Target type: biologicalprocess
Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating a decline in oxygen levels to trace amounts, <0.1%. [GOC:kmv]
Anoxia, or the complete absence of oxygen, presents a severe challenge to organisms. The response to anoxia is a complex and multifaceted process involving a cascade of physiological and molecular changes aimed at minimizing damage and maintaining vital functions.
**1. Cellular Energy Crisis:**
* The immediate consequence of anoxia is the depletion of cellular ATP, the primary energy currency.
* Cellular respiration, which relies on oxygen as the final electron acceptor in the electron transport chain, ceases.
* This energy deficit disrupts various cellular processes, including active transport, protein synthesis, and muscle contraction.
**2. Anaerobic Metabolism:**
* To compensate for the lack of oxygen, cells switch to anaerobic metabolism.
* This process involves the breakdown of glucose through glycolysis, generating a small amount of ATP without the involvement of oxygen.
* Lactic acid is a byproduct of anaerobic metabolism, leading to a drop in pH and potentially causing cellular damage.
**3. Gene Expression Changes:**
* Anoxia triggers significant changes in gene expression, altering the production of proteins that help the organism cope with oxygen deprivation.
* These changes include the upregulation of genes encoding proteins involved in anaerobic metabolism, stress response, and cell survival.
**4. Physiological Adaptations:**
* In response to anoxia, organisms exhibit various physiological adaptations.
* These adaptations may include a reduction in metabolic rate, a slowing of heart rate, and a redistribution of blood flow to vital organs.
* Some organisms, such as fish and turtles, can enter a state of torpor or hibernation during prolonged anoxia, further reducing their energy requirements.
**5. Tissue Damage and Cell Death:**
* If anoxia persists, cellular damage can occur, leading to apoptosis (programmed cell death) or necrosis (uncontrolled cell death).
* The extent of tissue damage depends on the duration of anoxia, the tissue type, and the organism's ability to withstand oxygen deprivation.
**6. Recovery and Reoxygenation:**
* Upon reoxygenation, the organism undergoes a recovery process.
* This process involves restoring cellular energy levels, clearing accumulated lactic acid, and repairing any damage that may have occurred during anoxia.
* The duration and effectiveness of recovery depend on the severity and duration of oxygen deprivation.
**In summary, the response to anoxia is a crucial adaptation that allows organisms to survive in environments lacking oxygen. This response involves a complex interplay of cellular, metabolic, and physiological processes aimed at minimizing damage, preserving energy, and maintaining vital functions until oxygen is restored.**'
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Protein | Definition | Taxonomy |
---|---|---|
Oxytocin receptor | An oxytocin receptor that is encoded in the genome of human. [PRO:WCB, UniProtKB:P30559] | Homo sapiens (human) |
Compound | Definition | Classes | Roles |
---|---|---|---|
opc 21268 | OPC 21268: structure given in first source; vasopressin V1 receptor antagonist | ||
mozavaptan | mozavaptan: aquaretic agent; vasopressin V2 receptor antagonist; structure given in first source | benzamides | aquaretic |
lixivaptan | |||
oxytocin | oxytocin : A cyclic nonapeptide hormone with amino acid sequence CYIQNCPLG that also acts as a neurotransmitter in the brain; the principal uterine-contracting and milk-ejecting hormone of the posterior pituitary. Together with the neuropeptide vasopressin, it is believed to influence social cognition and behaviour. Oxytocin: A nonapeptide hormone released from the neurohypophysis (PITUITARY GLAND, POSTERIOR). It differs from VASOPRESSIN by two amino acids at residues 3 and 8. Oxytocin acts on SMOOTH MUSCLE CELLS, such as causing UTERINE CONTRACTIONS and MILK EJECTION. | heterodetic cyclic peptide; peptide hormone | oxytocic; vasodilator agent |
deaminooxytocin | demoxytocin : A heterodetic cyclic peptide that is the synthetic analog of the peptide hormone oxytocin where the free amino group in the half-cystine residue is replaced by hydrogen. The mechanism of action and pharmacological properties of demoxytocin and oxytocin are similar. The drug affects the permeability of the cell membrane, increasing the content of calcium ions in smooth muscle cells, thereby increasing its contraction. It stimulates the contraction of smooth muscles of the uterus, as well as stimulating the contraction of myoepithelial cells of the mammary gland, and enhances the secretion of milk. | heterodetic cyclic peptide | oxytocic |
arginine vasopressin | Arginine Vasopressin: The predominant form of mammalian antidiuretic hormone. It is a nonapeptide containing an ARGININE at residue 8 and two disulfide-linked cysteines at residues of 1 and 6. Arg-vasopressin is used to treat DIABETES INSIPIDUS or to improve vasomotor tone and BLOOD PRESSURE. argipressin : The predominant form of mammalian vasopressin (antidiuretic hormone). It is a nonapeptide containing an arginine at residue 8 and two disulfide-linked cysteines at residues of 1 and 6. | vasopressin | cardiovascular drug; hematologic agent; mitogen |
atosiban | oligopeptide | ||
deamino arginine vasopressin | Deamino Arginine Vasopressin: A synthetic analog of the pituitary hormone, ARGININE VASOPRESSIN. Its action is mediated by the VASOPRESSIN receptor V2. It has prolonged antidiuretic activity, but little pressor effects. It also modulates levels of circulating FACTOR VIII and VON WILLEBRAND FACTOR. | heterodetic cyclic peptide | diagnostic agent; renal agent; vasopressin receptor agonist |
l 372662 | L 372662: structure in first source | ||
way-151932 | WAY-151932: structure in first source | ||
l 371257 | L 371257: structure given in first source | ||
l 368899 | |||
ssr 149415 | |||
gsk221149a | GSK221149A: highly selective oxytocin receptor antagonist; structure in first source | dipeptide | |
epelsiban | epelsiban: structure in first source | dipeptide | |
carbetocin | carbetocin : Oxytocin in which the hydrogen on the phenolic hydroxy group is substituted by methyl, the amino group on the cysteine residue is substituted by hydrogen, and the sulfur of the cysteine residue is replaced by a methylene group. A synthetic carba-analogue of oxytocin, it is used to control bleeding after giving birth. Like oxytocin, it causes contraction of the uterus. | heterodetic cyclic peptide | oxytocic |
vasopressin, 1-deamino-4-val-8-arg- | |||
obe001 | OBE001: an oxytocin receptor antagonist | ||
way 267464 |