To learn the essence of life you have to leave the grasp of Earth’s gravity. The gravity vector field that surrounds the fabric of time space exists at the molecular scale of interactions. The stress of life within cells is felt within the effects of gravity. Place a life form in anti-gravity and life will change. But you also glimpse the essential blueprint of design within gravity simultaneously, the blueprint of tensegrity. That is the lens to see the essence of the shape of life.
“In the life-science field of space-science research, one of the important themes is a building theory of life systems produced by the earth itself and their evolution/adaptation mechanisms that have been at work for over 3.8 billion years. The life system’s strategy in pursuit of maintenance against stress can suggest hints about the existence of human beings, who have developed scientific and technological methods to cope with stress. Among the items I will introduce here are: structural adaptation systems and cytoskeletal proteins, which have been under performance analysis as key molecules in the gravitational adaptation of living things with form – especially mammals including human beings – that seem to be constructed as a system principle; and molecular chaperones (proteins that take care of proteins) essential for temporal adaptation of the cytoskeletal protein. These teach us that adaptation is acquired by bringing out skillfully the body’s stress response system. The core stress factors causing adaptation are gravitational and mechanical stimuli.” YORIOKO ATOMI / University of Tokyo, Institute of Space and Astronautical Science, JAXA Japan Aerospace Exploration Agency
Rapid heat hardening can be elicited by a brief exposure of cells to sub-lethal high temperature, which in turn provides protection from subsequent and more severe temperature. In 1962, Italian geneticist Ferruccio Ritossa reported that heat and the metabolic uncoupler 2,4 dinitrophenol (dinitrophenol uncouples oxidative phosphorylation, causes release of calcium from mitochondrial stores and prevents calcium re-uptake. This leads to free intracellular calcium and causes muscle contraction and hyperthermia) induced a characteristic pattern of puffing in the chromosomes of , fruit flies, Drosophila. This discovery eventually led to the identification of the heat-shock proteins (HSP) or stress proteins whose expression these puffs represented. Increased synthesis of selected proteins in Drosophila cells following stresses such as heat shock was first reported in 1974. Shape changes are at the core of bacterial infection causing a fever response.
Beginning in the mid-1960s, investigators recognized that many HSPs function as molecular chaperones and thus play a critical role in protein folding, intracellular trafficking of proteins, and coping with proteins denatured by heat and other stresses.
Notice the many references to shape like protein folding, the distortion of chromosomes using the description of puffing.
Production of high levels of heat shock proteins can also be triggered by exposure to different kinds of environmental stress conditions, such as infection, inflammation, exercise, exposure of the cell to toxins (ethanol, arsenic, trace metals, and ultra violet light, among many other stresses) starvation, oxygen starvation, (hypoxia)in plants nitrogen deficiency or water deprivation. As a consequence, the heat shock proteins are also referred to as stress proteins and their upregulation is sometimes described more generally as part of the stress response.
The mechanism by which heat-shock (or other environmental stressors) activates the heat shock factor has been determined in bacteria. During heat stress outer membrane proteins (OMPs) do not fold and cannot insert correctly into the outer membrane. They accumulate in the periplasmic space. These OMP’s are detected by DegS, an inner membrane protease, that passes the signal through the membrane to the sigmaE transcription factor. However, some studies suggest that an increase in damaged or abnormal proteins brings HSPs into action. (thank you Scholarpedia and Wiki for background)
Nature has built its own non coding non protein forming RNA thermometers that basically unzip their shape when exposed to excessive heat found in rod-shaped, gram negative salmonella that cause diseases such as typhoid fever or food poisoning. One of the reasons we cook food for at least 10 minutes and 75 C is to kill off any residual salmonella in the middle food portions.
