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Overview of gastrointestinal peptides in health and disease

Rodger A Liddle, MD
Section Editor
J Thomas Lamont, MD
Deputy Editor
Shilpa Grover, MD, MPH, AGAF


Gastrointestinal (GI) hormones are predominantly polypeptides produced in and secreted from specialized gut endocrine cells [1,2]. These cells produce a variety of chemical transmitters that are involved in GI motility, secretion, absorption, growth, and development. Many of the peptides in the GI tract are also found in the enteric nervous system and the central nervous system.

An overview of the synthesis, secretion, and regulation of GI peptides; their role in causing disease; and their clinical application will be discussed here. The regulation and functions of the individual GI peptides are discussed separately. (See "Physiology of gastrin" and "Ghrelin" and "Pancreatic polypeptide, peptide YY, and neuropeptide Y" and "Insulin action" and "Physiology of somatostatin and its analogues" and "Physiology of cholecystokinin" and "Secretin".)


Gastrointestinal (GI) peptides are classified into families based on their primary structure (table 1). Conservation of amino acid sequence among different GI peptides suggests a common biosynthetic origin.


Synthesis — Enteroendocrine cells producing gastrointestinal (GI) peptides are dispersed throughout the GI tract. However, specific types of cells demonstrate regional specificity (table 2) [3]. This specificity may be related to the physiologic action of the peptide and receptor location.

All GI peptides are synthesized via gene transcription of DNA into messenger RNA (mRNA) and subsequently undergo translation into precursor proteins known as preprohormones. Translation occurs on ribosomes, which are complex organelles composed of many proteins (greater than 50) and multiple large RNA molecules [4,5].

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Literature review current through: Nov 2017. | This topic last updated: May 23, 2016.
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