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Related Experiment Videos

Serotonin binding protein: synthesis, secretion, and recycling

H Tamir1, K P Liu, S Hsiung

  • 1Division of Neuroscience, New York State Psychiatric Institute, NY 10032.

Journal of Neurochemistry
|July 1, 1994
PubMed
Summary

Serotonin binding protein (SBP) forms are primary translation products, not derived from cleavage. The 45-kDa SBP is secreted and located on cell surfaces, indicating its role in serotonergic vesicles.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Neuroscience

Background:

  • Serotonin binding protein (SBP) is crucial for serotonin (5-HT) storage in neurectodermally derived cells.
  • Three distinct SBP forms (68, 56, and 45 kDa) exist, all reactive with anti-SBP antibodies that inhibit 5-HT binding.

Purpose of the Study:

  • To investigate if 56- and 45-kDa SBP forms result from posttranslational cleavage of a 68-kDa precursor.
  • To determine if 45-kDa SBP is a component of serotonergic secretory vesicles.

Main Methods:

  • Pulse-chase experiments using [35S]methionine labeling in medullary thyroid carcinoma cells.
  • Immunoprecipitation and electrophoretic analysis of SBP forms under varying chase conditions (temperature, ATP inhibition).
  • Analysis of SBP secretion and cell surface localization upon induction.

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Main Results:

  • All three SBP forms (68, 56, 45 kDa) were found to be independently synthesized as primary translation products.
  • The relative proportions of SBP forms remained constant, unaffected by chase conditions, indicating no precursor cleavage.
  • 45-kDa SBP was secreted and detected on the cell surface, while 56- and 68-kDa forms were not secreted.

Conclusions:

  • The distinct SBP forms are primary translation products, not generated by proteolytic processing of a larger precursor.
  • 45-kDa SBP is specifically localized to and secreted from serotonergic vesicles.
  • The size of SBP translation products is not altered during transit through the Golgi apparatus or post-Golgi compartments.