They are named ‘FourU’ due to the four highly conserved uridine nucleotides found directly opposite the Shine-Delgarno sequence on hairpin II . RNA thermometers such as FourU control regulation of temperature via heat shock in many prokaryotes. FourU thermometers are relatively small RNA molecules, only 57 nucleotides in length, and have a simple two-hairpin shaped structure. The secondary structure is a descriptive feature used by biologists to describe the 3 dimensional character of a local segment of the nucleic acid or protein, RNA in this particular case. It’s like describing a portion of a small feature of an aircraft wing as a general functional aeronautical device on the wing. Notice how these biologists employ this slang language but they don’t make it as part of the wider assembly of the language features within the backbone of a tensegrity matrix which it is. But make no mistake they are talking shape features despite the fancy FourU Hairpin ll slang they have invented. Notice I started off talking about gravity forcing tensegrity then into the mix are RNA thermometers that happen during disease stress, by the way passing a message which is information processing by shape. This is the tensegrity fabric that I mentioned earlier of time space gravity. Shape sensing on an RNA thermometer prevents the backbone to unzip to form a protein because it can’t start to unzip. But also notice the ultra tiny dimensions of all of these things being governed by the shape process.
Life as we know it is all about shape processes within the backbone of tensegrity tension/compression networks. Scientists are not consistent in their language to describe the shapes as a general event. That will take some time.
Stress plays out in our body or in our mind or both as imaginary or real or both.
” Just as foundations and pillars are necessary to build a house on the ground, formed cells have a dynamic foundation, an extra-cellular matrix consisting of proteins, and a cytoskeleton, the raw materials that form them. The strength (tension) exerted by the cytoskeleton differs with the cells. When the cytoskeleton is destroyed or supplied with material that prevents its dynamics, the cell dies. Cell death also occurs when cells are peeled off their foundations, the extra-cellular matrix. Bioinformation is written in the genome, but it does not build forms. To read a genome, the field requires mechanical strength. To endure that strength, living things build a dynamically balanced structure with proteins or sugar outside and inside the cell.”
Tension/compression as floating tensegrity fills life with form with shape not only as form but as sensing within the shape. Loose the shape of the cell, the cell will die. Loose the pull of gravity eventually the cell will die. Gravity promotes life within stress. Shape responds to the stress.
The cytoskeleton is a fiber structure to generate expansive or contractile elasticity and, at the same time, to resist that elasticity. Actin filament in cultured cells produces stress fiber that has a contractile structure similar to the sarcomere structure of muscles. Donald Ingber of Harvard University named this dynamic structure the “tensegrity model” since it controls by tension as in a tent or Fukuoka Dome, and applied it to cells.
“All cells have three kinds of protein fiber, or cytoskeleton, in common: actin, tubulin and medium-diameter filament. Contrary to the names “tensegrity” or “skeleton,” these are dynamically reproduced. In particular, the hollow nano-fibers and microtubes produced by tubulin reveal so-called dynamic instability. As the name indicates, the nano-fibers and microtubes combine and co-polymerize GTP, extending the microtubes. Once GTP is decomposed to GDP, however, it becomes unstable and starts depolymerizing and contracting. This results in an increase of non-polymerizing free forms, causing the extension to occur again. The maintenance of these chemically balanced relations forms the background to the dynamic instability. Further, once combined with increased free forms, tubulin’s mRNA is destabilized and destroyed. It becomes unable to produce tubulin. This suggests that the cells’ dynamic state is adjusted by proteins working at site in co-polymerizing/de-polymerizing states, rather than by self-control at genetic level.”
