TY - JOUR T1 - Deletion of Annexin 2 Light Chain p11 in Nociceptors Causes Deficits in Somatosensory Coding and Pain Behavior JF - The Journal of Neuroscience JO - J. Neurosci. SP - 10499 LP - 10507 DO - 10.1523/JNEUROSCI.1997-06.2006 VL - 26 IS - 41 AU - Thomas Foulkes AU - Mohammed A. Nassar AU - Tim Lane AU - Elizabeth A. Matthews AU - Mark D. Baker AU - Volker Gerke AU - Kenji Okuse AU - Anthony H. Dickenson AU - John N. Wood Y1 - 2006/10/11 UR - http://www.jneurosci.org/content/26/41/10499.abstract N2 - The S100 family protein p11 (S100A10, annexin 2 light chain) is involved in the trafficking of the voltage-gated sodium channel NaV1.8, TWIK-related acid-sensitive K+ channel (TASK-1), the ligand-gated ion channels acid-sensing ion channel 1a (ASIC1a) and transient receptor potential vanilloid 5/6 (TRPV5/V6), as well as 5-hydroxytryptamine receptor 1B (5-HT1B), a G-protein-coupled receptor. To evaluate the role of p11 in peripheral pain pathways, we generated a loxP-flanked (floxed) p11 mouse and used the Cre-loxP recombinase system to delete p11 exclusively from nociceptive primary sensory neurons in mice. p11-null neurons showed deficits in the expression of NaV1.8, but not of annexin 2. Damage-sensing primary neurons from these animals show a reduced tetrodotoxin-resistant sodium current density, consistent with a loss of membrane-associated NaV1.8. Noxious coding in wide-dynamic-range neurons in the dorsal horn was markedly compromised. Acute pain behavior was attenuated in certain models, but no deficits in inflammatory pain were observed. A significant deficit in neuropathic pain behavior was also apparent in the conditional-null mice. These results confirm an important role for p11 in nociceptor function. ER -