Energy-dependent thymic involution vs evolution (3)
MicroRNA-mediated therapy prevents thymic involution. Energy-dependent light-activated microRNA biogenesis will soon be linked from the ability of light to override carbon as a major regulator of ASN1 and GLN2 in etiolated seedlings to healthy longevity at every level of biological organization…
We simultaneously quantified host-cell mRNA and vRNA abundance at the single-cell level, thereby identifying proviral and antiviral factors that correlated with intracellular viral abundance (21).
The ability to detect viral load at the single-cell level can be linked to detection and effective treatment of virus-caused cancers and all other virus-caused pathology. Naturally occurring RNA interference (RNAi) will gradually replace nearly all drug treatments because the control of light-activated microRNA biogenesis has virtually no negative side effects.
Moving forward, see: 2018: a mildly muddled review of the year in neuroscience
This clarified how the virus-driven degradation of messenger RNA is linked to all pathology, which typically is prevented by the light-activated creation of microRNAs in plants and the role that microRNAs play in the stability of all organized genomes.
…we have likely documented…the initial steps of a possible path of virus-mediated horizontal transfer of chromosomal DNA between plant species.
See also for the link from virues to all pathology: Virus-mediated archaeal hecatomb in the deep seafloor
For the link from biophysically constrained viral latency to energy-dependent healthy longevity, see: Eukaryotic plankton diversity in the sunlit ocean
The energy for healthy longevity comes from the sun and is delivered via light-activated microRNA biogenesis in plants. The energy-dependent light-activated creation of microRNAs is the antithesis of the virus-driven energy theft that links the degradation of messenger RNA to mutations and all pathology.
For example, C. elegans is a model organism for aging.
See: Intrinsically aggregation-prone proteins form amyloid-like aggregates and contribute to tissue aging in C. elegans
Reduced 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.
Proteins do not self-assemble and quantized energy-dependent autophagy prevents “intrinsically” aggregation-prone proteins from causing all neurodegenerative diseases.
See also: Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers
Oligomeric species populated during the aggregation process of α-synuclein have been linked to neuronal impairment in Parkinson’s disease and related neurodegenerative disorders. By using solution and solid-state nuclear magnetic resonance techniques in conjunction with other structural methods, we identified the fundamental characteristics that enable toxic α-synuclein oligomers to perturb biological membranes and disrupt cellular function; these include a highly lipophilic element that promotes strong membrane interactions and a structured region that inserts into lipid bilayers and disrupts their integrity. In support of these conclusions, mutations that target the region that promotes strong membrane interactions by α-synuclein oligomers suppressed their toxicity in neuroblastoma cells and primary cortical neurons.
Toxic oligomers form at an early stage in the series of events that lead to Parkinson’s Disease, which are believed to begin when alpha synuclein proteins malfunction and begin to stick together. Their emergence is lethal to neuronal function in this context. Once the oligomers have formed, they disperse, and allow the initial toxicity to spread to other cells.
The claim that toxic oligomers form when alpha synuclein proteins malfunction and begin to stick together before their emergence exemplifies human idiocy. The claim that something forms before the malfunction emerges has no explanatory power.
See for comparison an example from another model organism: Akt kinases are required for efficient feeding by macropinocytosis in Dictyostelium
Macropinocytosis is an actin-driven process of large-scale, non-specific fluid uptake used for feeding by some cancer cells and the macropinocytosis model organism Dictyostelium discoideum. In Dictyostelium, macropinocytic cups are organised by ‘macropinocytic patches’ in the plasma membrane. These contain activated Ras, Rac and PI(3,4,5)P3 and direct actin polymerisation to their periphery. Here, we show that a classical (PkbA) and a variant (PkbR1) Akt protein kinase acting downstream of PI(3,4,5)P3 are together are near-essential for fluid uptake. This pathway enables the formation of larger macropinocytic patches and macropinosomes, thereby dramatically increasing fluid uptake. Akt targets identified by phosphoproteomics were highly enriched in small G-protein regulators, including the RhoGAP GacG. GacG knockout mutants make few macropinosomes but instead redeploy their cytoskeleton from macropinocytosis to motility, moving rapidly but taking up little fluid. The function of Akt in cell feeding through control of macropinosome size has implications for cancer cell biology.
See also: Mechanisms of mitophagy in cellular homeostasis, physiology and pathology
Mitophagy is an evolutionary conserved cellular process to remove dysfunctional or superfluous mitochondria, thus fine-tuning mitochondrial number and preserving energy metabolism.
Mitophagy is energy-dependent biophysically constrained autophagy, which prevents the degradation of messenger RNA. Serious scientists have linked the degradation of messenger RNA from mutations to all pathology.