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Microprotein-Derived Secreted Peptide That Stimulates Cellular cAMP Production.

Joan M Vaughan1, Victor J Pai1, Brendan Miller1

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Researchers discovered novel bioactive peptides from the microproteome, including a secreted peptide from HCP5 RNA (HCP5-SP). This peptide stimulates cAMP signaling and cell proliferation, highlighting the microproteome as a source of functional endogenous peptides.

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Area of Science:

  • Molecular Biology
  • Genomics
  • Biochemistry

Background:

  • Microproteins, though short, may yield functional secreted peptides.
  • The biological activity of microprotein-derived peptides is largely unknown.
  • The human microproteome is a vast, untapped source of potential bioactive molecules.

Purpose of the Study:

  • To screen microproteome-derived secreted peptides for biological activity.
  • To identify novel endogenous peptides with signaling functions.
  • To investigate the function of a secreted peptide from HLA complex P5 RNA (HCP5).

Main Methods:

  • Screening a library of secreted micropeptides using GPCR signaling assays.
  • Measuring cAMP production downstream of GPCR activation.
  • In vitro synthesis and functional validation of identified peptides and analogs.

Main Results:

  • Identified several cAMP-stimulating peptides, including HCP5-secreted peptide (HCP5-SP).
  • HCP5-SP is encoded by a small open reading frame in HCP5 mRNA.
  • Wild-type C-terminal sequence is essential for HCP5-SP activity.
  • HCP5-SP promotes HEK293T cell proliferation, potentially linking to cancer biology.

Conclusions:

  • Established a workflow for identifying bioactive microproteins.
  • Demonstrated that the microproteome is a source of novel bioactive endogenous peptides.
  • HCP5-SP exhibits cAMP-stimulating activity and promotes cell proliferation.