Karl Albert Muniz - Autophagy: The Ultimate Guide To Purify Your Body, Grow Muscle, Lose Weight, Promote Longetivity And Build Body Balance With Intermittent Fasting

The Ultimate Guide To Purify Your Body, Grow Muscle, Lose Weight, Promote Longetivity And Build Body Balance With Intermittent Fasting

By

Karl Albert Muniz

Copyright 2020

All rights reserved.

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The year 2013 marked the 50th anniversary of the coining by C de Duve of the term "autophagy" for the process of degradation of cytoplasmic constituents in lysosome / vacuole. This year, we have regretfully lost this great scientist, who has contributed a great deal to the field of autophagy during the early years of research. Soon after de Duve's observation of lysosomes, electron microscopy identified autophagy as a means of delivering intracellular components to the lysosome. For a long time after the discovery of autophagy, the studies have not shown any significant advances at the molecular level in our understanding of this fundamental path of degradation. The first breakthrough was made in the early 1990s when autophagy was detected in yeast hunger through microscopic examination. Next, a genetic effort to address the poorly understood problem of autophagy led to the discovery of many autophagic-defective mutants. Subsequent identification of autophagic genes in yeasts revealed unique sets of molecules involved in autophagic membrane dynamics. Subsequently, ATG homologs were found in various animals, suggesting that the basic process of autophagy is well preserved among eukaryotes. These findings have brought about revolutionary changes in research in this field. For example, we have seen remarkable progress over the last 10 years in our understanding of autophagy, not only in terms of autophagy molecular mechanisms but also in terms of its broad physiological roles and relevance to health and disease. Today, our understanding of autophagy is growing rapidly day by day. Here, the historic landmarks underpinning the explosion of autophagy research are described with a particular focus on the contribution of yeast as a model organism.

With every progress in scientific understanding, the broad fluid nature of life becomes more and more apparent. In addition to metabolites, cellular machines, proteins, and organelles themselves are maintained in the balance between continuous synthesis and degradation, which is an essential difference between life and man-made machinery. A constant supply of chemicals and energy from the external environment is necessary to maintain this state of balance. The most prolific source of such chemicals found in animals is the digestion of protein taken as food in the digestive tract, which is topologically held outside the body. In terms of intracellular proteins, the pioneering work of R. Schoenheimer has presented an important concept, that of "protein turnover" in the body. His prescient studies using isotopic protein labeling were unconventional at the time but stimulated much debate and subsequent work on intracellular protein metabolism. Nevertheless, for many years, people have still assumed that proteins are safe in vivo and that degradation does not play an important role in protein homeostasis. In the 1970s, research to measure individual protein lifetimes by cell degradation through an infusion of pure proteins into cells or by pulse-chase experiments have shown that each in vivo protein has a distinct half-life of just a few minutes and more than 100 days. We already recognize that the proteins that make up our bodies are replaced nearly exclusively every 1-2 months without any noticeable change in appearance. They still do not fully understand what actually defines the particular lifetimes of proteins, how and why this process happens, or indeed the biochemical importance behind such complex and distinct forms of protein degradation. However, it is clear that the turnover of proteins must play an essential role in order to adapt to continuous or abrupt changes in environmental conditions.

In nature, starvation, which is simply a lack of nutrient supply, is the most frequent and serious threat to the maintenance and maintenance of life. In order to cope with this adversity, the recycling of proteins is the primary line of defense by which cells can reserve amino acids for the synthesis of a minimal complement of proteins essential for survival. At the early stage of evolution, the cells must have acquired a certain mechanism of intracellular protein degradation that has been refined over the course of evolution; a striking example of this is that all organisms on Earth possess protease without exception. It is now recognized that, even under normal conditions, the bulk of protein synthesis amino acids in our body are produced from the breakdown of cell-specific proteins, suggesting that recycling is an inherent feature of life.

At the same time, intracellular protein degradation could be a hazardous process. Indiscriminate degradation, along with protein synthesis within the same compartment, could conceivably lead to a futile cycle resulting in energy waste. However, at least four key strategies have been developed to avoid this problem: first, the activity of the protease is tightly regulated, and the activation of the hydrolytic enzyme occurs only when necessary. Third, protease creates a large cage complex like a tank, reducing its decaying behavior. Second, goals are carefully adjusted prior to depletion, allowing for a degree of control over what is broken down. Asa result, hydrolytic enzymes are sequestered into the membrane pocket, mechanically segregating this process within the cell. The ubiquitin / proteasome system is responsible for both cases 2 and 3. Case 4 relies on the method of lysosomaldegradation. Segregation of hydrolases by a membrane inevitably gives rise to another problem, namely how to access substrates destined for degradation by hydrolytic enzymes. Degradation by the lysosomal system, which is largely dependent on autophagy, therefore necessarily involves certain membrane-mediated processes.