| First Author | Okuda-Ashitaka E | Year | 2012 |
| Journal | J Biol Chem | Volume | 287 |
| Issue | 13 | Pages | 10403-13 |
| PubMed ID | 22311985 | Mgi Jnum | J:183272 |
| Mgi Id | MGI:5318155 | Doi | 10.1074/jbc.M111.271866 |
| Citation | Okuda-Ashitaka E, et al. (2012) Identification of NIPSNAP1 as a nocistatin-interacting protein involving pain transmission. J Biol Chem 287(13):10403-13 |
| abstractText | 4-Nitrophenylphosphatase domain and non-neuronal SNAP25-like protein homolog 1 (NIPSNAP1) is a molecule of physiologically unknown function, although it is predominantly expressed in the brain, spinal cord, liver, and kidney. We identified NIPSNAP1 as a protein that interacts with the neuropeptide nocistatin (NST) from synaptosomal membranes of mouse spinal cord using high-performance affinity latex beads. NST, which is produced from the same precursor protein as an opioid-like neuropeptide nociceptin/orphanin FQ (N/OFQ), has opposite effects on pain transmission evoked by N/OFQ. The calculated full-length pre-protein of NIPSNAP1 was 33 kDa, whereas the N-terminal truncated form of NIPSNAP1 (29 kDa) was ubiquitously expressed in the neuronal tissues, especially in synaptic membrane and mitochondria of brain. The 29-kDa NIPSNAP1 was distributed on the cell surface, and NST interacted with the 29-kDa but not the 33-kDa NIPSNAP1. Although intrathecal injection of N/OFQ induced tactile allodynia in both wild-type and NIPSNAP1-deficient mice, the inhibition of N/OFQ-evoked tactile allodynia by NST seen in wild-type mice was completely lacking in the deficient mice. These results suggest that NIPSNAP1 is an interacting molecule of NST and plays a crucial role in pain transmission. |
