Transient Receptor Potential Cation Channel, Member A1
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Transient Receptor Potential Cation Channel, Member A1
Transient receptor potential cation channel, subfamily A, member 1, also known as transient receptor potential ankyrin 1, TRPA1, or The Wasabi Receptor, is a protein that in humans is encoded by the ''TRPA1'' (and in mice and rats by the ''Trpa1'') gene. TRPA1 is an ion channel located on the plasma membrane of many human and animal cells. This ion channel is best known as a sensor for pain, cold and itch in humans and other mammals, as well as a sensor for environmental irritants giving rise to other protective responses (tears, airway resistance, and cough). Function TRPA1 is a member of the transient receptor potential channel family. TRPA1 contains 14 N-terminal ankyrin repeats and is believed to function as a mechanical and chemical stress sensor. One of the specific functions of this protein studies involves a role in the detection, integration and initiation of pain signals in the peripheral nervous system. It can be activated at sites of tissue injury or sites of infl ...
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Protein
Proteins are large biomolecules and macromolecules that comprise one or more long chains of amino acid residues. Proteins perform a vast array of functions within organisms, including catalysing metabolic reactions, DNA replication, responding to stimuli, providing structure to cells and organisms, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific 3D structure that determines its activity. A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than 20–30 residues, are rarely considered to be proteins and are commonly called peptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residue ...
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Nociception
Nociception (also nocioception, from Latin ''nocere'' 'to harm or hurt') is the sensory nervous system's process of encoding noxious stimuli. It deals with a series of events and processes required for an organism to receive a painful stimulus, convert it to a molecular signal, and recognize and characterize the signal in order to trigger an appropriate defense response. In nociception, intense chemical (e.g., capsaicin present in Chili pepper or Cayenne pepper), mechanical (e.g., cutting, crushing), or thermal (heat and cold) stimulation of sensory neurons called nociceptors produces a signal that travels along a chain of nerve fibers via the spinal cord to the brain. Nociception triggers a variety of physiological and behavioral responses to protect the organism against an aggression and usually results in a subjective experience, or perception, of pain in sentient beings. Detection of noxious stimuli Potentially damaging mechanical, thermal, and chemical stimuli are detected ...
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Phosphatidylinositol 4,5-bisphosphate
Phosphatidylinositol 4,5-bisphosphate or PtdIns(4,5)''P''2, also known simply as PIP2 or PI(4,5)P2, is a minor phospholipid component of cell membranes. PtdIns(4,5)''P''2 is enriched at the plasma membrane where it is a substrate for a number of important signaling proteins. PIP2 also forms lipid clusters that sort proteins. PIP2 is formed primarily by the type I phosphatidylinositol 4-phosphate 5-kinases from PI(4)P. In metazoans, PIP2 can also be formed by type II phosphatidylinositol 5-phosphate 4-kinases from PI(5)P. The fatty acids of PIP2 are variable in different species and tissues, but the most common fatty acids are stearic in position 1 and arachidonic in 2. Signaling pathways PIP2 is a part of many cellular signaling pathways, including PIP2 cycle, PI3K signalling, and PI5P metabolism. Recently, it has been found in the nucleus with unknown function. Functions Cytoskeleton dynamics near membranes PIP2 regulates the organization, polymerization, and bran ...
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Polyphosphate
Polyphosphates are salts or esters of polymeric oxyanions formed from tetrahedral PO4 (phosphate) structural units linked together by sharing oxygen atoms. Polyphosphates can adopt linear or a cyclic ring structures. In biology, the polyphosphate esters ADP and ATP are involved in energy storage. A variety of polyphosphates find application in mineral sequestration in municipal waters, generally being present at 1 to 5 ppm. GTP, CTP, and UTP are also nucleotides important in the protein synthesis, lipid synthesis, and carbohydrate metabolism, respectively. Polyphosphates are also used as food additives, marked E452. Structure Image:Triphosphorsäure.svg, Structure of triphosphoric acid Image:Polyphosphoric acid.svg, Polyphosphoric acid Image:Trimetaphosphat.svg, Cyclic trimetaphosphate Image:Adenosindiphosphat protoniert.svg, Adenosine diphosphate (ADP) The structure of tripolyphosphoric acid illustrates the principles which define the structures of polyphosp ...
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Calcium In Biology
Calcium ions (Ca2+) contribute to the physiology and biochemistry of organisms' cell (biology), cells. They play an important role in signal transduction pathways, where they act as a second messenger, in neurotransmitter release from neurons, in contraction of all muscle cell types, and in fertilization. Many enzymes require calcium ions as a Cofactor (biochemistry), cofactor, including several of the coagulation factors. Extracellular calcium is also important for maintaining the potential difference across excitable cell cell membrane, membranes, as well as proper bone formation. Plasma calcium levels in mammals are tightly regulated, electronic-book electronic- with bone acting as the major mineral storage site. Calcium ions, Ca2+, are released from bone into the bloodstream under controlled conditions. Calcium is transported through the bloodstream as dissolved ions or bound to proteins such as serum albumin. Parathyroid hormone secreted by the parathyroid gland regulates ...
