PMID- 24085547
OWN - NLM
STAT- MEDLINE
DCOM- 20141106
LR  - 20211203
IS  - 1932-846X (Electronic)
IS  - 1932-8451 (Print)
IS  - 1932-8451 (Linking)
VI  - 74
IP  - 3
DP  - 2014 Mar
TI  - Axonal protein synthesis and the regulation of primary afferent function.
PG  - 269-78
LID - 10.1002/dneu.22133 [doi]
AB  - Local protein synthesis has been demonstrated in the peripheral processes of 
      sensory primary afferents and is thought to contribute to the maintenance of the 
      neuron, to neuronal plasticity following injury and also to regeneration of the 
      axon after damage to the nerve. The mammalian target of rapamycin (mTOR), a 
      master regulator of protein synthesis, integrates a variety of cues that regulate 
      cellular homeostasis and is thought to play a key role in coordinating the 
      neuronal response to environmental challenges. Evidence suggests that activated 
      mTOR is expressed by peripheral nerve fibers, principally by A-nociceptors that 
      rapidly signal noxious stimulation to the central nervous system, but also by a 
      subset of fibers that respond to cold and itch. Inhibition of mTOR complex 1 
      (mTORC1) has shown that while the acute response to noxious stimulation is 
      unaffected, more complex aspects of pain processing including the setting up and 
      maintenance of chronic pain states can be disrupted suggesting a route for the 
      generation of new drugs for the control of chronic pain. Given the role of mTORC1 
      in cellular homeostasis, it seems that systemic changes in the physiological 
      state of the body such as occur during illness are likely to modulate the 
      sensitivity of peripheral sensory afferents through mTORC1 signaling pathways.
CI  - Copyright (c) 2013 The Authors. Developmental Neurobiology Published by Wiley 
      Periodicals, Inc.
FAU - Obara, Ilona
AU  - Obara I
AD  - Department of Cell and Developmental Biology, University College London, Gower 
      Street, London WC1E 6BT, United Kingdom; School of Medicine, Pharmacy and Health, 
      Durham University, Stockton-on-Tees TS17 6BH, United Kingdom.
FAU - Hunt, Stephen P
AU  - Hunt SP
LA  - eng
GR  - G0801381/Medical Research Council/United Kingdom
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PT  - Review
DEP - 20131108
PL  - United States
TA  - Dev Neurobiol
JT  - Developmental neurobiology
JID - 101300215
RN  - 0 (Multiprotein Complexes)
RN  - EC 2.7.11.1 (Mechanistic Target of Rapamycin Complex 1)
RN  - EC 2.7.11.1 (TOR Serine-Threonine Kinases)
SB  - IM
MH  - Afferent Pathways/physiology
MH  - Animals
MH  - Axons/*metabolism
MH  - Homeostasis
MH  - Humans
MH  - Mechanistic Target of Rapamycin Complex 1
MH  - Multiprotein Complexes/metabolism
MH  - Neurons, Afferent/*physiology
MH  - Nociception/physiology
MH  - *Protein Biosynthesis
MH  - Pruritus/metabolism
MH  - TOR Serine-Threonine Kinases/metabolism
MH  - Thermosensing/physiology
PMC - PMC4237183
OTO - NOTNLM
OT  - itch
OT  - local translation
OT  - nociceptors
OT  - pain
OT  - the mammalian target of rapamycin complex 1 (mTORC1)
EDAT- 2013/10/03 06:00
MHDA- 2014/11/07 06:00
PMCR- 2014/11/19
CRDT- 2013/10/03 06:00
PHST- 2013/06/20 00:00 [received]
PHST- 2013/08/27 00:00 [revised]
PHST- 2013/09/15 00:00 [accepted]
PHST- 2013/10/03 06:00 [entrez]
PHST- 2013/10/03 06:00 [pubmed]
PHST- 2014/11/07 06:00 [medline]
PHST- 2014/11/19 00:00 [pmc-release]
AID - 10.1002/dneu.22133 [doi]
PST - ppublish
SO  - Dev Neurobiol. 2014 Mar;74(3):269-78. doi: 10.1002/dneu.22133. Epub 2013 Nov 8.