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Related Experiment Videos

Proteolytic processing yields two secreted forms of sonic hedgehog

D A Bumcrot1, R Takada, A P McMahon

  • 1Department of Molecular and Cellular Biology, Harvard University, Cambridge, Massachusetts 02138.

Molecular and Cellular Biology
|April 1, 1995
PubMed
Summary
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Sonic hedgehog (Shh) protein is processed into two secreted peptides. These peptides may have distinct roles in regulating cell interactions during embryonic development.

Area of Science:

  • Developmental Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Sonic hedgehog (Shh) is a signaling molecule crucial for embryonic development.
  • Shh plays roles in floor plate induction, somite patterning, and limb polarity.
  • Its precise biochemical processing and function require further investigation.

Purpose of the Study:

  • To investigate the biochemical processing of Sonic hedgehog (Shh) protein.
  • To determine the molecular characteristics and potential functions of Shh processing products.
  • To confirm if Shh processing occurs during normal embryonic development.

Main Methods:

  • Expression of mouse Shh in Xenopus oocytes, COS cells, and insect cells.
  • Analysis of Shh protein processing, including signal peptide cleavage, glycosylation, and proteolytic cleavage.

Related Experiment Videos

  • Investigation of Shh peptide interactions with cell surfaces and extracellular matrix components using heparin and suramin.
  • Detection of Shh processing products in various embryonic tissues.

    • Main Results:

    • Shh protein undergoes proteolytic processing into approximately 19 kDa (amino-terminal) and 27 kDa (carboxy-terminal) peptides.
    • Both processed peptides are secreted, but the 19 kDa peptide's accumulation is enhanced by heparin or suramin, indicating cell-associated retention.
    • This retention is dependent on sequences within the carboxy-terminal portion of the 19 kDa peptide.
    • The same proteolytic processing of Shh is observed in mouse and chicken embryonic tissues, confirming its occurrence during development.

    Conclusions:

    • Sonic hedgehog (Shh) protein is processed into distinct amino- and carboxy-terminal peptides.
    • These peptides are secreted and may interact with the cell surface or extracellular matrix.
    • The processing of Shh observed in vitro reflects a normal developmental process.
    • The distinct Shh peptides may possess separate functions in regulating cell-cell interactions in the embryo.