Control Mechanisms ◽  
Older Subjects ◽  
Football Training ◽  
Over Time

This narrative review aims to critically analyze the effects of exercise on health in aging. Here we discuss the main clinical and biomolecular modifications induced by long-term recreational football training in older subjects. In particular, the effects induced by long-term recreational football training on cardiovascular, metabolic and musculo-skeletal fitness, together with the modifications in the muscle expression of hallmarks related to oxidative metabolism, DNA repair and senescence suppression pathways and protein quality control mechanisms will be provided. All these topics will be debated also in terms of preventing non-communicable metabolic diseases, in order to achieve successful aging over time.

Cytosolic protein quality control machinery: Interactions of Hsp70 with a network of co-chaperones and substrates

2021 ◽  
pp. 153537022199981
Author(s):  
Chamithi Karunanayake ◽  
Richard C Page
Keyword(s):  
Quality Control ◽  
Protein Quality ◽  
Protein Quality Control ◽  
Structural Features ◽  
Cellular Protein ◽  
Mechanisms Of Action ◽  
Control Mechanisms ◽  
Nucleotide Exchange ◽  
Domain Organization ◽  
Nucleotide Exchange Factors

The chaperone heat shock protein 70 (Hsp70) and its network of co-chaperones serve as a central hub of cellular protein quality control mechanisms. Domain organization in Hsp70 dictates ATPase activity, ATP dependent allosteric regulation, client/substrate binding and release, and interactions with co-chaperones. The protein quality control activities of Hsp70 are classified as foldase, holdase, and disaggregase activities. Co-chaperones directly assisting protein refolding included J domain proteins and nucleotide exchange factors. However, co-chaperones can also be grouped and explored based on which domain of Hsp70 they interact. Here we discuss how the network of cytosolic co-chaperones for Hsp70 contributes to the functions of Hsp70 while closely looking at their structural features. Comparison of domain organization and the structures of co-chaperones enables greater understanding of the interactions, mechanisms of action, and roles played in protein quality control.

scholarly journals Targeting Protein Quality Control Mechanisms by Natural Products to Promote Healthy Ageing

Molecules ◽  
2018 ◽  
Vol 23 (5) ◽  
pp. 1219 ◽  
Author(s):  
Sophia Wedel ◽  
Maria Manola ◽  
Maria Cavinato ◽  
Ioannis Trougakos ◽  
Pidder Jansen-Dürr
Keyword(s):  
Quality Control ◽  
Natural Products ◽  
Protein Quality ◽  
Protein Quality Control ◽  
Healthy Ageing ◽  
Control Mechanisms

scholarly journals Phosphorylation Modifications Regulating Cardiac Protein Quality Control Mechanisms

2020 ◽  
Vol 11 ◽  
Author(s):  
Sumita Mishra ◽  
Brittany L. Dunkerly-Eyring ◽  
Gizem Keceli ◽  
Mark J. Ranek
Keyword(s):  
Quality Control ◽  
Protein Quality ◽  
Protein Quality Control ◽  
Control Mechanisms

Protein quality control at the mitochondrion

2016 ◽  
Vol 60 (2) ◽  
pp. 213-225 ◽  
Author(s):  
Wolfgang Voos ◽  
Witold Jaworek ◽  
Anne Wilkening ◽  
Michael Bruderek
Keyword(s):  
Quality Control ◽  
Structural Integrity ◽  
Protein Quality ◽  
Mitochondrial Protein ◽  
Protein Quality Control ◽  
Eukaryotic Cell ◽  
Control Mechanisms ◽  
Biochemical Processes ◽  
Unfolded Protein ◽  
Protein Response

Mitochondria are essential constituents of a eukaryotic cell by supplying ATP and contributing to many mayor metabolic processes. As endosymbiotic organelles, they represent a cellular subcompartment exhibiting many autonomous functions, most importantly containing a complete endogenous machinery responsible for protein expression, folding and degradation. This article summarizes the biochemical processes and the enzymatic components that are responsible for maintaining mitochondrial protein homoeostasis. As mitochondria lack a large part of the required genetic information, most proteins are synthesized in the cytosol and imported into the organelle. After reaching their destination, polypeptides must fold and assemble into active proteins. Under pathological conditions, mitochondrial proteins become misfolded or damaged and need to be repaired with the help of molecular chaperones or eventually removed by specific proteases. Failure of these protein quality control mechanisms results in loss of mitochondrial function and structural integrity. Recently, novel mechanisms have been identified that support mitochondrial quality on the organellar level. A mitochondrial unfolded protein response allows the adaptation of chaperone and protease activities. Terminally damaged mitochondria may be removed by a variation of autophagy, termed mitophagy. An understanding of the role of protein quality control in mitochondria is highly relevant for many human pathologies, in particular neurodegenerative diseases.

scholarly journals Protein Quality Control and Lipid Droplet Metabolism

2020 ◽  
Vol 36 (1) ◽  
pp. 115-139 ◽  
Author(s):  
Melissa A. Roberts ◽  
James A. Olzmann
Keyword(s):  
Quality Control ◽  
Protein Quality ◽  
Metabolic Diseases ◽  
Neutral Lipids ◽  
Protein Quality Control ◽  
Cellular Protein ◽  
Nutrient Sensing ◽  
Nonalcoholic Fatty Liver ◽  
Triacylglycerol Synthesis ◽  
Associated Proteins