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Second Messenger System
Second messengers are intracellular signaling molecules released by the cell in response to exposure to extracellular signaling molecules—the first messengers. (Intercellular signals, a non-local form or cell signaling, encompassing both first messengers and second messengers, are classified as autocrine, juxtacrine, paracrine, and endocrine depending on the range of the signal.) Second messengers trigger physiological changes at cellular level such as proliferation, differentiation, migration, survival, apoptosis and depolarization. They are one of the triggers of intracellular signal transduction cascades. Examples of second messenger molecules include cyclic AMP, cyclic GMP, inositol triphosphate, diacylglycerol, and calcium. First messengers are extracellular factors, often hormones or neurotransmitters, such as epinephrine, growth hormone, and serotonin. Because peptide hormones and neurotransmitters typically are biochemically hydrophilic molecules, these first messenger ...
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Homotetramer
A tetrameric protein is a protein with a protein quaternary structure, quaternary structure of four subunits (tetrameric). Homotetramers have four identical Protein subunit, subunits (such as glutathione S-transferase), and heterotetramers are Multiprotein complex, complexes of different subunits. A tetramer can be assembled as dimer of dimers with two homodimer subunits (such as sorbitol dehydrogenase), or two heterodimer subunits (such as hemoglobin). Subunit interactions in tetramers The interactions between subunits forming a tetramer is primarily determined by non covalent interaction. Hydrophobic effects, hydrogen bonds and electrostatic interactions are the primary sources for this binding process between subunits. For homotetrameric proteins such as Sorbitol dehydrogenase (SDH), the structure is believed to have evolved going from a monomeric to a dimeric and finally a tetrameric structure in evolution. The binding process in SDH and many other tetrameric enzymes can be ...
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Cryogenic Electron Microscopy
Cryogenic electron microscopy (cryo-EM) is a cryomicroscopy technique applied on samples cooled to cryogenic temperatures. For biological specimens, the structure is preserved by embedding in an environment of vitreous ice. An aqueous sample solution is applied to a grid-mesh and plunge-frozen in liquid ethane or a mixture of liquid ethane and propane. While development of the technique began in the 1970s, recent advances in detector technology and software algorithms have allowed for the determination of biomolecular structures at near-atomic resolution. This has attracted wide attention to the approach as an alternative to X-ray crystallography or NMR spectroscopy for macromolecular structure determination without the need for crystallization. In 2017, the Nobel Prize in Chemistry was awarded to Jacques Dubochet, Joachim Frank, and Richard Henderson "for developing cryo-electron microscopy for the high-resolution structure determination of biomolecules in solution." ''Nature ...
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Hyalinobatrachium Fleischmanni
''Hyalinobatrachium fleischmanni'', also known as Fleischmann's glass frog or the northern glass frog, is a species of frog in the family Centrolenidae. It is found in the tropical Americas from southern Mexico to Ecuador. Specifically, these frogs occur in Mexico, Belize, Costa Rica, El Salvador, Guatemala, Honduras, Nicaragua, and Panama, Colombia, and Ecuador. Notice that this and related species have often been confused with each other, and the exact distribution depends on the source. This frog tends to have green skin, pale yellowish spots, yellow fingertips and translucent skin covering its stomach. Etymology The specific name ''fleischmanni'' honors Carl Fleischmann, a collector in Costa Rica in the 1890s. Description ''H. fleischmanni'' are small and arboreal frogs that lives in lowland and mid-elevation forests of Central and South America. They call during the rainy season. Glass frogs have similarities to tree frogs. They look very close to the naked eye except glass ...
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Infrared Sensing In Snakes
The ability to sense infrared thermal radiation evolved independently in two different groups of snakes, one consisting of the families Boidae (boas) and Pythonidae (pythons), the other of the family Crotalinae (pit vipers). What is commonly called a pit organ allows these animals to essentially "see" radiant heat at wavelengths between 5 and 30 Micrometre, μm. The more advanced infrared sense of pit vipers allows these animals to strike prey accurately even in the absence of light, and detect warm objects from several meters away. It was previously thought that the organs evolved primarily as prey detectors, but recent evidence suggests that it may also be used in thermoregulation and predator detection, making it a more general-purpose sensory organ than was supposed.Greene HW. 1992. The ecological and behavioral context for pitviper evolution. ''In'' Campbell JA, Brodie ED Jr. 1992. Biology of the Pitvipers. Texas: Selva. 467 pp. 17 plates. . Phylogeny and evolution The fa ...
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Loreal Pit
The loreal pit is the deep depression, or fossa, in the loreal area on either side of the head in pit vipers (crotaline snakes). The area is located behind the nostril and in front of the eye, but below the line that runs between the centers of each. It is the external opening to an extremely sensitive infrared detecting organ. The loreal pit is bordered by lacunal scales. The loreal pit also functions as part of a thermal regulating system, enabling pit vipers to maintain their body temperature. References Snake anatomy {{snake-stub ...
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Freund's Adjuvant
Freund's adjuvant is a solution of antigen emulsified in mineral oil and used as an immunopotentiator (booster). The complete form, Freund's Complete Adjuvant (FCA or CFA) is composed of inactivated and dried mycobacteria (usually '' M. tuberculosis''), whereas the incomplete form (FIA or IFA) lacks the mycobacterial components (hence just the water in oil emulsion). It is named after Jules T. Freund. Regulation Freund's complete adjuvant is effective in stimulating cell-mediated immunity and leads to potentiation of T helper cells that leads to the production of certain immunoglobulins and effector T cells. Its use in humans is forbidden by regulatory authorities, due to its toxicity. Even for animal research there are currently guidelines associated with its use, due to its painful reaction and potential for tissue damage. Injections of FCA should be subcutaneous or intraperitoneal, because intradermal injections may cause skin ulceration and necrosis; intramuscular injections m ...
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