Guanosine-5′-triphosphate (GTP) can act as a substrate for the synthesis of RNA during the transcription process or DNA during DNA replication. All of this is about shape transformation within the basics of life, RNA and DNA. GTP also has the role of a source of energy or an activator of substrates in metabolic reactions, like that of ATP, but more specific. It is used as a source of energy for protein synthesis and gluconeogenesis. GTP is essential to signal transduction, in particular withG-proteins, in second-messenger mechanisms where it is converted to guanosine dipohosphate (GDP) through the action of GTPases. With genetic translation during the elongation stage of translation, GTP is used as an energy source for the binding of a new amino-bound tRNA to the A site of the ribosome. GTP is also used as an energy source for the translocation of the ribosome towards the 3′ end of the mRNA. During microtubule polymerization, each heterodimer formed by an alpha and a beta tubulin molecule carries two GTP molecules, and the GTP is hydrolyzed to GDP when the tubulin dimers are added to the plus end of the growing microtubule. Such GTP hydrolysis is not mandatory for microtubule formation, but it appears that only GDP-bound tubulin molecules are able to depolymerize. Thus, a GTP-bound tubulin serves as a cap at the tip of microtubule to protect from depolymerization; and, once the GTP is hydrolyzed, the microtubule begins to depolymerize and shrink rapidly. When things shrink information transfer also fails. Disconnect the information by shrinking the shape connections. Loose the tension lose the intelligence. Lose the capacity to perform to adapt.
Information in the form of transient signals happens when proteins shape change, altering local tension which adjusts throughout the entire assembly. Everything is within reach within tension/compression tensegrity since simultaneous local events are monitoring global events. The whole structure is on shape.
” While maintaining structure to generate functions, life systems function by circulating two aspects with different directionality in various times. The come-and-go between both poles becomes the dynamic-maintenance factor, or stress factor, to the cells and facilitates adaptation. This dynamic is the synthesis and decomposition of the protein itself: dynamic formation retention by copolymerization and depolymerization of cytoskeleton protein; consumption and generation of energy; form retention and tension exertion; contraction and relaxation (extension); exercise and structure maintenance; and stabilization and destabilization. Thus, cells regularly use functions of the regeneration system by the central dogma within one-generation lifespan. And cells entrust the maintenance of normal protein function in the regeneration system itself to the molecular chaperone (stress protein), which takes care of the protein’s lifespan. If protein denatures from this circulating system, it shifts to various clinical states (e.g., Alzheimer’s and prion disease). It is proved that 30% of the cell’s neo-genesis protein is abnormal, as it decomposes soon after it is synthesized. This evidence shows that the cell system must be continually, dynamically in motion. There are many stress proteins. In heart-muscle and slow-muscle cells, which are models for long life-adaptation strategy, there is a high expression rate of low-molecular-weight protein (sHSPs), among others, operating in the key part of the function/structure linkage system of energy dependency. “
HSP heat shock proteins are a group of proteins induced by heat shock, the most prominent members of this group are a class of functionally related proteins involved in the folding and unfolding of other proteins. Their expression is increased when cells are exposed to elevated temperatures or other stress. This increase in expression is transcriptionally regulated. The dramatic upregulation of the heat shock proteins is a key part of the heat shock response and is induced primarily by heat shock factor (HSF). HSPs are found in virtually all living organisms, from bacteria to humans.
Shape sensing scales seamlessly between all levels of life from bacteria to humans seen with heat shock proteins interacting within tensegrity design structures.
“One sHSPs, αB-crystallin, decreases specifically in a rat hind-leg suspension model, a zero-gravity muscle-atrophy model. In a space environment, if production of the stress protein (the cell’s adaptive-acquisition molecule obtained under gravity) becomes low, the continued stimulation of the adaptation system in living things, including humankind, will become a major problem. A mouse knocked out by αB-crystallin does not die immediately, but measurement shows extremely low levels in its motor activity. When expression of thermal-shock factor (the stress protein’s transcriptional control element) is forced on C elegans, its life almost doubles. Thus, it has been reported that the stress protein, as with IGF-1, is a longevity element. In this model, the stress protein that works to constrain the aggregation of denaturation proteins is another sHSPs, like αB-crystallin. “
When HSP is forced onto an earth worms metabolism, this doubles the life span. By longevity element, think of influencing the aging effect.
