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(Created page with '{{BioPsy}} Cleavage sites of [[phospholipases. Phospholipase C enzymes cut just before the phosphate attached to the R<sub>3<…')
 
(In other organisms: Took out section)
 
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{{Further|[[Calcium function in vertebrates]], [[Function of protein kinase C]]}}
 
{{Further|[[Calcium function in vertebrates]], [[Function of protein kinase C]]}}
 
==In other organisms==
 
Other phospholipase C enzymes have been identified in [[bacteria]] and in [[trypanosome]]s, each with its own [[EC number]]
 
 
* [[Phosphoinositide phospholipase C]] {{EC number|3.1.4.11}} The main form found in eukaryotes, especially mammals.
 
 
* [[Zinc-dependent phospholipase C]] family of bacterial enzymes {{EC number|3.1.4.3}} that includes [[alpha toxin]]s
 
 
* [[Phosphatidylinositol diacylglycerol-lyase]] {{EC number|4.6.1.13}} Another related bacterial enzyme
 
 
* [[Glycosylphosphatidylinositol diacylglycerol-lyase]] {{EC number|4.6.1.14}} A trypanosomal enzyme.
 
   
 
==References==
 
==References==

Latest revision as of 07:14, May 14, 2010

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File:Phospholipases2.png

Phospholipase C is a class of enzymes that cleave phospholipids just before the phosphate group (see figure). It is most commonly taken to be synonymous with the human forms of this enzyme, which plays an important role in eukaryotic cell physiology, in particular signal transduction pathways. Thirteen kinds of mammalian phospholipase C are classified into six models (β, γ, δ, ε, ζ, η) according to structure.

Human variantEdit

The human variant has EC 3.1.4.11.

ActivationEdit

Receptors that activate this pathway are mainly G protein-coupled receptors coupled to the Gαq subunit, including:

Other, minor, activators than Gαq are:

EffectsEdit

PLC cleaves a phospholipid. In the process, phosphatidylinositol 4,5-bisphosphate (PIP2) is cleaved into diacyl glycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG remains bound to the membrane, and IP3 is released as a soluble structure into the cytosol. IP3 then diffuses through the cytosol to bind to IP3 receptors, particular calcium channels in the endoplasmic reticulum (ER). This causes the cytosolic concentration of calcium to increase, causing a cascade of intracellular changes and activity.[4] In addition, calcium and DAG together work to activate protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity.[4] End effects include taste, tumor promotion, etc.[4]

Further information: Calcium function in vertebrates, Function of protein kinase C

ReferencesEdit

  1. 1.0 1.1 1.2 1.3 1.4 Gq alpha subunit. Wikipedia. URL accessed on 2009-03-03.
  2. 2.0 2.1 Walter F., PhD. Boron (2003). Medical Physiology: A Cellular And Molecular Approaoch, 1300, Elsevier/Saunders. Page 104
  3. GeneGlobe -> GHRH Signaling Retrieved on May 31, 2009
  4. 4.0 4.1 4.2 Alberts B, Lewis J, Raff M, Roberts K, Walter P (2002). Molecular biology of the cell, 4th, New York: Garland Science.


Template:Eicosanoid metabolism enzymes

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