The trefoil peptide family

B. E. Sands, D. K. Podolsky

Research output: Contribution to journalReview article

193 Scopus citations

Abstract

The unique three-loop structure of the trefoil motif, formed by intrachain disulfide bonds in a 1-5, 2-4, 3-6 configuration between six conserved cysteine residues, is the defining feature of a recently recognized family of peptides. Expression of trefoil peptides is closely related to that of mucin glycoproteins in diverse biological sources. Three distinct members of the family (pS2, intestinal trefoil factor, and spasmolytic polypeptide) are produced in the mammalian gastrointestinal tract by mucus-secreting cells and targeted primarily for luminal secretion. The compact structure of the trefoil motif may be responsible for marked resistance of trefoil peptides to proteolytic digestion, enabling them to function in the harsh environment of the gastrointestinal lumen. Trefoil peptides are ectopically expressed adjacent to areas of inflammation within the gastrointestinal tract and may play an important role in both maintaining die barrier function of mucosal surfaces and facilitating healing after injury.

Original languageEnglish (US)
Pages (from-to)253-273
Number of pages21
JournalAnnual review of physiology
Volume58
DOIs
StatePublished - Jan 1 1996

Keywords

  • ITF
  • mucin glycoprotein
  • pS2
  • spasmolytic polypeptide
  • wound healing

ASJC Scopus subject areas

  • Physiology

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