Foulkes, T; Nassar, MA; Lane, T; Matthews, EA; Baker, MD; Gerke, V; Okuse, K; ... Wood, JN; + view all Foulkes, T; Nassar, MA; Lane, T; Matthews, EA; Baker, MD; Gerke, V; Okuse, K; Dickenson, AH; Wood, JN; - view fewer (2006) Deletion of annexin 2 light chain p11 in nociceptors causes deficits in somatosensory coding and pain behavior. J NEUROSCI , 26 (41) 10499 - 10507. 10.1523/JNEUROSCI.1997-06.2006.

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Abstract

The S100 family protein p11 (S100A10, annexin 2 light chain) is involved in the trafficking of the voltage-gated sodium channel Na(V)1.8, 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.

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