Proline-rich membrane anchor 1, also known as PRiMA, is a protein that in humans is encoded by the PRIMA1gene.[4][5]
Function
PRiMA functions to organize acetylcholinesterase (AChE) into tetramers, and to anchor AChE at neural cell membranes.[4] This is accomplished by the proline rich anchor domain (PRAD) of PRIMA1 which anchors the tetramer of AChE into the plasma membrane of neural cells and myocytes.[6] The PRAD interacts with the C-terminal T-peptide of AChE.[7]
PRiMA plays a role in targeting AChE to the cell surface and, in neuroblastoma cells, PRiMA the limiting factor of such targeting.[5] In both mice and humans, PRiMA exists as two alternative splice variants that differ in their cytoplasmic regions.
Clinical significance
The severity of neurogenerative diseases, such as Alzheimer’s, can be related to the degradation of AChE.[8]
^Xie HQ, Siow NL, Peng HB, Massoulié J, Tsim KW (Dec 2005). "Regulation of PRiMA: membrane anchor of acetylcholinesterase (AChE) in neuron and muscle". Chemico-Biological Interactions. 157–158: 432. Bibcode:2005CBI...157..432X. doi:10.1016/j.cbi.2005.10.093. PMID16429581.
^Perrier NA, Khérif S, Perrier AL, Dumas S, Mallet J, Massoulié J (Oct 2003). "Expression of PRiMA in the mouse brain: membrane anchoring and accumulation of 'tailed' acetylcholinesterase". The European Journal of Neuroscience. 18 (7): 1837–47. doi:10.1046/j.1460-9568.2003.02914.x. PMID14622217. S2CID21808922.
^Atack JR, Perry EK, Bonham JR, Perry RH, Tomlinson BE, Blessed G, Fairbairn A (Sep 1983). "Molecular forms of acetylcholinesterase in senile dementia of Alzheimer type: selective loss of the intermediate (10S) form". Neuroscience Letters. 40 (2): 199–204. doi:10.1016/0304-3940(83)90302-6. PMID6633975. S2CID45149066.
