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Peripheral thermosensation is the perception of external temperature. A change in temperature (on the surface of the skin and other tissues) is detected by a family of temperature-sensitive ion channels called Transient Receptor Potential, or TRP, receptors. These receptors are located on free nerve endings. Those detecting cold temperatures are closer to the surface of the skin than the nerve endings detecting warmth. These thermoTRP channels, while temperature selective, have relatively...
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Strategies for Study of Neuroprotection from Cold-preconditioning
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Phosphoproteome profiling for cold temperature perception.

Seyeon Park1, Mi Jang

  • 1Department of Applied Chemistry, Dongduk Women's University, Seoul, Korea. sypark21@dongduk.ac.kr

Journal of Cellular Biochemistry
|January 27, 2011
PubMed
Summary

This study used phosphoproteome profiling to identify cellular changes in human lung cells responding to cold. Researchers found RNA-related proteins were key to cold sensation, with specific markers verified.

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Area of Science:

  • Cellular Biology
  • Molecular Biology
  • Physiology

Background:

  • Temperature sensation is initiated by cellular receptors responding to decreased temperatures.
  • Understanding cellular cold responses is crucial for various biological processes.
  • Human lung epithelial cells (BEAS-2B) serve as a model for investigating cold-induced cellular changes.

Purpose of the Study:

  • To elucidate intracellular phosphorylation changes associated with cold sensation in human lung epithelial cells.
  • To identify specific proteins and pathways involved in cellular cold response.
  • To investigate the temporal dynamics of phosphoproteome alterations under cold stress.

Main Methods:

  • Phosphoproteome profiling was applied to BEAS-2B cells exposed to cold stimuli (18°C and 10°C).
  • Quantitative analysis identified differentially phosphorylated protein spots over time (5, 10, 30, and 60 minutes).
  • Western blotting was used to verify the phosphorylation of specific cold-responsive markers in TRPM8/TRPA1 transfected cells.

Main Results:

  • Eighteen protein spots showed differential phosphorylation in response to cold exposure.
  • Most identified proteins were RNA-related, involved in RNA binding and splicing.
  • A time-shift in phosphoproteome changes was observed between the two temperature stimuli, with most proteins returning to baseline levels within 60 minutes.

Conclusions:

  • Cold exposure triggers significant, yet transient, changes in the phosphoproteome of lung epithelial cells.
  • RNA-related proteins play a critical role in the cellular response to cold.
  • Specific proteins like ribosomal protein large P0 and heterochromatin-associated proteins 1 are potential cold-responsive markers.