Chimerin

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Chimerin is a type of nerve tissue protein.[1]

Chimerins are a family of non-PKC phorbol-ester receptors. They were the first to be discovered within this family. The name stems from their resemblance to the "chimera." There are four known isoforms of the Chimerin protein. These include α1, α2, β1, and β2. α1-Chimerin was the first protein to be isolated from the brain. The other domains were discovered through alternative splicing. The α and β isoforms are almost identical, the key difference stems from the SH2 domain at the N-terminal.

α1-Chimerin is a GTPase-activating protein in the brain that effects the ras related p21rac. α1-Chimerin is also able to regulate dendritic spinal density by binding to NMDA receptors at the NR2A subunit. Over expression of this protein in hippocampus tissue can inhibit the formation of new spines and remove existing spines.[2]

α2-Chimerin acts in a similar manner to α1-Chimerin, but is primarily found in the brain and testes. It is also an SH2 containing GTPase activating protein and bears many similarities in function. It Is derived from alternative splicing of the α-Chimera gene.[3]

β2-chimerin has been shown to play a role in breast cancer. In breast cancer cells the amount of β2-chimerin messengers are extremely low. When introduced to the cancerous cells β2-chimerin then causes the G1 cell cycle  to stop and therefore it stops the cells from multiplying.[4]

β2-chimerin can be linked to a fusion gene that is associated with a key insulin receptor that causes people to have decreased levels of insulin.[5]

References[]

  1. ^ Chimerin+Proteins at the US National Library of Medicine Medical Subject Headings (MeSH)
  2. ^ Van de Ven, Thomas J.; VanDongen, Hendrika M. A.; VanDongen, Antonius M. J. (2005-10-12). "The nonkinase phorbol ester receptor alpha 1-chimerin binds the NMDA receptor NR2A subunit and regulates dendritic spine density". The Journal of Neuroscience. 25 (41): 9488–9496. doi:10.1523/JNEUROSCI.2450-05.2005. ISSN 1529-2401. PMC 6725706. PMID 16221859.
  3. ^ Hall, C.; Sin, W. C.; Teo, M.; Michael, G. J.; Smith, P.; Dong, J. M.; Lim, H. H.; Manser, E.; Spurr, N. K.; Jones, T. A. (1993-08-01). "Alpha 2-chimerin, an SH2-containing GTPase-activating protein for the ras-related protein p21rac derived by alternate splicing of the human n-chimerin gene, is selectively expressed in brain regions and testes". Molecular and Cellular Biology. 13 (8): 4986–4998. doi:10.1128/MCB.13.8.4986. ISSN 0270-7306. PMC 360144. PMID 8336731.
  4. ^ Yang, Chengfeng; Liu, Ying; Leskow, Federico Coluccio; Weaver, Valerie M.; Kazanietz, Marcelo G. (2005-07-01). "Rac-GAP-dependent Inhibition of Breast Cancer Cell Proliferation by β2-Chimerin". Journal of Biological Chemistry. 280 (26): 24363–24370. doi:10.1074/jbc.M411629200. ISSN 0021-9258. PMID 15863513. S2CID 84567020.
  5. ^ Suliman, Sara G.I.; Stanik, Juraj; McCulloch, Laura J.; Wilson, Natalie; Edghill, Emma L.; Misovicova, Nadezda; Gasperikova, Daniela; Sandrikova, Vilja; Elliott, Katherine S.; Barak, Lubomir; Ellard, Sian (December 2009). "Severe Insulin Resistance and Intrauterine Growth Deficiency Associated With Haploinsufficiency for INSR and CHN2: New Insights Into Synergistic Pathways Involved in Growth and Metabolism". Diabetes. 58 (12): 2954–2961. doi:10.2337/db09-0787. ISSN 0012-1797. PMC 2780873. PMID 19720790.


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