“On the ground, gravity is a constitutive factor. I considered a cell’s continuous dynamic response system by using the molecular chaperone. I examined: the molecular mechanism of αB-crystallin on cytoskeleton protein that generates the tension exertion and contraction mechanism inside the cell; the gravity load of the chaperone HSP47 on the main protein collagen in the extra-cellular matrix, that is essential for fulcrum formation outside the cell; and response to release (rat model). HSP47 is a sole molecular chaperone, the expression of which is controlled by HSF inside endoplasmic reticulum. It was proved that HSP47 is essential for three-spiral polymerization of collagen protein, and for adding and processing secreted hydroxyl to the exterior of the cell.”
A peek inside the Lego man by Jason Freeny. Is tensegrity hidden inside these shape contours?
“With regard to the amount of HSP47 expressed, observations indicate that protein and mRNA respond to over-gravity by hind-leg suspension and centrifugal force much earlier than their ground substance, mRNA of collagen. Collagen is believed to be synthesized with fibroblast. Muscle cells have a basement membrane structure, however, and it was proved that it is synthesized within muscle cells as a result of studies using cell-culture systems.”
Change the force of gravity by spinning causes the mRNA changes to happen sooner inside the muscle cell. A faster sequence when gravity is boosted hmmm does that mean that stress can be changed with increasing the force field of gravity to slow down aging perhaps adjust healing? Just a thought.
“In a myoblast with frequent αB-crystallin expression, tubulin/microtube (part of the cytoskeleton) and crystalline localization are well agreed (insert fig ref.). The tubulin and actin extracted from slow muscle with a high rate of αB-crystallin expression combine to form the primary ground substance. αB-crystallin functions as an effective molecular chaperone to constrain coagulation sedimentation by the thermal denaturation of tubulin. As a result of the investigation, the functional part was found on the C-terminal side where the “α-crystallin domain” common to sHSPs is present. It combines with MAPs that stabilize the microtube’s polymer, thus contributing to the stabilization of the microtube. Time-lapse images show that a cell with increasedαB-crystallin expression is dynamic but adheres without moving. After injecting anti-αB-crystallin antibody to the cell, however, it loses stability and an erratic motion arises.”
“It is suggested that systems that cannot be realized simultaneously by non-life systems (such as form building, tension exertion, contraction/extension movement and combination with energy supply system) are dynamically constructed in cells by molecular complex synchronization. In addition, the following are suggested: the maintenance of cytoskeleton dynamics is essential for the tension-exertion system with high perpetual-motion-like adaptability; the molecular chaperone αB-crystallin is an indispensable adaptive molecule in the system; environmental stimuli are important to provoke stress-protein expression, which tends increasingly toward activity dependence.”
“When tension cannot be exerted, the cell cannot maintain its system, resulting in death. The genome has been decoded and overall analysis is underway. Just as the cytoskeleton gene is used as a control for comparison, the cytoskeleton is probably designed to remain mostly constant at gene level. We are losing the life-system point of view, which is very inevitable and constitutive, including life-science research related to space and gravity response.”
When floating tension/compression is taken away as in microgravity aging effects take over as a result. Astronaut Chris Hadfield has stated , “That for every month aboard the International Space Station is equivalent for the body to age one year. ”
What professor Atomi has elegantly expressed although his english skills are admirable but way better than my Japanese skills can be summarized in his observations. Gravity is a necessary stress to the adaptation to life at the level of micro signalling within cells. Tension/compression based shape sensing is at the essence of life within the gravity field of Earth. We owe our ability to reproduce to sense to see to touch to smell to think move and live to the stress of gravity. Nature has also evolved a method to calibrate into the tensegrityness of shape sensing. That means a tensegrity based reflex orients to the direction of the gravity field. This tensegrity reflex is called a yawn. To yawn is to display tensegrity across your face to harmonize into the space fabric of time into gravity within your brain/body tensegrity cellular networks. We yawn because we are shape based sensing creatures. All mammals on Earth yawn. When you don’t yawn there is a metabolic derangement like autism or aging or reduced yawning with no gravity. Tensegrity within the human body changes as gravity is absent while in space. Astronauts reduce their yawning frequency and their bone density changes with time as the tensegrity system changes in antigravity and the bodies time clock speeds up.