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Related Experiment Videos

Vasoactive intestinal peptide and anterior pituitary function.

R A Prysor-Jones1, J S Jenkins

  • 1Department of Medicine, St. George's Hospital Medical School, London, UK.

Clinical Endocrinology
|December 1, 1988
PubMed
Summary

Vasoactive intestinal peptide (VIP) is a 28 amino-acid peptide found in the small intestine. Human VIP shares an identical amino-acid sequence with the porcine form and is co-synthesized with another peptide from a common precursor protein.

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Area of Science:

  • Biochemistry
  • Endocrinology
  • Molecular Biology

Background:

  • Vasoactive intestinal peptide (VIP) is a basic 28 amino-acid peptide.
  • VIP was initially isolated from porcine small intestine in 1970.
  • It shares structural similarities with other peptides like secretin and glucagon.

Purpose of the Study:

  • To detail the characteristics of Vasoactive intestinal peptide (VIP).
  • To compare the amino-acid sequence of human VIP with its porcine counterpart.
  • To investigate the synthesis of human VIP.

Main Methods:

  • Peptide isolation and sequencing.
  • Amino-acid sequence analysis.
  • Gene expression and protein precursor studies.

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Main Results:

  • The amino-acid sequence of human VIP is identical to the porcine form.
  • Human VIP is co-synthesized with peptide with N-terminal histidine and C-terminal methionine amide (PHM).
  • Both VIP and PHM originate from the same large precursor protein.

Conclusions:

  • Confirms the structural identity between human and porcine VIP.
  • Elucidates the co-synthesis mechanism of VIP and PHM.
  • Highlights the conserved nature of VIP across species and its complex precursor processing.