Lipid droplets (LDs) are endoplasmic reticulum–derived organelles that consist of a core of neutral lipids encircled by a phospholipid monolayer decorated with proteins. As hubs of cellular lipid and energy metabolism, LDs are inherently involved in the etiology of prevalent metabolic diseases such as obesity and nonalcoholic fatty liver disease. The functions of LDs are regulated by a unique set of associated proteins, the LD proteome, which includes integral membrane and peripheral proteins. These proteins control key activities of LDs such as triacylglycerol synthesis and breakdown, nutrient sensing and signal integration, and interactions with other organelles. Here we review the mechanisms that regulate the composition of the LD proteome, such as pathways that mediate selective and bulk LD protein degradation and potential connections between LDs and cellular protein quality control.

scholarly journals The nucleolus functions as a phase-separated protein quality control compartment

Science ◽  
2019 ◽  
Vol 365 (6451) ◽  
pp. 342-347 ◽  
Author(s):  
F. Frottin ◽  
F. Schueder ◽  
S. Tiwary ◽  
R. Gupta ◽  
R. Körner ◽  
...  
Keyword(s):  
Quality Control ◽  
Protein Quality ◽  
Protein Quality Control ◽  
Misfolded Proteins ◽  
Control Mechanisms ◽  
Culture Cells ◽  
Irreversible Aggregation ◽  
Nuclear Proteome ◽  
Prolonged Stress

The nuclear proteome is rich in stress-sensitive proteins, which suggests that effective protein quality control mechanisms are in place to ensure conformational maintenance. We investigated the role of the nucleolus in this process. In mammalian tissue culture cells under stress conditions, misfolded proteins entered the granular component (GC) phase of the nucleolus. Transient associations with nucleolar proteins such as NPM1 conferred low mobility to misfolded proteins within the liquid-like GC phase, avoiding irreversible aggregation. Refolding and extraction of proteins from the nucleolus during recovery from stress was Hsp70-dependent. The capacity of the nucleolus to store misfolded proteins was limited, and prolonged stress led to a transition of the nucleolar matrix from liquid-like to solid, with loss of reversibility and dysfunction in quality control. Thus, we suggest that the nucleolus has chaperone-like properties and can promote nuclear protein maintenance under stress.

Mitochondria-Associated Proteostasis

2020 ◽  
Vol 49 (1) ◽  
pp. 41-67 ◽  
Author(s):  
Linhao Ruan ◽  
Yuhao Wang ◽  
Xi Zhang ◽  
Alexis Tomaszewski ◽  
Joshua T. McNamara ◽  
...  
Keyword(s):  
Quality Control ◽  
Cardiovascular Diseases ◽  
Protein Quality ◽  
Therapeutic Potential ◽  
Nuclear Genome ◽  
Mitochondrial Proteins ◽  
Protein Homeostasis ◽  
Control Mechanisms ◽  
Mitochondrial Proteome ◽  
Functional States

Mitochondria are essential organelles in eukaryotes. Most mitochondrial proteins are encoded by the nuclear genome and translated in the cytosol. Nuclear-encoded mitochondrial proteins need to be imported, processed, folded, and assembled into their functional states. To maintain protein homeostasis (proteostasis), mitochondria are equipped with a distinct set of quality control machineries. Deficiencies in such systems lead to mitochondrial dysfunction, which is a hallmark of aging and many human diseases, such as neurodegenerative diseases, cardiovascular diseases, and cancer. In this review, we discuss the unique challenges and solutions of proteostasis in mitochondria. The import machinery coordinates with mitochondrial proteases and chaperones to maintain the mitochondrial proteome. Moreover, mitochondrial proteostasis depends on cytosolic protein quality control mechanisms during crises. In turn, mitochondria facilitate cytosolic proteostasis. Increasing evidence suggests that enhancing mitochondrial proteostasis may hold therapeutic potential to protect against protein aggregation–associated cellular defects.

Feasibility of centralized measurements of glycated hemoglobin in the Diabetes Control and Complications Trial: a multicenter study. The DCCT Research Group.

1987 ◽  
Vol 33 (12) ◽  
pp. 2267-2271 ◽  
Keyword(s):  
Quality Control ◽  
High Performance ◽  
Glycated Hemoglobin ◽  
Multicenter Trial ◽  
Diabetes Control ◽  
Mean Values ◽  
Hb A1c ◽  
Control Procedures ◽  
Over Time

Abstract A method for measuring glycated hemoglobin (Hb A1c) and an accompanying method of specimen transport to a central laboratory were developed for the multicenter Diabetes Control and Complications Trial (DCCT). In the DCCT, results for Hb A1c are used to assess chronic glycemic control for data collection and patient management. During the feasibility phase of the trial, central (CHL) and backup laboratories using automated, "high-performance" ion-exchange liquid-chromatographic methods were established. Whole-blood samples were stored (4 degrees C) at each of the 21 clinical centers for up to 72 h before air-express shipment to the CHL. Quality-control procedures included daily analyses of three calibration specimens. A pooled hemolysate was assayed frequently over time as a long-term quality control (LTQC). After 18 months, within- and between-run CVs were less than 6%. Mean values for split duplicate samples assayed in a masked fashion at the CHL were nearly identical. LTQC results indicated no significant assay drift over time. More than 6000 samples were assayed (mean interval between obtaining the blood sample and completing the assay: less than six days). Hb A1c evidently can be precisely and reliably measured in the context of a long-term, multicenter trial such as the DCCT.

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