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Thermosensation

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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Combined Peripheral Nerve Stimulation and Controllable Pulse Parameter Transcranial Magnetic Stimulation to Probe Sensorimotor Control and Learning
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MSPL/TMPRSS13.

Hiroshi Kido1, Yuushi Okumura

  • 1Division of Enzyme Chemistry, Institute for Enzyme Research, The University of Tokushima, 3-18-15 Kuramoto-cho, Tokushima 770-8503, Japan. kido@ier.tokushima-u.ac.jp

Frontiers in Bioscience : a Journal and Virtual Library
|November 6, 2007
PubMed
Summary

Two novel serine proteases, mosaic seine protease large-form (MSPL) and transmembrane protease serine 13 (TMPRSS13), were identified. These transmembrane proteins show potential roles in processing prohormones and in viral/bacterial pathogenesis.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • Two novel serine protease cDNAs, MSPL and TMPRSS13, were identified in human lung tissue.
  • These proteins possess a type II transmembrane structure with distinct cytoplasmic tails and extracellular protease domains.

Purpose of the Study:

  • To characterize the structure, expression, and enzymatic properties of MSPL and TMPRSS13.
  • To investigate the potential biological roles of these newly identified proteases.

Main Methods:

  • Polymerase chain reaction (PCR) was used to identify MSPL and TMPRSS13 cDNAs.
  • Sequence analysis revealed structural similarities and differences.
  • Recombinant proteins were expressed and their enzymatic activities assessed.
  • Gene expression patterns were analyzed across various human tissues and cell types.

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Main Results:

  • MSPL and TMPRSS13 share identical serine protease sequences but differ at their C-terminal ends.
  • Protease domains exhibit sequence identity with known proteases like plasma kallikrein and TMPRSS2.
  • Both genes are widely expressed, with predominant expression in lung, placenta, pancreas, and prostate.
  • TMPRSS13 shows higher expression in thymus, spleen, and lymphocytes (CD8+ and CD19+ cells).
  • Enzymatic assays demonstrated preferential cleavage at paired basic amino acid residues, with inhibition by specific protease inhibitors.

Conclusions:

  • MSPL and TMPRSS13 are novel transmembrane serine proteases with distinct expression profiles.
  • Their enzymatic properties suggest roles in proteolytic processing of prohormones and growth factors.
  • These proteases may be involved in the pathogenicity of viruses and bacteria.