Phosphocholine

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Phosphocholine
Skeletal formula
Ball-and-stick model
Names
Other names
Choline phosphate
Identifiers
3D model (JSmol)
MeSH Phosphocholine
  • C[N+](C)(C)CCOP(O)(O)=O
Properties
C5H15NO4P+
Molar mass 184.151 g/mol
Except where otherwise noted, data are given for materials in their standard state (at 25 °C [77 °F], 100 kPa).
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Not to be confused with phosphatidylcholine.

Phosphocholine is an intermediate in the synthesis of phosphatidylcholine in tissues. Phosphocholine is made in a reaction, catalyzed by choline kinase, that converts ATP and choline into phosphocholine and ADP. Phosphocholine is a molecule found, for example, in lecithin.

It is also used by nematodes and human placentas as a posttranslational modification to suppress an immune response by their hosts.[1][2]

It is also one of the binding targets of C-reactive protein (CRP).[3] Thus, when a cell is damaged, CRP binds to phosphocholine, beginning the recognition and phagocytotic immunologic response.

Phosphocholine is a natural constituent of hens' eggs (and many other eggs) often used in biomimetic membrane studies.[4]

See also

References

  1. ^ Lovell TM, Woods RJ, Butlin DJ; et al. (September 2007). "Identification of a novel mammalian post-translational modification, phosphocholine, on placental secretory polypeptides". J. Mol. Endocrinol. 39 (3): 189–98. doi:10.1677/JME-07-0007. PMC 2189575. PMID 17766644. {{cite journal}}: Explicit use of et al. in: |author= (help)CS1 maint: multiple names: authors list (link)
  2. ^ "Placenta 'fools body's defences'". BBC News. 2007-11-10. Retrieved 2010-05-22.
  3. ^ Thompson D, Pepys MB, Wood SP. (1999). "The physiological structure of human C-reactive protein and its complex with phosphocholine". Structure. 7 (2): 169–77. doi:10.1016/S0969-2126(99)80023-9. PMID 10368284.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  4. ^ Rose L, Jenkins ATA (2006). "The effect of the ionophore valinomycin on biomimetic solid supported lipid DPPTE/EPC membranes". Bioelectrochem. 70 (2): 387–93. doi:10.1016/j.bioelechem.2006.05.009. PMID 16875886.

External links